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NB100-304

53BP1 Antibody - BSA Free

(14 Reviews)

(712 Publications)

0.1 mg

NB100-304

Irradiated cochlear spiral ganglion cells, mouse, frozen section of fixed material. Image from verified customer review.

<b>Genetic Strategies Validation. </b>53BP1 was detected in immersion fixed HeLa cells (left) but was not detected in 53BP1 knockout Hela cells (right) using Rabbit Anti-human 53BP1 polyclonal antibody (Catalog #NB100-304) at 0.3 ug/mL for 3 hours at room temperature. Cells were stained using the NorthernLights™ 557-conjugated Anti-Rabbit IgG Secondary Antibody (red; Catalog # NL004) and counterstained with DAPI (blue). Specific staining was localized to nuclei.

Total protein from HeLa, A431, Neuro2A, and PC12 was separated on a 12% gel by SDS-PAGE, transferred to PVDF membrane and blocked in 5% non-fat milk in TBST. The membrane was probed with 1.0 ug/mL in 5% block buffer and detected with an anti-rabbit HRP secondary antibody using chemiluminescence. The observed molecular weight for these samples are ~250 kDa and the theoretical molecular weight is 214 kDa.

Human breast tumors stained with 53BP1 antibody. Image from verified customer review.

Detection of Human and Mouse 53BP1 by IHC. Sample: FFPE sections of human ovarian carcinoma (left) and mouse teratoma (right). Antibody: 53BP1 Antibody (Catalog #NB100-304) used at a dilution of 1:1000 (1ug/mL). Detection: DAB.

Human medulloblastoma (DAOY) and mouse astrocyte (C8D1A) cell lines were exposed for 48 hours to DMSO or 1ug/mL of the DNA damaging agent EPE. Cells were immunostained for 53BP1 (green). The nuclei were counterstained with DAPI (blue). Image from verified customer review.

An intracellular stain was performed on RH-30 cells with 53BP1 Antibody (Catalog #NB100-304AF647) (blue) and a matched isotype control (orange). Cells were fixed with 4% PFA and then permeabilized with 0.1% saponin. Cells were incubated in an antibody dilution of 5 ug/mL for 30 minutes at room temperature. Both antibodies were conjugated to Alexa Fluor 647.

Immunoprecipitation analysis lysates from HCC44 cells in 1% NP40. Image from verified customer review.

<b>Biological Strategies Validation. </b>Effect of RK-33 on radiation-induced DNA damage. A Immunofluorescence images showing 53BP1 and gamma-H2AX foci in A549 cells after 2-Gy radiation and A549 cells pre-treated with 6 uM RK-33, 12 h before radiation. Overlap of 53BP1 and gamma-H2AX is seen in the merged picture of the co-immunofluorescence staining. Scale bar is 2 um. Image collected and cropped by CiteAb from the following publication (//embomolmed.embopress.org/cgi/doi/10.15252/emmm.201404368) licensed under a CC-BY license.

Lamin A/C-53BP1 interaction is regulated in a DNA damage-dependent manner. U2OS/GFP-lamin A cells were pretreated with 10 um ATMi f for 1 h before exposure to IR (10 Gy, 1 h recovery). Cell extracts were then subjected to immunoprecipitation using GFP-Trap beads, and bound complexes were then analyzed by immunoblotting using 53BP1 and GFP antibodies. WCE represents 1% input. Image collected and cropped by CiteAb from the following publication (//doi.wiley.com/10.1111/acel.12258), licensed under a CC-BY license.

HeLa cells were fixed in 4% paraformaldehyde for 10 minutes and permeabilized in 0.5% Triton X-100 in PBS for 5 minutes. The cells were incubated with 53BP1 Antibody conjugated to DyLight 550 (NB100-304R) at 5 ug/ml for 1 hour at room temperature. Nuclei were counterstained with DAPI (Blue). Cells were imaged using a 40X objective.

An intracellular stain was performed on Ntera2 cells with 53BP1 Antibody NB100-304 (blue) and a matched isotype control NBP2-24891 (orange). Cells were fixed with 4% PFA and then permeabilized with 0.1% saponin. Cells were incubated in an antibody dilution of 1.0 ug/mL for 30 minutes at room temperature, followed by Rabbit IgG (H+L) Cross-Adsorbed Secondary Antibody, Dylight 550 (SA5-10033, Thermo Fisher).

Whole cell lysate from U2OS or 293T cells. Bands indicate an observed molecular weight of ~220 kDa and the theoretical molecular weight is 214 kDa.

<b>Biological Strategies Validation. </b>Upper Panel: 53BP1 foci in proliferating MEFs. Lower Panel: 53BP1 foci in proliferating MEFs exposed to 10 Gy of IR.

Embryonic Fibroblast cells pre-extraction for 5 mins with CSK buffer. Fixed with 4% PFA and 75% Ethanol. Primary Antibody at 1:1000. Secondary Antibody at 1:1000. Image from verified customer review.

<b>Biological Strategies Validation. </b>Upper Panel: Control untreated cells. Lower Panel: Cells exposed to irradiation (10 Gy) and probed for 53BP1 foci. Cells were grown on coverslips, fixed with 4% paraformaldehyde, methanol permeabilized, blocked for 1 h, RT. Incubated with primary antibody (1:200) overnight, washed 3x with PBS, probed with tubulin (Alexa Fluor 594) antibody for 2 h, RT. Washed 3x with PBS, mounted on slides using prolong gold, imaged using Nikon confocal microscope (100x oil). Image from verified customer review.

<b>Genetic Strategies Validation. </b>MUS81 inhibition in BRCA2-deficient cells causes accumulation of 53BP1 nuclear bodies and G1 arrest. H1299 cells carrying a DOX-inducible BRCA2 shRNA were transfected with control or MUS81 siRNAs. Representative images of cells processed 72 h later for immunostaining with 53BP1 Antibody (green) and anti-cyclin A (red) antibodies. DNA was counterstained with DAPI. Scale bar, 10 um. Image collected and cropped by CiteAb from the following publication (//www.nature.com/doifinder/10.1038/ncomms15983), licensed under a CC-BY license.

<b>Biological Strategies Validation. </b>Pot1a prevents DDR in HSCs. Telomeric DDR in 8 week-old LSK cells upon Pot1a knockdown. Immunocytochemical staining of TRF1 (green). Foci co-stained with TRF1 and 53BP1 were identified as TIFs. Nuclei were stained with TOTO3 (blue). Scale bar, 2 um. Image collected and cropped by CiteAb from the following publication (//www.nature.com/articles/s41467-017-00935-4), licensed under a CC-BY license.

Lamin A/C-53BP1 interaction is regulated in a DNA damage-dependent manner. U2OS cells were transfected with siCTRL or siLMNA and subjected to laser micro-irradiation, fixed 15 min later and then processed for immunofluorescence with gamma-H2AX and 53BP1 antibodies. Scale bar, 10 um. Image collected and cropped by CiteAb from the following publication (//doi.wiley.com/10.1111/acel.12258), licensed under a CC-BY license.

Ntera2 cells were fixed in 4% paraformaldehyde for 10 minutes and permeabilized in 0.5% Triton X-100 in PBS for 5 minutes. The cells were incubated with anti-53BP1 Antibody NB100-304 at 2 ug/ml overnight at 4C and detected with an anti-rabbit Dylight 488 (Green) at a 1:1000 dilution for 60 minutes. Alpha tubulin (DM1A) NB100-690 was used as a co-stain at a 1:1000 dilution and detected with an anti-mouse Dylight 550 (Red) at a 1:1000 dilution. Nuclei were counterstained with DAPI (Blue). Cells were imaged using a 100X objective and digitally deconvolved.

NIH3T3 cells were fixed in 4% paraformaldehyde for 10 minutes and permeabilized in 0.5% Triton X-100 in PBS for 5 minutes. The cells were incubated with anti-53BP1 Antibody NB100-304 at 2 ug/ml overnight at 4C and detected with an anti-rabbit Dylight 488 (Green) at a 1:1000 dilution for 60 minutes. Alpha tubulin (DM1A) NB100-690 was used as a co-stain at a 1:1000 dilution and detected with an anti-mouse Dylight 550 (Red) at a 1:1000 dilution. Nuclei were counterstained with DAPI (Blue). Cells were imaged using a 100X objective and digitally deconvolved.

Staining of 53BP1 in human colon cancer using DAB with hematoxylin counterstain.

An intracellular stain was performed on A431 cells with 53BP1 Antibody (Catalog #NB100-304AF647) (blue) and a matched isotype control (orange). Cells were fixed with 4% PFA and then permeabilized with 0.1% saponin. Cells were incubated in an antibody dilution of 2.5 ug/mL for 30 minutes at room temperature. Both antibodies were conjugated to Alexa Fluor 647.

For 53BP1 staining, samples were incubated for 1 hour with 1:200 53BP1 primary antibody in PBS/BSA 1%, at room temperature. Green: 53BP Blue: DAPI. Image from verified customer review.

DYNLL1 is required for 53BP1-dependent p53 responses to Nutlin-3. a Immunoblot analysis of the MCF-7 cell lines used in (a) with anti-53BP1 or anti-RPA32 antibodies prior to N3 treatment. b Quantification of n = 3 independent experiments represented in (a), each performed in triplicate. Mean ± SD. c Indicated parental or stably complemented 53BP1-/- MCF-7 cell lines were incubated in the presence (11 days) or absence (7 days) of Nutlin-3 (4 µM)

Depletion of PNUTS and NPAT induces a global DDR.(A) Induction of telomere dysfunction–induced foci (TIF) upon candidate knockdown in HeLa cells from Fig 5. Depletion of TRF2 was used as a positive control. 53BP1 was detected by indirect IF and telomeres by FISH with a Cy3-[CCCTAA]3 probe. (B) Frequency distribution of the number of TIFs per cell from (A). n indicates the number of cells analyzed for each condition and red lines mark the mean.

HPV+ HNSCCs have decreased expression of NHEJ and HR proteins including DNA-Pk and BRCA2Cells were treated with mock or 4 Gy radiation, harvested and lysed at 15 minutes post-treatment, and analyzed by western blot for relative expression of indicated proteins. beta -actin was used as a loading control. Shown is a representative blot from 2 independent experiments.

LNCaP cells in culture were treated for 24 hrs with DMSO or ENZ, then irradiated with 0 or 1 Gy.Cell were fixed and immunostained for 53BP1 0.5, 1.5 and 24 hrs after irradiation. Immunofluorescent images were obtained by confocal microscopy. White bar = 20 microns. A) DMSO alone, B) ENZ alone, C) 1 Gy, D) ENZ + 1 Gy. White bar = 20 microns.

Representative immunohistochemistry staining for 53BP1 expression in pancreatic adenocarcinoma. (A) is high intensity of 53BP1 expression and (B) is low intensity of 53BP1 expression.

Absence of Roma Leads to Activation of the DNA Damage Response and Genomic Instability(A) Representative immunofluorescence analysis of RPA2-pT21, gammaH2AX, and 53BP1 foci in tissue sections from WT and Roma-/- glands at 10dL. The white arrow indicates nucleolar gammaH2AX. Scale bars, 10 um. The higher magnification panels on the right have been chosen to highlight the foci and are not zoomed images of the left panels. Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/27149840), licensed under a CC-BY licence.

Persistent DNA damage exists in ALT cells. (A) IF-FISH showing DNA damage response (53BP1) in ALT (VA13, U2OS, SAOS2, SKLU-1), telomerase positive (MCF7, A549), and human normal fibroblast cells (MRC5, BJ). Scale bar: 10 um. Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31115790), licensed under a CC-BY licence.

Persistence of repair foci at suboptimal pHe. (A) Left panel shows immunofluorescence detection of gammaH2AFX and 53BP1 following 24 h recovery from bleomycin treatment. Control, sample before damage induction. Colocalization is shown in white; PCC, Pearson correlation coefficient score. Right panel corresponding to gammaH2AFX foci/cell at 24 h and 48 h following recovery. Only foci larger than 10 pixels were counted. Experiments were performed in triplicate. Values are mean +/- SEM. *P 3 (c) gamma-H2AX or d 53BP1 foci per nucleus. n = 90 cells from three independent experiments. Mean +/- SEM; two-way ANOVA (gamma-H2AX: F = 35.77, DFn = 4, DFd = 20, p 10 foci was called positive and counted). DAPI was used for nuclear staining. Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/28489060), licensed under a CC-BY licence.

USP15 regulates homologous recombination (HR) and breast cancer response to poly-(ADP-ribose) polymerase (PARP) inhibitor. c) Non-homologous end-joining (NHEJ) efficiency in USP15-depleted cells were determined using the EJ5-GFP reporter assay, as described in the Methods section. CtIP or 53BP1 small interfering RNAs (siRNAs) were used as a positive control, respectively, in b, c. Data are shown as average of three independent experiments, presented as mean +/- SD, two-tailed Student's t test, *P < 0.01. Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/30874560), licensed under a CC-BY licence.

MRE11 poly(T)11/12 sequence variant has no apparent functional consequence on DNA damage detection and repair. (D) DNA repair foci was observed by immunofluorescence after 1.5 Gy IR followed by 1 h and 4 h recovery. Irradiation resulted in the formation of both MRE11 and 53BP1 foci in Daudi and Raji cells, whereas Jurkat failed to form MRE11 foci. Nuclei were counterstained with DAPI. Merged figure presents co-localization of MRE11 and 53BP1 foci visualized in yellow. Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/21637783), licensed under a CC-BY licence.

Phenotypic consequences of R325Q mutation. (D) DNA damage is increased in patients' B-LCLs as compared to control, with an accumulation of 53BP1 foci. Left: immunostainings of 53BP1 imaged by confocal microscopy, Right: quantification of 53BP1 foci number. Graph represents the average count obtained from two independent experiments (Mean +/- SEM). Total number of cells in control = 508; P2_E71K n = 315; P_R325Q n = 452; Sidak's multiple comparisons test, ****p < 0.0001. Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31787977), licensed under a CC-BY licence.

Bystander signaling evokes DNA damage foci formation in urothelial cancer and normal urothelial cells. (A) Schematic representation of experimental conditions including non-irradiated, uniformly-irradiated and shielding protocols where 50% of the slide was exposed and 50% shielded with MCP alloy. Cells were fixed and processed for 53BP1-immunofluorescence, one hour following irradiation. Micrographs of urothelial cancer T24 cells labelled with anti-53BP1 (green) to label nuclear DNA double stand break foci and DAPI to counterstain nuclei are shown for each experimental condition. Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/29228614), licensed under a CC-BY licence.

Cry2-/- cells accumulate damaged DNA.(A) Representative early passage (P3-4) primary wildtype (WT), Cry1-/-, Cry2-/-, and Cry1-/-;Cry2-/- adult ear fibroblasts stained with anti-53BP1 antibody (green) and DAPI (blue). Insets show enlarged view of indicated cells. Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/25756610), licensed under a CC-BY licence.

Chromatibody-driven DDR alteration. (B) RNF8-dependent H2A di-ubiquitylation. HT1080 cells were transfected with the indicated constructs for 24 h. Whole-cell extracts were analyzed with an anti-ubiquitinylated H2A antibody (UbH2A). Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/27206857), licensed under a CC-BY licence.

The susceptibility of human LECs to low-dose ionizing radiation. The human lens cell line FHL124 was exposed to low-dose IR up to 2.28 Gy. Exposed cells were then processed for both immunofluoresence microscopy (a) and immunoblotting (b) 1 h later. The signals obtained by immunoblotting were quantified and the mean from three independent experiments calculated and plotted (c) against IR dose. GAPDH was used as a loading control. Both gammaH2AX and RAD51 increased linearly with IR dose. Signals for other markers of DNA repair, 53BP1, MRE11 and TP53, remained unchanged as assessed by immunoblotting (b). By immunofluoresence microscopy (a), MRE11 and 53BP1 redistributed into nuclear foci, particularly at the 2.28 Gy level. TP53 remained uniformly distributed throughout the nuclear compartment, but excluded from nucleoli (a). As the levels of gammaH2AX and RAD51 increased after exposure to IR (c), so the number of nuclear foci also increased (a). Scale bar, 10 um. Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/25924630), licensed under a CC-BY licence.

General chromatin effects of Adeltarod and Adeltaroddeltahbs. (c) No co-localization between Adeltarod structures and 53BP1 in HeLa cells indicates that chromatin is not damaged by the structures. Image collected and cropped by CiteAb from the following publication (//www.mdpi.com/2073-4409/6/2/9), licensed under a CC-BY licence.

Specificity of antibodies for tryptophan 2,3-dioxygenase (TDO) by Western blot (A) and immunofluorescent staining (B). A: The total protein (20 μg) of the dentate gyrus, extracted from the wild-type (lanes 1 and 3) and Tdo-/- mice (lane 2), was subjected to 4% to 12% gradient sodium dodecyl sulfate polyacrylamide gel electrophoresis, and transferred to polyvinylidene difluoride membranes. TDO was detected as described in the Methods section. Note that a 45-kDa band was detected with the anti-TDO antibody. The positions of molecular weight markers are shown on the left. Lane 3: negative control without the primary antibody. beta -Tubulin is a positive control for the Western blot. B: The hippocampal sections of wild-type and Tdo-/- mice were stained with anti-TDO antibody. In sections of Tdo-/- mice, immunofluorescence signals were not detected in granule cells, interneurons (arrowhead), CA1, or CA3 cells, suggesting that the secondary antibody used in this study bound specifically to the primary antibody (mouse IgG). g, granule cell layer; h, hilus. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/20815922), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

$CO attenuates mitochondrial dysfunction-derived sterile inflammation through TFEB-mediated mitophagy and mitochondrial biogenesis.Mice were exposed to LPS/D-galactosamine (D-GalN) with or without CO (250 ppm, 2 h/day) pretreatment, the blood and liver samples were collected 2 h and 6 h (b–i) after LPS/D-GalN administration. a The levels of ALT and AST were determined. Data are shown as mean ± SEM (n = 5). ***P < 0.001. b Liver sections were stained with H&E for morphological evaluation. c The levels of serum IL-1 beta were measured by ELISA. Data are shown as mean ± SEM (n = 4). **P < 0.01. ***P < 0.001. d Cytosolic mtDNA amounts in liver tissues were measured by qRT-PCR. Data are shown as mean ± SEM (n = 4). *P < 0.05. e Cleaved caspase-1 in cell lysates isolated from liver tissues was analyzed by immunoblotting. f The level of nuclear TFEB in liver tissues was determined by immunoblotting. Lamin B served as the nuclear standard. g Mitochondrial fractionation in liver tissues was analyzed by immunoblotting using antibodies against PINK1, Parkin, and LC3B-II. COX IV was used as marker for mitochondrial fractions. h, i The levels of autophagy-related genes and lysosomal genes (h) or mitochondrial biogenesis-associated genes (i) expressed in liver tissues were analyzed by qRT-PCR. Data are shown as mean ± SEM (n = 4). *P < 0.05, **P < 0.01. ***P < 0.001. j A scheme for the mechanisms of attenuating LSP/D-GalN-induced liver failure by CO through maintaining the balance between mitophagy and mitochondrial biogenesis. CO/CORM inhibits complexes of the mitochondrial respiratory chain (1) and then induces mitochondrial ROS (mtROS) production (2). Increased mtROS leads to PERK activation in the mitochondria-associated membrane (MAM) (3). The phosphorylation of PERK by mtROS increases intracellular calcium concentration. The activation of calcineurin by increased [Ca2 + ]i causes dephosphorylation of TREB (4), followed by its translocation into the nucleus. The nuclear translocation of TFEB increases the expression of genes involved in mitophagy (5) and mitochondrial biogenesis (6) Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/30333475), licensed under a CC-BY license. Not internally tested by Novus Biologicals.$

Precision quantitative image analysis workflow for the characterization of functional ITH.(a) Representative areas with positive immunohistochemical (IHC) staining for HIF-1 alpha , HIF-2 alpha , phospho-mTOR S2448, phospho-S6RP S235/236 and Ki-67. Only nuclear HIF-1 alpha and HIF-2 alpha expression was included in the analysis. Scale bar, 100 μm. (b) Overview of the quantitative IHC analysis process using a representative image of a whole-slide scanned pT1M1 tumour after phospho-mTOR S2448 staining. The image was overlaid with a virtual grid consisting of 1 mm2 squares that defines the tumour regions to be analysed. Non-cancerous tissue was subtracted manually (dark grey) and a positive pixel count was performed on the corrected area. Positivity per square was expressed as percentage of positive pixels. If a square contained non-tumorous tissue, the positivity was normalized to the corrected square area. Computed values were depicted as a heat map. Coloured squares represent tumour, whereas open squares indicate completely non-tumorous areas. Squares defined as peripheral tumour zone are marked by a black line. Scale bar, 1 cm. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/27291893), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Reduction of HIF-1 alpha and HIF-2 alpha levels leads to differential effects on apoptosis in RCC10 cells. (A) RCC10 cells stably expressing wild-type VHLp30 or expressing a control shRNA targeting luciferase (Luc shRNA) or a pool of two shRNAs targeting either HIF-1 alpha or HIF-2 alpha were created. These cells were grown to confluence and lysed. Cell lysates were equally loaded and separated by SDS-PAGE. Western blots were performed for VHL, HIF-1 alpha , HIF-2 alpha , GLUT-1, and alpha -tubulin. (B) The RCC10 cell lines described in (A) were grown to confluence and treated with ultraviolet (UV) light and lysed one day later. Cell lysates were equally loaded and separated by SDS-PAGE. Western blots were performed for PARP, cleaved caspase-3, and alpha -tubulin. (C) The RCC10 cell lines described in (A) were glucose starved for 24 hours as described in Methods. Cell lysates were equally loaded and separated by SDS-PAGE. Western blots were performed for PARP, cleaved caspase-3, and alpha -tubulin. (D) The RCC10 cell lines described in (A) were serum starved for 2 days as described in Methods. Cell lysates were equally loaded and separated by SDS-PAGE. Western blots were performed for PARP, cleaved caspase-3, and alpha -tubulin. Similar results were seen with serum starvation for 4 and 6 days (data not shown). Image collected and cropped by CiteAb from the following open publication (//cancerci.biomedcentral.com/articles/10.1186/s12935-015-0175-3), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Expression of hypoxia-inducible factor (HIF) proteins after bilateral renal ischemia or sham ischemia. Immunoblots for HIF-1 alpha (A–C) and HIF-2 alpha (D–F) of tissue extracts from the cortex and outer and inner medulla of the left kidneys of rats 24 h and 5 days following recovery from either sham ischemia (○) or bilateral renal ischemia (●); n = 6 per group. G: typical image of the gel following electrophoresis. H: typical image of the nitrocellulose membrane following transfer. Values are expressed as medians (25th percentile, 75th percentile). Paired comparisons were performed using the Mann-Whitney U-test. Because paired comparisons were made at two time points, P values were conservatively adjusted using the Dunn-Sidak method with k = 2. PTr, PT, and PTr*T are the outcomes of two-way analysis of variance on ranking with the factors treatment (Tr) and time (T). AU, arbitrary unit; I1, 24 h after ischemia; I5, 5 days after ischemia; S1, 24 h after sham ischemia; S5, 5 days after sham ischemia. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/30110566), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Active DNA end processing in late micronuclei compartments. a: Detection and quantification of RPA32 phosphorylation (pSerine 33) and ssDNA by specific antibodies in MN compartments of OVCAR-8 cells 36 h after 2-Gy irradiation. Note the nuclear signals have reduced while those in MN were intense. n = 3 biological repeats. Error bars = s.d. **P < 0.01; ***P < 0.005 (t-test). b: Immunostaining and enumeration of phosphorylated NBS1-pSerine 343, BRCA1-pSerine 1524 and TP53-pSerine 15 in MN compartments. **P < 0.01; ***P < 0.005 (t-test). c: Representative images (Upper panel) and quantification of RPA signal in MN compartments (Lower left) or RPA foci in nuclei (lower right) of post-IR OVCAR-8 cells after indicated treatments. Pro-resection genes (MRE11, BRCA1 and WDR70) were knockdown by specific siRNA. Percentage of positive RPA32-pS33 MN population was calculated after 36 h of IR treatment Image collected and cropped by CiteAb from the following open publication (//bmccancer.biomedcentral.com/articles/10.1186/s12885-018-4347-0), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Curcumin Analogs Induce Apoptosis in Cancerous Cells by Several Pathways. (a) E6-1 (Jurkat), dominant negative FADD (dnFADD) Jurkat, and overexpressing BCL-2 Jurkat were treated for 48 hours then stained for Annexin V and PI (b) E6-1 cells were plated and treated with or without the broad spectrum caspase inhibitor ZVAD(oMe)-FMK for 48 hours. Cells were stained for Annexin V and PI. Results were obtained using image-based cytometry with the Y-axis representative of percent of cells positive for Annexin V (green), PI (red), Annexin V and PI (yellow), or negative for both Annexin V and PI (blue). Values are expressed as a mean ± SD from three independent experiments. (c) E6-1 cells were treated for 24 hours with or without the broad spectrum caspase inhibitor ZVAD(oMe)-FMK and the studied compounds, lysed and subjected to Western blot analysis. (d) NHF and NCM460 cells were treated for 48 hours and 72 hours respectively, lysed and subjected to Western blot analysis. Bands were visualized with a chemiluminescence reagent. Images are representative of three independent experiments. Statistical calculations were performed using Two-Way ANOVA multiple comparison. *p < 0.05 vs % viable of Control (DMSO); #p < 0.05 vs % viable cells for groups without Z-VAD(oMe)FMK. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/28439094), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

PEM induces apoptosis of NSCLC cells via YIPF2-TNFRSF10B axis.a, b A549 (a) and H1792 (b) cells were treated with PEM at 5.0 μM for the indicated times (0, 6, 12, 24, 36 and 48 h). Cell lysates were analyzed by Western blotting with antibodies against YIPF2, TNFRSF10B and ACTB. c A549 cells were treated with doxorubicin (DOX) at various concentrations (0–2.0 μM) for 18 h. Cell lysates were analyzed by Western blotting with antibodies against YIPF2, TNFRSF10B and ACTB. d Overexpression of YIPF2 in H1792 and H1299 cells in the presence or absence of PEM at 5.0 μM for 36 h. Cell lysates were analyzed by Western blotting with antibodies against YIPF2, TNFRSF10B and ACTB. e Knockdown of YIPF2 expression by YIPF2–1 siRNA in A549 and H1792 cells in the presence or absence of PEM at 5.0 μM for 36 h. Cell lysates were analyzed by Western blotting with antibodies against YIPF2, TNFRSF10B and ACTB. f Overexpression of YIPF2 in H1299 cells (left) or Knockdown of YIPF2 expression by YIPF2–1 siRNA in H1792 cells (right) in the presence or absence of PEM at 5.0 μM for 36 h. Cell lysates were analyzed by Western blotting with antibodies against YIPF2, TNFRSF10A and ACTB. g Three A549 cell lines (Ctrl, YIPF2, YIPF2 + siTNFRSF10B) in the presence or absence of PEM at 5.0 μM for 36 h. Cell lysates were analyzed by Western blotting with antibodies against YIPF2, TNFRSF10B, CASP8, CASP3 and ACTB. h Three H1299 cell lines (Ctrl, siYIPF2–1, siYIPF2–1 + TNFRSF10B (short isoform)) in the presence or absence of PEM at 5.0 μM for 36 h. Cell lysates were analyzed by Western blotting with antibodies against YIPF2, TNFRSF10B, CASP8, CASP3 and ACTB. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/32303681), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Inhibition of CIP2A by siRNA impeded cell viability and DNA synthesis in HPV‐16E6–expressing cells. A, Elevated expression of CIP2A protein in 16E6‐expressing RPE1 cells. B, Western blot analysis of CIP2A and p53 proteins after transfection with scrambled siRNA (siCon) or CIP2A siRNA (siCIP2A) for 48 h. A representative of 3 independent experiments is shown. C, Cell viability assay of RPE1‐16E6 cells with CIP2A knockdown. D, Representative flow cytometry of BrdU staining profiles is shown. E, The mean and SD of BrdU‐positive cells from 3 experiments are summarized. **, P < .01. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/29893470), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Characterization of CIP2A expression in a panel of normal human melanocytes (NHM) and melanoma cell lines. (A) Immunoblot analysis and (B) quantification of protein expression levels of CIP2A (C) CIP2A mRNA expression measured by qRT-PCR. NHM1 line was used as calibrator. (D) Cytoplasmic and nuclear expression of CIP2A in normal melanocytes, primary and metastatic melanoma cell lines assessed by immunoblot analysis and (E) by immunohistochemical staining. CIP2A, cancerous inhibitor of protein phosphatase 2A. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/25663244), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

$TAZ induces Tfam protein expression at the translational level.a The expression of mitochondrial biogenic factors, including Tfam, Ppargc1a (Pgc1 alpha ), Nrf1, and Nrf2, was analysed using quantitative reverse transcription (qRT)-PCR in the gastrocnemius muscle of wild-type (WT) and muscle-specific TAZ knockout (mKO) mice; n = 6 for each condition (Tfam; *p = 0.0498, Nrf1; *p = 0.0467). b Protein was analysed via immunoblotting to detect TAZ and the indicated mitochondrial biogenic factors in (a). Alpha-tubulin was used as the loading control. c RNA was isolated from the control (Con) and TAZ knockdown (KD) C2C12 myotubes, and the expression of the indicated mitochondrial biogenic factors was analysed using qRT-PCR. The experiments were performed in triplicate (Tfam; *p = 0.04). d Protein from the Con and TAZ KD C2C12 myotubes was assessed via immunoblotting to detect TAZ and mitochondrial biogenic factors. Beta-actin was used as the loading control. e RNA was isolated from WT, TAZ-knockout (KO), and TAZ-rescued (T) mouse embryonic fibroblasts (MEF), and the indicated mitochondrial biogenic factors were analysed via qRT-PCR. f Protein from WT, KO, and T MEF was assessed via immunoblotting to detect TAZ and the indicated mitochondrial biogenic factors. Beta-actin was used as the loading control. g Protein was isolated from the gastrocnemius muscle of WT and mKO mice and analysed via immunoblotting to detect TAZ, YAP, and proteins involved in the translation of both phosphorylated and total forms. Alpha-tubulin was used as the loading control. h Protein obtained from the Con and TAZ KD C2C12 myotubes was assessed via immunoblotting to observe TAZ and proteins involved in translation. Beta-actin was used as the loading control. i Protein was isolated from WT, KO, and T MEF and analysed via immunoblotting to detect TAZ and proteins involved in translation. Vinculin was used as the loading control. j The polysome profile of cells described in panel i was evaluated continuously by measuring absorbance at 254 nm. The 40S, 60S, 80S, and polysome fractions are denoted by the corresponding peaks. k The distribution of Tfam, Atp5d, and Gapdh mRNA from cells described in (j) across a density gradient was analysed using reverse transcription (RT)-PCR. bp = base pairs. For a, b, g 8 to 10-week-old mice were used. Data are presented as mean ± SEM for (a), mean ± SD for (c, e). Statistical significance was analysed via two-sided t-test for (a) and one-sided t-test for (c). One-way ANOVA with Tukey’s multiple comparison test was used for (e). Representative data was shown and experiments were performed at least twice with similar results for (b, d, f–i, k). Source data are provided as a Source data file. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/35115527), licensed under a CC-BY license. Not internally tested by Novus Biologicals.$

Dynamics of the hypoxia-triggered decrease in MET phosphorylation and its reversal upon reoxygenation(A) MCF10A cells were incubated under normoxia or hypoxia for 1 h. They were then treated, under the same oxygen pressure, with 10 ng/mL HGF/SF for 5, 10, 20, 30, 60, 90 and 120 minutes. A control (Ctrl) without any HGF/SF stimulation was also performed. The same amount of protein was analyzed by western blotting with antibodies directed against: phosphorylated residues in the MET kinase domain, the MET kinase domain, the hypoxia marker HIF1a, phosphorylated Akt, Akt, Erk2, phosphorylated Erk, and actine. The positions of prestained molecular weight markers are indicated. Arrows indicate the positions of precursor and mature full-length MET. (B) MCF10A cells were incubated under hypoxia for 5, 10, 15 or 30 minutes. Another set of cells were incubated under hypoxia for 1 h and then returned to normoxia for 5, 10, 15 or 30 min (re-oxygenation). A control under normoxic (N) conditions was also included. The same amount of protein was analyzed by western blotting as previously described with the addition of GAB1 and its phosphorylated form. (C) MCF10A cells were placed under normoxic or hypoxic conditions for 1 h or hypoxia for 1 h and then normoxia for 10 minutes (reoxygenation). Cells were then treated at the indicated time with 10 ng/mL of HGF/SF. Cell lysates were incubated for AlphaScreen specific phospho-Erk and phospho-Akt quantitation. Error bars represent standard deviations (n = 3; ± SD). Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/29930749), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Downregulation of La autoantigen, hVAP-A, PSMA7, and NS5B leads to reduction in viral replication: overnight grown Huh-7.5 cells were transfected with La autoantigen, hVAP-A, and PSMA7 siRNAs for 48 h. Cells were then infected with the virus and again transfected with same siRNAs. After incubation total RNA was isolated and subjected to RT-PCR. NS5B siRNA was transfected once only after cells were infected. (a), (c), (e), and (g) represent RT-PCR results for target genes and NS5B gene upon treatment with La autoantigen, hVAP-A, PSMA7, and NS5B siRNAs, respectively. Densitometric analysis of (a), (c), (e), and (g) images is expressed in percentage in (b), (d), (f), and (h), respectively. The data represent mean ± standard deviation. ∗P value < 0.05 versus control considered statistically significant. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/27446609), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

FUS does not bind VAPB or PTPIP51 in immunoprecipitation assays from transfected HEK293 cellsCells were transfected as indicated with control vector (CTRL), HA‐FUS + CTRL, myc‐VAPB + CTRL, or myc‐VAPB + either HA‐FUS, HA‐FUSR521C or HA‐FUSR518K. VAPB was immunoprecipitated via the myc‐tag and the samples probed on immunoblots for VAPB using rabbit VAPB antibody and for co‐immunoprecipitating FUS via the HA tag. Input VAPB and FUS were detected using myc and HA antibodies.Cells were transfected as indicated with control vector (CTRL), HA‐FUS + CTRL, HA‐PTPIP51 + CTRL or HA‐PTPIP51 + either HA‐FUS, HA‐FUSR521C or HA‐FUSR518K. PTPIP51 was immunoprecipitated using rat anti‐PTPIP51 and the samples probed for PTPIP51 using rabbit anti‐HA antibody and for co‐immunoprecipitating FUS using rabbit FUS antibody. Input PTPIP51 and FUS were detected using PTPIP51 and EGFP antibodies, respectively. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/27418313), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

APCDD1 is co-regulated by MEIS1 and EWS-FLI1 and mediates the oncogenic role of MEIS1. (A, B) Silencing of (A) MEIS1 or (B) EWS-FLI1 downregulated expression of both APCDD1 mRNA and protein. Error bars represent mean ± SD of three replicates (**P < 0.01, ***P < 0.001). (C, D) APCDD1 knockdown potently (C) inhibited cell proliferation and (D) decreased colony formation. Error bars represent mean ± SD of three replicates (*P < 0.05, **P < 0.01, ***P < 0.001). (E) A673 and SKNMC cells stably expressing shMEIS1 were transiently transfected with plasmid encoding APCDD1, and subjected to immunoblotting and MTT assays. Bars represent mean ± SD of three replicates (**P < 0.01). (F) Proposed model showing that MEIS1 and EWS-FLI1 co-operatively activate APCDD1 transcription, thereby promoting the malignant phenotype of Ewing sarcoma cells. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/30496486), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Pharmacologic inhibition of ATM rescues oxidative stress-induced senescence by suppressing ATM- and NEMO-mediated NF-kappa B activation. (A) Representative images of primary WT and Ercc1-/- MEFs were induced to undergo senescence by serial passaging at 20% oxygen. At passage 5, MEFs were grown in the presence or absence of KU-55933 (10 μM) for 72 hrs. Senescence was determined by SA-beta gal staining. Images were obtained at the magnification of 10x. (B) Quantitation of the percent SA-beta gal positive cells. Graph represents the mean +/- s.e.m. of three independent experiments. Student’s t-test, ***p <0.001, ****p <0.0001. (C) Passage 5 Ercc1-/- MEFs treated with vehicle or KU-55933 (10 μM) for 72 hours were collected and levels of p21 and p16INK4a were determined by western blotting. (D) Passage 5 Ercc1-/- MEFs were treated with KU-55933 (10 μM) for 72 hours and whole cell lysate (CL) and nuclear extracts (NE) were analyzed by immunoblotting for expression of proteins involved in the DNA damage response. (E) Whole cell lysate (CL) and nuclear extract (NE) were extracted from Ercc1-/- MEFs treated with 10 μM of KU-55933 for analysis of nuclear NEMO and p65. GAPDH was used as a loading control of total proteins and LaminA/C as a loading control of nuclear protein. (F) Passage 5 WT and Ercc1-/- MEFs transfected with a NF-kappa B-luciferase reporter construct were cultured in the presence or absence of KU-55933 (10 μM) and were collected for luciferase assays after 72 hours. (G) qRT-PCR analysis of mRNA expression in passage 5 WT and Ercc1-/- MEFs treated with or without of KU-55933 (10 μM) for 72 hrs. P values were determined using a Student’s t-test. *p<0.05, **p<0.01, ***p <0.001. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/32201398), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Inhibition of splicing downregulates repair factors at both the mRNA and protein levels. (a) U2OS cells were treated with pladienolide B for 2, 6 and 16 h and irradiated (6 Gy, 1 h recovery) 1 h prior to termination of the treatment. The levels of the indicated mRNAs were measured through qPCR analysis. The change is relative to the DMSO control and two reference genes (18S rRNA and beta -actin). Means±S.D. are shown, n=3. (b) qPCR analysis of the levels mRNA and pre-mRNA for RNF8 and RAD51 in U2OS cells treated with pladienolide B or isoginkgetin for 2, 6 or 16 h and irradiated (6 Gy, 1 h recovery) 1 h prior to termination of this treatment. The change is expressed relative to the DMSO control value and the levels of mRNA for two reference genes (18S rRNA and beta -actin). Means±S.D. are shown, n=3. The arrows indicate the positioning of the PCR primers used and their sequences are shown in Supplementary Table S1. (c) Western blotting following pladienolide B treatment of U2OS cells as described in (a). beta -Actin was used as a loading control. Densitometric quantification of each protein is shown in Supplementary Figure S2B. The three MDC1 bands correspond to the unphosphorylated, phosphorylated and hyperphosphorylated forms of full-length MDC1 Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/27315300), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

LAIR-1 inhibits Glut1-related glucose uptake in OS cells. a Heatmap showing the levels of differentially expressed mRNAs. b Top 20 KEGG pathway annotation categories for target gene functions of predicted mRNAs. c Selected significantly differentially expressed mRNA-related to EMT in RNA-seq data between two groups, ***P < 0.001. d qPCR validation of differentially expressed EMT-related genes in LV-NC and LV-LAIR-1-overexpressing OS cells, **P < 0.01. e Glut1 expression analyzed by western blotting. f Immunofluorescence staining of Glut1 in the LV-LAIR-1-overexpressing OS cells. Scale bar = 50 μm. Data were obtained from at least two independent experiments. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/32563267), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Lysyl Oxidase (LOX) expression in malignant and non-malignant human prostate tissue.(A) Representative immunohistochemical staining of LOX (brown) in sections of non-malignant prostate tissue specimens (TINT epithelium and TINT stroma) from two prostate cancer patients (original magnifications x 200). Case A show weak epithelial staining (score 1) and Case B strong epithelial staining (score 3). (B) Consecutive sections from non-malignant prostate tissue stained with in situ hybridization or immunohistochemistry for LOX. Note that mRNA (brown dots) and protein (brown) expression in individual glands were related, in the stroma in contrast mRNA was generally low but protein often detected (original magnifications x200). (C) LOX mRNA expression in non-malignant prostate tissue (TINT) (n = 12), in primary prostate tumor tissue (n = 12), and in castration-resistant bone metastases (CRPC) (n = 30) using Illumina gene expression array. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/26501565), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Recruitment of 53BP1 and TRF2 to fs NIR laser-induced DNA lesions. (A) EGFP-53BP11220-1711 and TRF2-YFP cell lines were subjected to NIR laser microirradiation with the input power ranging from 20 mW to 155 mW (corresponding to ≈7 × 1010 W/cm2 to 5.41 × 1011 W/cm2 peak irradiance) as indicated. EGFP-53BP11220-1711 and TRF2-YFP recruitment was monitored for 15 min and 6 min p.i., respectively. The number of the cells with the recruitment and the number of cells examined are shown at the top of each histogram. Detailed microirradiation energy and irradiance calculations versus the laser input power (the power of the laser beam entering the microscope) are shown in Table 2. (B) Time course fluorescence measurement of the damage-site recruitment of EGFP-53BP11220-1711 and TRF2-YFP. PtK2 cells stably expressing EGFP-53BP11220-1711 or TRF2-YFP were damaged with either low (60 mW input power with peak irradiance of ≈2.1 × 1011 W/cm2; upper panel) or high (100 mW input power with peak irradiance of 3.49 × 1011 W/cm2; lower panel) dose of NIR laser microirradiation as indicated. For EGFP-53BP11220-1711, four and three cells were followed for 30 min for 60 mW and 100 mW damage, respectively. For TRF2-YFP, four cells each were followed for 4 min. The fluorescent intensity at the damage site was divided by that in the nucleoplasm and was subtracted by one for normalization. (C) Similar experiments as in (B) were performed following EGFP-53BP11220-1711 recruitment, and live fluorescent images of one representative cell each at indicated p.i. time points are shown. Time 0:00 refers to pre-laser condition. The irradiation site is indicated by a black line at time 0:00 and white arrowheads. Consistent results were obtained with 12 and 8 cells examined for the low (60 mW) and high (100 mW) irradiation condition, respectively. Scale bar = 10 μm. (D) Similar experiments as in (C) for TRF2-YFP. Consistent results were obtained with 11 and 12 cells examined for the low (60 mW) and high (100 mW) irradiation condition, respectively. Scale bar = 10 μm. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/26424850), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Reactivity:

Hu, Mu, Rt, Bt, Bv, Ca, Fi, Gt, Pm, Po, Pm, Fe, Pm-Or, Rb, Sh

Species Glossary

Reactivity: Hu, Mu, Rt, Bt, Bv, Ca, Fi, Gt, Pm, Po, Pm, Fe, Pm-Or, Rb, Sh

Applications:

, , , , , , , , , ,

Applications: , , , , , , , , , ,

Host:

Rabbit Polyclonal

Host: Rabbit Polyclonal

Sizes:

Sample Size Available

Sizes: Sample Size Available

Conjugate:

Unconjugated

Available Conjugates:

Validated by:

Validated by:

Conjugate	Catalog #	Availability	Size	Price
Alexa Fluor 350	NB100-304AF350
Alexa Fluor 405	NB100-304AF405
Alexa Fluor 488	NB100-304AF488
Alexa Fluor 532	NB100-304AF532
Alexa Fluor 594	NB100-304AF594
Alexa Fluor 647	NB100-304AF647
Alexa Fluor 700	NB100-304AF700
Alexa Fluor 750	NB100-304AF750
Allophycocyanin	NB100-304APC
Allophycocyanin/Cy7	NB100-304APCCY7
Biotin	NB100-304B
DyLight 350	NB100-304UV
DyLight 405	NB100-304V
DyLight 488	NB100-304G
DyLight 550	NB100-304R
DyLight 594	NB100-304DL594
DyLight 650	NB100-304C
DyLight 680	NB100-304FR
DyLight 755	NB100-304IR
FITC	NB100-304F
HRP	NB100-304H
Janelia Fluor 549	NB100-304JF549
Janelia Fluor 646	NB100-304JF646
PE	NB100-304PE
PE/Atto594	NB100-304PEATT594
PE/Cy5.5	NB100-304PECY55
PE/Cy7	NB100-304PECY7
PerCP	NB100-304PCP
mFluor Violet 450 SE	NB100-304MFV450
mFluor Violet 500 SE	NB100-304MFV500
mFluor Violet 610 SE	NB100-304MFV610

Available Formulations

Formulation	Catalog #	Availability	Price
BSA Free	NB100-304SS

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AB-108-C

Goat IgG Isotype Control [Unconjugated]

(2 Reviews)

(615 Publications)

1 mg

AB-108-C

SH-SY5Y human neuroblastoma cell line was stained with Goat Anti-Human/Mouse/RatEphrin-B2 Antigen Affinity-purified Polyclonal Antibody (Catalog #AF496,filled histogram) or Normal Goat IgG Isotype Control Antibody(Catalog # AB-108-C, open histogram), followed by Phycoerythrin-conjugatedAnti-Goat IgG Secondary Antibody (Catalog #F0107).

Decreased macrophage recruitment correlates with decreased angiogenesis.A) Quantification of BrdU incorporation demonstrates that decreased macrophage infiltration does not significantly correlate with a change in epithelial cell proliferation (N.S. = not significant). B) Quantification of VWF staining reveals decreased blood vessels associated with epithelial structures in mammary glands from mice treated with B/B and anti-CX3CR1 blocking antibody compared with mice treated with B/B and IgG control antibody. *p<0.05. C, D) Representative images of VWF stained mammary glands from mice treated with B/B and either control IgG antibody (C) or anti-CX3CR1 (D). Green = VWF staining, blue = DAPI. Arrows indicate VWF-positive structures. Scale bars represent 50 µM. Results in each figure panel are representative of a minimum of three different mice for each treatment group and genotype. Image collected and cropped by CiteAb from the following open publication (//dx.plos.org/10.1371/journal.pone.0045877), licensed under a CC-BY license. Not internally tested by R&D Systems.

iFGFR1 activation in vivo promotes recruitment of CX3CR1-positive macrophages.MMTV-iFGFR1 transgenic mice were treated with B/B in order to analyze the population of macrophages that are recruited to the mammary epithelium during early stages of iFGFR1-induced mammary tumorigenesis. A) MMTV-iFGFR1 mice treated with B/B demonstrated an increase in macrophage recruitment after 10 days as indicated by an increased in the number of F4/80 positive cells. MMTV-iFGFR1 mice treated with anti-CX3CR1 in conjunction with B/B demonstrated a reduction in macrophage recruitment at 10 days indicating that iFGFR1 activation is responsible for recruiting a subset of macrophages that express CX3CR1. ***p<0.0001. Error bars represent SEM. B) Representative image of macrophages associated with budding epithelial structures in mammary glands from mice treated with control IgG antibody. C) Representative image of macrophages associated with budding epithelial structures in mammary glands from mice treated with anti-CX3CR1. Red = F4/80 staining, blue = DAPI. Scale bars represent 50 µM. Results in each figure panel are representative of a minimum of three different mice for each treatment group and genotype. Image collected and cropped by CiteAb from the following open publication (//dx.plos.org/10.1371/journal.pone.0045877), licensed under a CC-BY license. Not internally tested by R&D Systems.

Reactivity:

Gt

Species Glossary

Reactivity: Gt

Applications:

Applications:

Host:

Goat Polyclonal

Host: Goat Polyclonal

Conjugate:

Unconjugated

Available Conjugates:

Conjugate	Catalog #	Availability	Size	Price
Alexa Fluor 488	IC108G
Alexa Fluor 647	IC108R
Alexa Fluor 700	IC108N
Allophycocyanin	IC108A
Biotin	BAF108
Fluorescein	IC108F
PerCP (Peridinin-chlorophyll Protein Complex)	IC108C
Phycoerythrin	IC108P

Available Formulations

Formulation	Catalog #	Availability	Price
Carrier Free	IC108A
Carrier Free	IC108C
Carrier Free	IC108F
Carrier Free	IC108G
Carrier Free	IC108N
Carrier Free	IC108P
Carrier Free	IC108R

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NB100-479

HIF-1 alpha Antibody - BSA Free

(28 Reviews)

(497 Publications)

0.1 ml

NB100-479

ChIP-qPCR assay of HIF-1 binding to hypoxia response element (HRE) of the PKM2 gene in human MDA-MB-231 breast cancer cells treated with vehicle or DMOG (HIF inducer) for 8 hours. Negative control: immunoprecipitation was performed with IgG. Image courtesy of Gregg Semenza, Johns Hopkins University School of Medicine.

<b>Biological Strategies Validation. </b>Normoxic pre-treatment sensitizes glioma cells to radiation after graded chronic hypoxic (GCH) exposure. The results of anchorage-independent colony forming assays are shown for U87, U87-luc, GL261 glioma cells and 0308 GSCs after 5 Gy radiation exposure under varying O2 conditions. For easier comparisons among cell types, raw values are expressed as a % of the cell type's negative (non-irradiated) control and the means & SEMs are plotted. Each result represents at least 3 independent samples, plated in triplicate. Holm-Sidak comparisons for multiple groups were used for statistical comparisons of raw values (*p0.05. (d) IDH1R132H expression diminishes DEPTOR levels. Flag-IDH1R132H was introduced in p53−/− MEFs by retroviral transduction and whole-cell lysates immunoblotted. (e) Inhibition of endogenous mutated IDH1R132C decreases mTOR activity in a KDM4A-dependent manner. HT1080 cells were transduced with lentivirus expressing sh_KDM4A.3 or sh_Control. The cells were treated with 3 μM AGI-5198 twice every day for 5 days and whole-cell lysates blotted for markers of mTOR activation. (f) Expression of mutant IDH1 in NHA-hTERT increases mTOR signalling. IDH1WT-Flag or IDH1R132H genes were introduced in astrocytes through retroviral infection and cell lysates were blotted for mTORC2 activation. (g) IDH1R132H overexpression increases 2HG production in astrocytes. Intracellular 2HG levels were normalized to glutamate. Asterisk denotes a statistical difference between IDH1R132H and empty vector cells, two-sided t-test P<0.0001 (graph represents three independent experiments). Error bars represent standard deviation. (h) Treatment of NHA-hTERT with octyl-2HG activates mTOR signalling. The cells were treated for 8 h with 1 mM octyl-2HG. The experiment shown is a representative of triplicates. (i) Non-canonical mTOR activation in IDH1/2WT and IDH1R132H human astrocytomas. Scale bar, 50 μm. Representative samples from IDH1/2WT (n=3) and IDH1R132H (n=3) human astrocytomas are shown. Image collected and cropped by CiteAb from the following open publication (//www.nature.com/articles/ncomms12700), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Comparison between primary tumor and mLNs of the mouse model. Expression of CA9 and GGT1 in mLNs was higher than that in the primary tumor at 1week after injection of cells. (A) CA9 and GGT1 expression of HT29 mLNs compared to primary tumor at 6 weeks or 1 week after injection of cells. (B) Tissue oxygen concentration (%) of rectal submucosa (SM) and nLNs (n = 3). Error bars represent SD. mNs: metastatic lymph nodes, nLNs: non metastatic lymph nodes. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/30542087), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

SPOC1 is recruited to I-SceI-induced DSBs where it colocalizes with 53BP1. (A) In situ immunofluorescence studies with U2OS19 ptight13 GFP-LacR cells with a stably integrated I-SceI cleavage site flanked by lac operator repeats reveals localization of the GFP-lac repressor protein (GFP-LacR) at the lac-operator DNA sequences in the nucleus before (−I-SceI) and 16 h after I-SceI-induced (+ I-SceI) DSB. In contrast, SPOC1 (white) and 53BP1 (red) are distributed throughout the nucleus in the absence of I-Scel, and partially colocalized in naturally occurring repair foci. After I-SceI cleavage to generate DSBs, SPOC1 and 53BP1 colocalize at distinct foci, including the cleaved DNA adjacent to DNA-bound GFP-LacR. Proteins were visualized by immunostaining and confocal microscopy. Scale bars = 10 μm. (B) Quantitative analysis of SPOC1 recruitment to the 53BP1 and GFP-LacR positive lacO array before and 16 h after I-SceI induction. (C) Monitoring of the kinetics of SPOC1 and 53BP1 recruitment to DSBs between 0 and 24 h post-I-SceI induction. (D) Quantifying ATM kinase inhibitor-mediated effects on recruitment of SPOC1 and 53BP1 to DSBs as evident 16 h after I-SceI-induced cleavage. (E) SPOC1 and 53BP1 colocalize at a large discrete endogenous repair focus as observed in some non-irradiated U2OS cells by immunostaining. Scale bar = 10µm. Image collected and cropped by CiteAb from the following open publication (//academic.oup.com/nar/article-lookup/doi/10.1093/nar/gks868), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Hif1 alpha expression in neonatal and adult testis.(A) Section of testis from 5-day old (P5) male new born pups showing Hif1 alpha expression in MVH+ gonocytes within the seminiferous tubules (top) and negative control images without primary antibodies (bottom). Scale bar: 50μm. (B) Western blot analysis of Hif1 alpha expression in P5 testes (left) compared to extract of the adult brain sub-ventricular zone (SVZ) (right). Loading control ( beta -Actin) is shown below. (C) Section of adult (3 month old) testis showing Hif1 alpha expression in spermatogonia. Scale bar: 30μm. (D) Western blot analysis of whole adult testis. HEK293 cells treated with DFX were used as a positive control and intestinal tissue was used as a negative control. Loading control ( beta -Actin) is shown below. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/27148974), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Subcellular localization of mPARM-1 and hPARM-1 (full-length and mutant proteins). (a) NIH/3T3 cells, transiently transfected with GFP-tagged mParm-1 or hParm-1 constructs were visualized using confocal microscopy. (b) For the Golgi co-localization, transfected NIH/3T3 cells were fixed and stained with Bodipy ceramide marker. For late and early endosomes co-localization, fixed cells were labeled with (c) anti-Rab5 (early endosomes (1:100, Cell signaling)) and (d) anti-Rab7 (late endosomes (1:100, Cell signaling)) antibodies, respectively. Jurkat T cells, transiently transfected with hParm-1-GFP proteins were visualized (e) without fixation or (f) following fixation and staining with CellMask plasma membrane labeling. NIH/3T3 cells were transiently transfected with (g) ∆EC-GFP, (h) ∆SP-GFP, (i) EC-GFP, (j) ∆TM-GFP and (k) ∆CT-GFP constructs of hPARM-1 and visualized using confocal microscopy. (l) hPARM-1-GFP co-localizes with microtubules. NIH/3T3 cells transfected with hParm-1-GFP construct were fixed and stained with anti-alpha -tubulin (1/2000, Sigma) antibody. Arrows indicate co-localized hPARM-1-GFP vesicles and microtubules. NIH/3T3 cells transiently expressing (m) hPARM-1-GFP or (n) ∆CT-GFP were fixed, immunostained for caveolin-1 (1:100, Novus Biologicals), and examined by confocal fluorescence microscopy. For hPARM-1-GFP-caveolin-1 co-localization, cells that clearly demonstrated cell membrane PARM-1 localization were chosen. All co-localizations were observed following merging images of GFP-tagged proteins with those of Golgi, endosomes, plasma membrane, alpha -tubulin or caveolin-1 labeling. Cells were imaged with a laser-scanning confocal microscope (Bio-Rad MRC-1024 ES) mounted on a Nikon TE-300 using a Plan Apochromat 60x (NA 1.40) oil objective (Nikon), digitally acquired using Laser Sharp software Version 3.2 (Bio-Rad). For live cell imaging, signals were collected at a rate of 2 seconds. Images were analyzed using NIH ImageJ Version 1.42l software. Data are representative of 3 independent experiments. Image collected and cropped by CiteAb from the following open publication (//molecular-cancer.biomedcentral.com/articles/10.1186/1476-4598-12-84), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Inhibition of Cdk1 and Cdk2 by CIP2A knockdown in cervical cancer SiHa cells caused G1 arrest. A, Western blot analysis of 16E6, p53 and CIP2A after HPV‐16E6 knockdown in cervical cancer SiHa cells. B, Protein expression of CIP2A, B‐Myb, Cdk1 and Cdk2 in SiHa cells after CIP2A knockdown. Data from a representative of 3 experiments are shown. C, Flow cytometric analysis of SiHa cells with CIP2A knockdown treated with PBS or bleomycin. A representative flow cytometry of 3 independent experiments is shown. D, Quantification of percentages G1 phase cells. Data from 3 experiments are summarized. *, P < .05 Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/29893470), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

$Immunoblot analysis of livers from control and L-Chrebp−/− mice subjected to fasting and refeeding with a high-sucrose diet. Littermate control and L-Chrebp−/− mice (same as those described in supplemental Tables S2A and S2B) were subjected to fasting and refeeding. The nonfasted (N) groups were fed chow diet ad libitum. The fasted (F) group was fasted 12 h, and the refed (R) group was fasted for 12 h and then refed with 60% (w/w) high-sucrose diet for 12 h prior to study. Liver whole-cell lysates and membrane fractions were prepared individually, and equal amounts of protein from each mouse of the same group (four per group) were pooled. Aliquots (40 μg for whole-cell lysates and 30 μg for membrane fractions) of the pooled protein were subjected to SDS-PAGE and immunoblot analysis. Immunoblot analysis of Insig-1 and Insig-2 were carried out using membrane fractions. Whole-cell lysates were used to detect other proteins. The precursor and nuclear forms of SREBPs are denoted as P and N, respectively. Calnexin was used as loading control. Image collected and cropped by CiteAb from the following open publication (//linkinghub.elsevier.com/retrieve/pii/S0022227520331369), licensed under a CC-BY license. Not internally tested by Novus Biologicals.$

Reactivity:

Hu, Mu, Rt, Po, Ca, Fi, Gt, Ha, Pm, Rb, Ze

Species Glossary

Reactivity: Hu, Mu, Rt, Po, Ca, Fi, Gt, Ha, Pm, Rb, Ze

Applications:

, , , , , , , ,

Applications: , , , , , , , ,

Host:

Rabbit Polyclonal

Host: Rabbit Polyclonal

Sizes:

Sample Size Available

Sizes: Sample Size Available

Conjugate:

Unconjugated

Available Conjugates:

Validated by:

Validated by:

Conjugate	Catalog #	Availability	Size	Price
Alexa Fluor 350	NB100-479AF350
Alexa Fluor 405	NB100-479AF405
Alexa Fluor 488	NB100-479AF488
Alexa Fluor 532	NB100-479AF532
Alexa Fluor 594	NB100-479AF594
Alexa Fluor 647	NB100-479AF647
Alexa Fluor 700	NB100-479AF700
Alexa Fluor 750	NB100-479AF750
Allophycocyanin	NB100-479APC
Allophycocyanin/Cy7	NB100-479APCCY7
Biotin	NB100-479B
DyLight 350	NB100-479UV
DyLight 405	NB100-479V
DyLight 488	NB100-479G
DyLight 550	NB100-479R
DyLight 594	NB100-479DL594
DyLight 650	NB100-479C
DyLight 680	NB100-479FR
DyLight 755	NB100-479IR
FITC	NB100-479F
HRP	NB100-479H
Janelia Fluor 549	NB100-479JF549
Janelia Fluor 646	NB100-479JF646
PE	NB100-479PE
PE/Atto594	NB100-479PEATT594
PE/Cy5.5	NB100-479PECY55
PE/Cy7	NB100-479PECY7
PerCP	NB100-479PCP
mFluor Violet 450 SE	NB100-479MFV450
mFluor Violet 500 SE	NB100-479MFV500
mFluor Violet 610 SE	NB100-479MFV610

Available Formulations

Formulation	Catalog #	Availability	Price
BSA Free	NB100-479SS

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NB100-2323

IRE1 alpha [p Ser724] Antibody - BSA Free

(9 Reviews)

(318 Publications)

0.1 ml

NB100-2323

P-Ire1a activation correlates with WFS1 cell expression. Cryosections of retina from 12 month old Wfs1+/+ and Wfs1-/- mouse were immunostained with anti-P-Ire1a antibody (red). DAPI was used for staining of cell nuclei (blue). RPE, retinal pigment epithelium; ONL, outer nuclear layer; INL, inner nuclear layer, RGC, retinal ganglion cells. Scale bars=50 um. Image collected and cropped by CiteAb from the following publication (//doi.org/10.1371/journal.pone.0097222) licensed under a CC-BY license.

Hepatic ER stress markers with cachexia progression. ER stress markers Bip, IRE1a, ATF6p50 and CHOP were examined in the liver of non, pre and severely cachectic mice. (n = 6-8 per group, p < 0.05) Dotted line indicates levels of Non-cachectic mice. Non = Non-Cachectic Apc Min/+ Sev = severely cachectic Apc Min/+; * denotes significantly different from Non-cachectic Apc Min/+ Image collected and cropped by CiteAb from the following publication (//doi.org/10.1371/journal.pone.0119888) licensed under a CC-BY license.

IRF-1 plays a central role in ER stress-mediated modulation of VCAM-1 expression by TGRL. HAEC were conditioned for 4 hr with TNFa (0.3 ng/ml) E: CHOP knockdown decreased TNFa-induced VCAM-1 expression. n=4. **P<0.01 vs. siCtrl+TNFa. Shown are representative blots from 3 independent experiments with similar results. Image collected and cropped by CiteAb from the following publication (//doi.org/10.1371/journal.pone.0078322) licensed under a CC-BY license.

Analysis using HRP conjugate of NB100-2323. Detection of phosphorylated IRE-1 alpha using NB100-2323. Lane 1: COS-7 untransfected Lane 2: COS-7 expressing wild-type IRE1 alpha Lane 3: COS-7 expressing kinase-dead IRE1 alpha. Theoretical molecular weight: 110 kDa.

<b>Biological Strategies Validation. </b>Analysis of anti-IRE1 alpha (pSer724) using Lot AN and AO of NB100-2323. HeLa cells were treated (+) or untreated (-) with 10 mM DTT for 60 min to activate the UPR. Total protein was separated on a 7.5% gel by SDS-PAGE, transferred to PVDF membrane and blocked in 5% BSA in TBST. The membrane was probed with 2.0 ug/ml antibody in 5% BSA, and detected with an anti-rabbit HRP secondary antibody using chemiluminescence. Theoretical molecular weight: 110 kDa.

Regulation of the unfolded protein response by KLF15. Western analysis of UPR activity in WT versus KLF15-/- primary hepatocytes. Hepatocytes were isolated from standard chow-fed 4-month-old male WT and KLF15 -/- mice. Two individual experiments were performed in triplicate; each lane indicates a technical replicate. Image collected and cropped by CiteAb from the following publication (//doi.org/10.1371/journal.pone.0077851) licensed under a CC-BY license.

HeLa cell lysate, 20 ug. Antibody at 1:1000, 1% skim milk in TBST, overnight incubation at 4C. WB image submitted by a verified customer review.

<b>Biological Strategies Validation. </b>Detection in Min6 cells which were treated with different concentrations of glucose for 3 hours prior to lysates preparation.

IRE1 (pS724) was detected in immersion fixed paraffin-embedded sections of human spleen using Rabbit Anti-Human IRE1 (pS724) polyclonal Antibody (Catalog # NB100-2323) at 1:300 for 1 hour at room temperature followed by incubation with the Anti-Rabbit IgG VisUCyte™ HRP Polymer Antibody (Catalog # VC003). Tissue was stained using DAB (brown) and counterstained with hematoxylin (blue). Specific staining was localized to the perinuclear cytoplasm in splenocytes.

Hepatic ER Stress.Representative hepatic western blots of BiP, phosphorylated (Ser51), total EIF2 alpha and phosphorylated:total EIF2 alpha , phosphorylated (Ser724), total IRE1 alpha and phosphorylated:total IRE1 alpha , and CHOP (n = 9). Diets not sharing a common letter differ significantly from one another (P≤.05).

Morphine suppressed 6-OHDA-induced ER stress through activation of UPR. (A,B) Morphine induced UPR in SH-SY5Y cells. Protein levels of GRP78, p-IRE1 alpha , IRE1 alpha , p-PERK, PERK, ATF6, CHOP and Tubulin in SH-SY5Y cells were analyzed (A) and quantified (B) by western blot. ∗P < 0.05, ∗∗P < 0.01, ∗∗∗P < 0.001 vs. control.

Effect of cancer on ER stress markers.Bip1, IRE-1, ATF-6 p50 and CHOP expression in the liver of non—cachectic ApcMin/+ mice (N = 6 per group), compared to healthy C57BL/6 mice. Dotted line on the western blot indicates two different sections of the same gel. Values are expressed as Mean ± SE. * denotes significantly different from the healthy C57BL/6 mice as analyzed by a pre—planned t—test. p < 0.05.

T helper cells upregulate the IRE1a-XBP1 pathway during activation. c) Naive T helper cells and in vitro differentiated Th2 lymphocytes were analyzed for IRE1a mRNA expression by qRT-PCR (left panel), protein expression by Western blot (middle panel), and phosphorylated IRE1a (P-IRE1a) by Western blot (right panel). The density of Western blot bands from five independent experiments of IRE1a and three independent experiments of phospho-IRE1a were measured and displayed on top of each Western blot panel. Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/30355343), licensed under a CC-BY licence.

IER3IP1 suppression decreases the UPR activation. (B) Effect of IER3IP1 suppression on the IRE1alpha arm of the UPR. 4 days after IER3IP1 KD in MIN6 cells, phosphorylation of IRE1alpha, Bip, sXBP-1 and uXBP-were determined by Western blot. The loaded proteins in the two

CETP inhibition reduces endoplasmic reticulum stress. HAECs transfected with CETP or control scrambled siRNA. (B) Phosphorylated and total IRE (n = 3, ns). Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/33430172), licensed under a CC-BY licence.

Apoptosis mediated by Arl6ip5 interference is regulated by Chop. (a) Immunoblotting was used to detect the protein level for p-IRE1alpha, IRE1, Chop, Arl6ip5 and beta-actin in the UAMS-32 cell with NC-siRNA or Arl6ip5-siRNA treatment for 72 h. Representative results were shown from three independent experiments. Image collected and cropped by CiteAb from the following publication (//www.nature.com/articles/cddis2014427), licensed under a CC-BY licence.

Activation of UPR signaling pathways after UIRI. e and f) The expression of p-IRE1 and t-IRE1 in mice kidneys were evaluated with western blotting and quantified. Data are expressed as means +/- SEM, n = 3 ~ 6 in each group. *P < 0.05, **P < 0.01, and ***P < 0.001, as compared with sham group Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/35765067), licensed under a CC-BY licence.

Effect of Insig-1 overexpression on nSREBP-1c and proteins related to ER stress pathway in INS-1 cells. INS-1 and INS-1-Insig-1 cells were stimulated with 11.2 mM and 25.0 mM glucose for 0, 24 and 72 h. A) nSREBP-1c and p-IRE1alpha pathway of ER stress related proteins were detected by Western blot. GAPDH was used as control for protein loading. Equal amount of proteins (50 ug) were loaded. Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/21843373), licensed under a CC-BY licence.

Protein expression of downstream markers of ER stress in islets from lean, obese and high-fat-diet-fed fZDF rats. Protein lysates from islets isolated from three age-matched fZDF rats (obese), HF-fZDF (HFD) rats and their heterozygous lean littermates (lean) were separated by SDS-PAGE and analysed by western blotting. As controls, lysates from the islets isolated from Wistar rats or MIN6 cells treated with 1 uM thapsigargin for 2 h or sorbitol for 1 h were run alongside. Proteins were detected using antisera against (a) Calreticulin, HYOU1, GRP78, p-IRE1alpha, p-eIF2alpha and CHOP and as protein loading control rpS6 and (b) p-JNK and total JNK1/2 as loading control. Western blots were quantified using Image-J software. Image collected and cropped by CiteAb from the following publication (//www.nature.com/articles/nutd201335), licensed under a CC-BY licence.

ABT-263 induces ER stress and activation of the unfolded protein response. c) Kinetic analysis of ER stress proteins in Mel270 cells treated with ABT-263 5 uM in the absence or presence of qVD-OPh 20 uM. HSP90 is used as a loading control. Representative western blots are shown. Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/32337074), licensed under a CC-BY licence.

$Localization of the WT and mutant Wrn proteins in different subcellular fractions. (C) Protein levels of GRP78, phosphorylated IREalpha, and beta-actin (top panels) and of total IREalpha, and beta-actin (bottom panels) in the spleen of three animals of each genotype. Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/26447695), licensed under a CC-BY licence.$

Glucocorticoids suppress NIX expression independent from PINK1-parkin pathway.a SH-SY5Y cells were incubated with cortisol for 12 h and mRNA expressions were analyzed by real-time PCR. n = 5. b, c Hippocampal neurons and SH-SY5Y cells were treated with corticosterone for 24 h and with cortisol for various time, respectively. Expression of NIX, PTEN-induced kinase 1 (PINK1), and BCL2 interacting protein 3 (BNIP3) were detected via western blot. n = 5. d, e Hippocampal neurons and SH-SY5Y cells were treated with corticosterone and cortisol, respectively, for 24 h. NIX (green), TOMM20 (red), and DAPI (nuclear counterstaining, blue) were visualized. Scale bars, 20 μm (magnification, ×1000). n = 5. f Nontargeting (NT) or PARK2 siRNA was transfected to SH-SY5Y cells for 24 prior to cortisol for 24 h. NIX was co-immunoprecipitated with parkin. Parkin levels in immunoprecipitated samples were quantified. n = 5. g, h Both hippocampal neurons and SH-SY5Y cells were transfected with mitochondria-targeted Keima (mt-Keima)-Red-Parkin for 24 h prior to corticosterone and cortisol for 24 h, respectively. Western blot was performed. n = 5. i–l Both hippocampal neurons and SH-SY5Y cells were pretreated with phorbol 12-myristate 13-acetate (PMA, 10 nM) for 30 min before corticosterone and cortisol for 24 h, respectively. i, j Hippocampal neurons and SH-SY5Y cells were transfected with mt-Keima at DIV 5 and 48 h prior to treatment, respectively. DAPI was used for nuclear counterstaining (blue). Ratio of red to sum of red and green was quantified. Scale bars, 20 μm (magnification, ×1000). n = 5. k, l TOMM20 levels were detected by western blot. n = 5. m SH-SY5Y cells were transfected with pcDNA3.1/c-eGFP or pcDNA3.1/NIX-c-eGFP vector for 24 h prior to cortisol for 24 h. TOMM20 levels were detected by western blot. n = 5. All blots and immunofluorescence images are representative. n = 5 from independent experiments with two technical replicates each. Quantitative data are presented as a mean ± S.E.M. The representative images were acquired by SRRF imaging. Two-sided unpaired student’s t test: Figs. 3a, b, d, e. Two-sided one-way ANOVA: Fig. 3c. Two-sided two-way ANOVA: Figs. 3f–m. ** indicates p < 0.01 versus control. ## indicates p < 0.01 versus corticosterone in hippocampal neurons and cortisol in SH-SY5Y. Data are provided as a Source data file. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/33473105), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Expression analysis of mouse Fchsd1 and Fchsd2 in different tissues.(A) Total RNA from postnatal day 5 mouse tissues was extracted and used as template for reverse transcription. PCR was performed using this cDNA as template. Upper panel, Fchsd1 mRNA is expressed more abundantly in nervous tissues. Middle panel, Fchsd2 mRNA is expressed ubiquitously in all tissues examined. Lower panel, beta -actin specific primers were used as the RT-PCR template control. (B) Total proteins of postnatal day 5 mouse cochlea and vestibula were extracted and separated by PAGE and detected with antibodies against FCHSD1(Novus), FCHSD2, or SNX9. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/23437151), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Phase contrast microscopy images of HFA and brain tumor cells and immunofluorescence images of cultured primary brain tumor cells, AA and HFA.HFA were derived from three different foetal brains. (A) 18-week foetus (10× magnification); (B) 19-week foetus, first week in culture (10× magnification); (C) 19-week foetus, day 5 in culture (20× magnification); (D) Primary GBM after 2 trypsinisations (20x); (E) Recurrent GBM (20x); (F) Secondary GBM after 3 trypsinisations (10x); (G) OII 14 days in culture (10x); (H) AII 13 days in culture (10x); (I) Negative control for NGS merged with DAPI; (J) Negative control for secondary antibodies merged with DAPI; (K) GBM cells derived from one patient – GFAP (DAKO) merged with DAPI and CD68 (zoomed: 2.4× magnification); (L) primary brain tumor cells from one patient (male, 40 years old) (passaged three times) - GFAP (Novocastra) merged with DAPI; (K and L) GFAP (green) was used as a GBM marker and CD68 (red) was used as a marker for microglia. (M) AA from one Female, 61 years old; (passaged twice) - GFAP (Novocastra) merged with DAPI; (N) AA from one male 40 years old; (passaged once) - GFAP (Sigma) merged with DAPI and CD68 (Abcam); (M and N) GFAP (green) was used as an astrocyte marker and CD68 (red) and CD11b (green) were used as markers for microglia; (O) HFA from one 17-week- old foetus (passaged once) - GFAP (Novocastra) merged with DAPI and CD11b (Novus); (P) HFA from an 18-week- old foetus (passaged once) - GFAP (DAKO) merged with DAPI and CD68 (zoomed: 2.1× magnification); (O and P) GFAP (green and red) was used as an astrocyte marker and CD68 (red) and CD11b (green) were used as markers for microglia. Nuclei indicated by DAPI (blue) in all images. Image collected and cropped by CiteAb from the following open publication (//dx.plos.org/10.1371/journal.pone.0112945), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Regulation of FOXC1 on TLR3/4 expression in mice subjected to myocardial ischaemia (MI). The siRNA against FOXC1 (si‐FOXC1) or FOXC1 adenovirus (Ad‐FOXC1) was injected into the left ventricle just after LAD ligation to generate FOXC1 knockdown (A) or FOXC1 overexpression (B), and the negative control (NC) siRNA and Ad‐GFP served as control, respectively. The mRNA (upper panel) and protein (middle and lower panel) levels of TLR3/4 were determined after 2 wk. Data are means ± SEM aP < .05, AP < .01 vs respective MI Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/31517441), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Analysis of protein levels of genes with increased transcription in hypoxia, IOX2 and VH032.HIF targets were increased in hypoxia, VH298 and FG-4592. 0.05% DMSO (vehicle control), 1% O2 (hypoxia), 100 µM VH298 and 50 µM FG-4592 were introduced to (A) HeLa or HFF for 24 hours and (B) HeLa for indicated time. Protein levels were analysed by immunoblotting using antibodies against indicated proteins, with beta -Actin as loading control. The blots shown are representative of three independent experiments. * indicates longer exposure. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/30801039), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Reactivity:

Hu, Mu, Rt, Po, Dr, Gt, Ma, Pm, Pm, Rb, SyHa

Species Glossary

Reactivity: Hu, Mu, Rt, Po, Dr, Gt, Ma, Pm, Pm, Rb, SyHa

Applications:

, , , , , , , ,

Applications: , , , , , , , ,

Host:

Rabbit Polyclonal

Host: Rabbit Polyclonal

Sizes:

Sample Size Available

Sizes: Sample Size Available

Conjugate:

Unconjugated

Available Conjugates:

Validated by:

Validated by:

Conjugate	Catalog #	Availability	Size	Price
Alexa Fluor 350	NB100-2323AF350
Alexa Fluor 405	NB100-2323AF405
Alexa Fluor 488	NB100-2323AF488
Alexa Fluor 532	NB100-2323AF532
Alexa Fluor 594	NB100-2323AF594
Alexa Fluor 647	NB100-2323AF647
Alexa Fluor 700	NB100-2323AF700
Alexa Fluor 750	NB100-2323AF750
Allophycocyanin	NB100-2323APC
Biotin	NB100-2323B
DyLight 350	NB100-2323UV
DyLight 405	NB100-2323V
DyLight 488	NB100-2323G
DyLight 550	NB100-2323R
DyLight 594	NB100-2323DL594
DyLight 650	NB100-2323C
DyLight 680	NB100-2323FR
DyLight 755	NB100-2323IR
FITC	NB100-2323F
HRP	NB100-2323H
Janelia Fluor 549	NB100-2323JF549
Janelia Fluor 646	NB100-2323JF646
PE	NB100-2323PE
PerCP	NB100-2323PCP
mFluor Violet 450 SE	NB100-2323MFV450
mFluor Violet 500 SE	NB100-2323MFV500
mFluor Violet 610 SE	NB100-2323MFV610

Available Formulations

Formulation	Catalog #	Availability	Price
BSA Free	NB100-2323SS

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(select up to 3 products from this page to compare)

NB100-449

HIF-1 alpha Antibody

(28 Reviews)

(286 Publications)

0.1 ml

NB100-449

Simple Western: HIF-1 alpha Antibody [NB100-449] - Simple Western lane view shows a specific band for HIF-1 alpha in 0.5 mg/ml of hypoxic HeLa lysate. This experiment was performed under reducing conditions using the 12-230 kDa separation system.

Immunohistochemistry: HIF-1 alpha Antibody [NB100-449] - Mouse Brain, Neurons 40X

Immunohistochemistry: HIF-1 alpha Antibody [NB100-449] - Detection of human HIF1-alpha by immunohistochemistry. Sample: FFPE section of renal cell carcinoma. Antibody: Affinity purified rabbit anti-HIF1-alpha antibody (NB110-58773). Detection: DAB

<b>Biological Strategies Validation. </b>Western Blot: HIF-1 alpha Antibody [NB100-449] - Detection of Human HIF-1 alpha by Western Blot and Immunoprecipitation. Samples: Whole cell lysate (5, 15 and 50 ug for WB; 1 mg for IP, 20% of IP loaded) from HeLa cells that were either treated with cobalt chloride (+; 200 uM) or mock treated (-). Antibodies: Affinity purified rabbit anti-HIF1 alpha antibody used for WB at 0.1 ug/mL(A) and 1 ug/mL (B) and used for IP at 3 ug/mg lysate. HIF-1 alpha was also immunoprecipitated by a previous lot of this antibody. Detection: Chemiluminescence with exposure times of 30 seconds (A) and 10 seconds (B).

Western Blot: HIF-1 alpha Antibody [NB100-449] - Blot showing the effect of hypoxia on the protein expression levels of the purine biosynthetic enzymes. HIF-1 alpha is stabilized in hypoxia as expected, and no significant increase in the purine enzymes was detected between normoxic (21% oxygen) and hypoxic (1% oxygen) growth conditions. The positions of molecular markers surrounding each band of interest are shown for each blot. ADSL (NBP2-03107), ATIC (NBP2-01941), FGAMS (NBP1-84691), GART (H00002618-M01), HIF-1a (NB100-449), PAICS (NBP2-02817), PPAT (NBP2-02056). Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/32439803/) licensed under a CC-BY license.

Immunocytochemistry/Immunofluorescence: HIF-1 alpha Antibody [NB100-449] - Murine primary bone marrow derived macrophages stained with HIF1-alpha antibody (red). Nuclei were counterstained with DAPI (blue). Image from verified customer review.

Immunohistochemistry-Paraffin: HIF-1 alpha Antibody [NB100-449] - Analysis of microvascular density and HIF-1alpha activity. Low, homogenous expression of HIF-1alpha was detected in the tumors of NNK treated mice (40X, scale bar = 25 um). Image collected and cropped by CiteAb from the following publication (//molecular-cancer.biomedcentral.com/articles/10.1186/1476-4598-11-4), licensed under a CC-BY license.

Flow Cytometry: HIF-1 alpha Antibody [NB100-449] - HeLa cells were treated for 15 hrs with 200 uM CoCl2, fixed in PFA, and permeabilized in 90% MeOH. 1 X 10^6 cells were stained with 0.125 ug anti-HIF-1 alpha and secondary FITC-conjugated goat anti-rabbit (in a 150 uL reaction). Black: treated, anti-KLH control IgG; Red: untreated, anti-HIF-1 alpha; Blue: treated, anti-HIF-1 alpha.

<b>Biological Strategies Validation. </b>Western Blot: HIF-1 alpha Antibody [NB100-449] - Analysis of HIF-1 alpha in human myeloma cell lysate using anti-HIF-1 alpha. Cells were untreated or treated with IGF-1, IL-6 or CoCl2. Image from verified customer review.

Western Blot: HIF-1 alpha Antibody [NB100-449] - Detection of HIF-1 alpha in a hypoxic sample. Lane 1: CoCl2 treated Cos-7 nuclear extract (hypoxic). Lane 2: Untreated Cos-7 nuclear extract (normoxic).

Western Blot: HIF-1 alpha Antibody [NB100-449] - Detection of mouse HIF-1 alpha on hypoxia treated MEFs

<b>Biological Strategies Validation. </b>Western Blot: HIF-1 alpha Antibody [NB100-449] - Samples: Whole cell lysate (5, 15 and 50 ug) from HeLa cells that were treated with cobalt chloride (+; 200 uM) or mock treated (-). Antibodies: Affinity purified rabbit anti-HIF1 alpha antibody NB100-449 used for WB at 0.1 ug/ml. Detection: Chemiluminescence with exposure times of 30 seconds.

Western Blot: HIF-1 alpha Antibody [NB100-449] - BMDM were seeded at 0.5x10^6 overnight. Cells were treated with 10 ng/ml LPS for 24 hrs. Image from verified customer review.

Western Blot: HIF-1 alpha Antibody [NB100-449] - Analysis of total protein using anti-HIF-1 alpha, -CAIX, -ISCU antibodies and VDACs antibody (PMID: 29596470).

Western Blot: HIF-1 alpha Antibody [NB100-449] - Analysis of total protein using anti-HIF-1 alpha, -ISCU, -FXN antibodies. CoCl2 was used to treat or not HeLa cells for 2 days (PMID: 29596470).

Western Blot: HIF-1 alpha Antibody [NB100-449] - Detection of human HIF1 alpha by western blot. Samples: Whole cell lysate (15 and 50 ug) from HEK293T cells that were either treated with 200 uM cobalt chloride (+) or mock treated (-). Antibodies: Affinity purified rabbit anti-HIF1 alpha antibody NB100-449 used for WB at 0.1 ug/ml. Detection: Chemiluminescence with exposure times of 3 minutes.

Western Blot: HIF-1 alpha Antibody [NB100-449] - 3T3-L1 mouse embryonic fibroblast adipose-like cell line. Antibody at 1:2000. WB image submitted by a verified customer review.

<b>Biological Strategies Validation. </b>Immunocytochemistry/Immunofluorescence: HIF-1 alpha Antibody [NB100-449] - Formaldehyde-fixed asynchronous HeLa cells.

Immunoprecipitation: HIF-1 alpha Antibody [NB100-449] - HIF-1 alpha analysis in HEK293 cells. Image from verified customer review.

Immunoprecipitation: HIF-1 alpha Antibody [NB100-449] - Detection of human HIF1 alpha by western blot of immunoprecipitates. Samples: Whole cell lysate (1 mg for IP, 20% of IP loaded) from HEK293T cells that were treated with 200 uM cobalt chloride. Antibodies: Affinity purified rabbit anti-HIF1 alpha antibody NB100-449 used for WB at 1 ug/ml and for IP at 6 ug/mg lysate. Detection: Chemiluminescence with exposure times of 3 minutes.

beta -Glucan size affects the requirement for reactive oxygen species (ROS) in IL-1 beta induction.(B) Human mDCs from healthy donors or chronic granulomatous disease (CGD) patients were stimulated with curdlan or glucan-mp for 8 h. HIF-1 alpha and pro-IL-1 beta protein expression measured by immunoblot (n = 2 donors).

Hypoxia downregulates CFTR expression. (e) Western blot showing the expression changes of HIF-1alpha and EMT markers induced by hypoxia in MDCK cells, quantification analysis is shown in the lower panel, *p < 0.05; (Full-length blot is shown in Supplementary Figure S7d.). Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/28701694), licensed under a CC-BY licence.

BCAT1 expression and inhibition in human macrophages. (e) Western blot analysis of IRG1, IL-1beta, HIF-1alpha and beta-actin (ACTB) in control (untreated), ERG240-treated (20 mM, 3 h), LPS treated (100 ng ml-1, 3 h) and LPS+ERG240 treated (LPS, 100 ng ml-1; ERG240, 20 mM for 3 h) hMDMs. The experiment is representative of three independent experiments using n=3 healthy donor hMDMs each. Image collected and cropped by CiteAb from the following publication (//www.nature.com/articles/ncomms16040), licensed under a CC-BY licence.

Elevated PIK3/AKT/HIF-1alpha pathways in KL SqCC tumours. (c) IHC analysis (top) and quantification (bottom) of p63, p-AKT, p-S6, p-4EBP1, HIF-1alpha and GLUT1 in KL tumours (n=6 each group). Two-tailed t-test, ****P<0.0001, ***P<0.001, **P<0.01. Scale bar, 50 um. Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/28548087), licensed under a CC-BY licence.

Adenosine mediates increase in pro-IL-1beta via a HIF-1alpha-dependent pathway. (h) LPS primed PECs obtained from HIF-1alpha-cKO and control mice were treated with or without NECA at different time points as indicated followed by pulsing with ATP. Cell lysates were collected after ATP pulsing. HIF-1alpha, pro-caspase-1, Caspaspe-1 and pro-IL-1beta was measured in cell supernatant by western blot. Immunoblots shown are representative results from at least three independent experiments. Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/24352507), licensed under a CC-BY licence.

Morphological alterations induced by DMOG are HIF-1alpha dependent. (A) glEND.2 cells were stably transfected with shGFP, shHIF-1alpha or shHIF-2alpha. The clones were cultured under normoxic (N) or hypoxic (H, 1% O2) conditions, or treated with DMOG (D, 1 mM) for 6 h. 30 ug protein of cellular protein were loaded for the detection of HIF-1alpha, and nuclear extracts (20 ug protein) were used for the detection of HIF-2alpha. Image collected and cropped by CiteAb from the following publication (//biosignaling.biomedcentral.com/articles/10.1186/1478-811X-11-80), licensed under a CC-BY licence.

Pyruvate kinase isoform M2 (PKM2) and hypoxia-inducible factor 1alpha (Hif-1alpha) bind directly to the promoter region of PDL1 in primary murine BMDM cells. BMDM cells were treated with TEPP-46 at 50 uM for 1 h prior to stimulation with LPS (100 ng/ml, 24 h) (C) Sequential ChIP assays measuring simultaneous endogenous binding of PKM2 and Hif-1alpha to chromatin in response to LPS (100 ng/ml, 24 h) +/-TEPP-46 (pretreatment using 50 uM, 60 min). ChIP data are calculated as percent of input, error bar represents mean +/- SEM, and statistics are performed as two-tailed unpaired t-test *P < 0.05, **P < 0.01, and ***P < 0.001. Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/29081778), licensed under a CC-BY licence.

Changes in Hepatic Oxygen Saturation and Hypoxia-related Protein Expression. (C) In the Western blot analysis, the experimental group was relatively higher expression of hypoxia-inducible factor-1alpha (HIF-1alpha) and vascular endothelial growth factor (VEGF) protein than the control group at eight weeks. The full-length blots with these antibodies were presented in supplementary Figure S1. Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/29079853), licensed under a CC-BY licence.

Effects of cell stress on VEGF-A and HIF1alpha expression in Muller cells and Y79 photoreceptors. (B) Western blots for HIF1alpha using cellular proteins, n = 4/group, ** p < 0.01. For MIO-M1 Muller cells: Grey bars: 5 mM glucose. Black bars: 25 mM glucose. For Y79 photoreceptors: Grey bars: 11 mM glucose. Black bars: 25 mM glucose. NS, not significant; LG, low glucose; HG, high glucose. Image collected and cropped by CiteAb from the following publication (//www.mdpi.com/1422-0067/18/3/533), licensed under a CC-BY licence.

Hypoxic conditions upregulate CNN3 in BeWo cells.BeWo cells were cultured either under normoxic or under hypoxic conditions for 24hr. (A) Total protein lysates were examined with the Western Blot technique to detect CNN3 protein levels. For normalization, HPRT was stained on the same membrane. As hypoxia marker, HIF-1 alpha was detected as well. Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/25050546), licensed under a CC-BY licence.

Phenylhydrazine administration results in hypoxia in retinal vessels and in HIF-1alpha and HIF-2alpha stabilization in peripheral blood leukocytes. (B) Representative analysis of HIFs by western blot: 50ug of protein from total cell lysate of blood leukocytes isolated from mice treated with PHZ compared to untreated. Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/28112274), licensed under a CC-BY licence.

Western Blot: Rabbit Polyclonal HIF-1 alpha Antibody - Analysis of HIF-1 alpha antibody on mouse liver nuclear extracts. Image from a verified customer review.

Improved survival and blood–brain barrier function post pneumococcal infection in mice by anti-HIF-1 alpha treatment using echinomycin. a Schematic depicting treatment protocol of mice infected with S. pneumoniae (D39). Mice were infected i.p., followed by anti-HIF-1 alpha treatment with echinomycin or just vehicle every 12 h starting 4 h post-infection (blue tick marks). Clinical scores were taken every 4 h starting 16 h post-infection (red line with tick marks) and study terminated at 48 h post-infection and brain tissues collected upon animal death or at the end point when the animals were sacrificed. b Clinical scores indicate improved symptoms in echinomycin-treated mice compared to vehicle-treated animals starting 16 h post-infection that were progression free (below score 1) up to 24 h (mean ± SEM at each time, N = 10/group, ****p < 0.0001, **p < 0.01, *p < 0.05 by 2-tailed unpaired non-parametric Mann–Whitney t test at each time point. c Echinomycin-treated mice showed significantly improved overall survival percentage by Kaplan–Meier analysis with the median survival at 32 h compared to 25 h in vehicle-treated mice (**p < 0.01, log-rank test, N = 10/group). d Kaplan–Meier analysis also indicated a significant improvement in progression-free survival in echinomycin-treated animals (median survival 25 h) with no clinical symptoms up to 24 h (b) compared to the vehicle group (median survival 17 h; ***p < 0.001, log-rank test, N = 10/group). e Immunofluorescence staining for HIF-1 alpha , BBB permeability and junctional markers in the echinomycin and vehicle groups at the survival end point. Left panel shows that echinomycin treatment leads to a reduction in HIF-1 alpha -positive nuclei including in ECs co-stained for podocalyxin, a vascular marker which was unchanged by the treatment. Middle panel displays reduced vascular permeability to fibrinogen in the echinomycin group as indicated by stronger intravascular signal compared to the vehicle-treated mice. Increased expression of tight junction proteins—occludin (middle panel) and claudin-5 (right top panel)—in echinomycin-treated mice indicate improved BBB function. Tight junction-associated ZO-1, adherens junction marker VE-Cadherin, and endothelial cell adhesion molecule CD31 were unchanged (middle, bottom right panel). There was also no difference in S. pneumoniae (Spn) staining (right top panel) between the two groups. Scale bar 10 μm. f Quantification of the staining from e utilizing four images per animal in the cortex region shows a significant reduction in HIF-1 alpha -positive cell number, whereas the total cell number or EC cell number was unchanged (left panel). As observed in e, the middle panel for quantification (arbitrary units—a.u.) of fibrinogen leakage shows significantly increased vascular staining for fibrinogen, supported by significantly increased expression of occludin, claudin-5, whereas other EC junction markers were unchanged. S. pneumoniae numbers in the vessels (v-Spn) or those transmigrated into brain parenchyma (b-Spn) were also unchanged. (mean ± SEM, N = 7–10/group indicated by the corresponding number of dots, ****p < 0.0001, **p < 0.01, *p < 0.05 by 2-tailed unpaired Student’s t test) Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/32529267), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Compound MI-743 causes intracellular 8-oxo-dG accumulation and DNA damage.a MGC-803, HGC-27 and GES-1 cells were treated with DMSO or 5 µM MI-743 for 48 h. Intracellular 8-oxo-dG was stained with Cy3-conjugated avidin. DNA was counterstained with 4,6-diamidino-2-phenylindole (DAPI). Images were acquired at ×100 magnification by a Nikon Eclipse TE 2000-S fluorescence microscope. At least three independent experiments were performed for each group. b MGC-803, HGC-27 and GES-1 cells were treated with DMSO or 10 µM MI-743 for 48 h and run in alkaline comet assay. Pictures were originally captured at ×40 magnification. H2O2 was used as positive control. c Tail moment was calculated by CometScore software. Three individual experiments were performed for each group. d–f Western blot analysis of the protein levels of MTH1, MUTYH, OGG1, p21, ATMpS1981 and p53pS15 in MGC-803, HGC-27 and GES-1 cells, treated with increasing concentrations of MI-743 (0, 1, 2, 4, 8 and 12 µM). g, h Densitometry shows relative protein expression normalized for GAPDH. Data are representative of three independent experiments. i–k Western Blot analysis of the protein levels of MTH1, MUTYH, OGG1, p21, ATMpS1981 and p53pS15 of protein lysates, isolated from MGC-803, HGC-27 and GES-1 cells, which were treated with 12 µM MI-743 for 0, 12, 24, 36 and 48 h. l, m Densitometry shows relative protein expression normalized for GAPDH. Data are presented as means ± SD. Three individual experiments were performed for each group. *P < 0.05, **P < 0.01, ***P < 0.001 as compared with the controls Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/31164636), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Successful knockdown of HIF-2 alpha in both 786-O and A498 renal cell lines. (A) Lysates from 786-O cells stably transfected with VHL (VHL +), parental 786-O cells (786-O), and 786-O cells infected with an empty retrovirus (pSuperRetro) or with retroviruses encoding single HIF-2 alpha shRNAs (HIF2 alpha shRNA 1; HIF2 alpha shRNA 2) or doubly infected with both shRNAs (HIF2 alpha shRNA 1+2) were immunoblotted for HIF-2 alpha (top panel), GLUT1 (upper middle panel) and VHL (lower middle panel). Bottom panel is an alpha tubulin immunoblot to demonstrate equal protein loading (25 μg) in each lane. (B) Lysates from A498 cells stably transfected with VHL (VHL +), parental A498 cells (A498), and A498 cells infected with an empty retrovirus (pSuperRetro) or doubly infected with both HIF-2 alpha shRNAs (HIF2 alpha shRNA 1+2) were immunoblotted as in (A). Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/17598890), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

IQGAP1 induces the epithelial-to-mesenchymal transition, invasiveness, and proliferation of endometrial cancer (EC) cellsA. Reverse transcription quantitative PCR (qPCR) analysis of IQGAP1 mRNA in the immortalized human endometrial cell line EM and the EC cells HEC-1, HEC-50, and HEC-50-HI (HI). The results are presented as the fold-change in expression compared to the EM cells. B. Western blot analysis of the IQGAP1 protein in EC cells. C, E. The expression of IQGAP1, E-cadherin, and N-cadherin proteins in HI cells transfected with control (Ctr) or IQGAP1 siRNA (C) and in HEC-1 cells expressing either the control or IQGAP1 vector (E). D, F. Phase-contrast microscopy shows the morphology of HI cells transfected with control or IQGAP1 siRNA (D) and HEC-1 cells transfected with the control or IQGAP1 vector (F). G-I. Detection of migration (G), invasion (H), and proliferation (I) in HI and HEC-1 cells after the indicated transfection. J, K. qPCR analysis of ZO-1, CK-18, and Vimentin expression in HI (J) and HEC-1 (K) cells, transfected as indicated. L. Representative images from the invasion assays. Image collected and cropped by CiteAb from the following open publication (//www.oncotarget.com/lookup/doi/10.18632/oncotarget.7754), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

FDFT1 inhibits glycolysis through suppressing the AKT-mTOR-HIF1 alpha pathway in CRC.aFDFT1 overexpression reduced glucose uptake in CT26 cells. bFDFT1 overexpression decreased lactate production via glycolysis in CT26 cells. c ECAR was reduced when FDFT1 was overexpressed in CT26 cells. d OCR was increased when FDFT1 was overexpressed in CT26 cells. eFDFT1 knockdown increased glucose uptake in CT26 cells. fFDFT1 knockdown increased lactate production via glycolysis in CT26 cells. g ECAR was increased when FDFT1 was knocked down in CT26 cells. h OCR was decreased when FDFT1 was knocked down in CT26 cells. i, mFDFT1 overexpression inhibited the protein and mRNA expression of mTOR-targeted glycolytic enzymes, including GLUT1, HK2, PGK1, GPI, and LDHA, in CT26 cells. j, mFDFT1 knockdown increased the protein and mRNA expression of mTOR-targeted glycolytic enzymes, including GLUT1, HK2, PGK1, GPI, and LDHA, in CT26 cells. k, nFDFT1 overexpression decreased the protein and mRNA expression of AKT, mTOR, and HIF1 alpha . l, nFDFT1 knockdown increased the protein and mRNA expression of AKT, mTOR, and HIF1 alpha . o Photograph of dissected tumors (the first line: normal diet, the second line: FMD + glucose, the third line: FMD, n = 5). p The tumor volumes were measured every 2 days after the 13th day. The FMD + glucose group can reverse the tumor growth inhibition induced by the FMD (n = 5; ns: P = 0.1838; P = 0.0001). q The protein level of FDFT1 and mTOR in dissected tumor samples from normal diet group, FMD group and FMD + glucose group was measured by western blotting. r The glucose level in these three groups. Error bars, mean ± SD, the data are from three independent experiments. Two-sided t tests. *P < 0.05, **P < 0.01, ***P < 0.001, compared with the control group (or normal diet group). #P < 0.05, ##P < 0.01. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/32313017), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Effect of MLL-HCF1 interaction on histone methylation and Nrf2 expression in SNUC5/5-FUR cellsA. HCF1 expression was determined by Western blotting. *Significantly different from SNUC5 cells (p<0.05). B. Interaction between MLL and HCF1was examined by immunoprecipitation analysis using anti-MLL and anti-HCF1 antibodies followed by Western blotting with anti-HCF1 and anti-MLL antibodies. *Significantly different from SNUC5 cells (p<0.05). C. Interaction between MLL and HCF1was assessed by PLA. Each green spot represents for a single interaction (MLL and HCF1) and DNA was stained with DAPI. *Significantly different from SNUC5 cells (p<0.05). The cells were transfected with non-targeting siRNA (siControl) or siHCF1 RNA for 24 h. D. Expression pattern of MLL mRNA in SNUC5/5-FUR cells was determined by RT-PCR analysis. *Significantly different from siControl-transfected cells (p<0.05). E. Expression pattern of HCF1, MLL, and Nrf2 in SNUC5/5-FUR cells was determined by Western blot analysis. *Significantly different from siControl-transfected cells (p<0.05). Image collected and cropped by CiteAb from the following open publication (//www.oncotarget.com/lookup/doi/10.18632/oncotarget.9745), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Induction of ubiquitin/proteasome-dependent DSBs in CPT-treated quiescent WI38 hTERT cells. (A–F) Serum-starved cells were treated with DMSO (1 h) or with MG132 (50 μM, 1 h), lactacystin (10 μM, 1 h), bortezomib (1 μM, 4 h), G5 (1.5 μM, 0.5 h) or Pyr-41 (9 μM, 0.5 h) before the addition of DMSO (untreated) or 25 μM CPT for 1 h and then co-stained for gamma H2AX (green) and 53BP1 (red) or analyzed by Western blot. ‘-’ in panels C and F means cells treated with DMSO. (A and D) Representative pictures. Nuclear contours, identified by DAPI staining (not shown), are indicated by dashed lines. Bars: 10 μm. (B and E) Number of gamma H2AX foci per nucleus from two independent experiments (147–153 nuclei were analyzed for each treatment). ****P < 0.0001. (C and F) Western blot of gamma H2AX. alpha Tubulin: loading control. Dashed lines indicate that intervening wells have been spliced out. The top panels show quantification of gamma H2AX normalized to alpha Tubulin (means ± SEM, n = 4 in panel C, n = 3 in panel F). ***P < 0.001; **P < 0.01. (G and H) Detection of DSBs by neutral Comet assays in serum-starved cells treated with DMSO or MG132 (25 μM) for 1 h before the addition of DMSO (untreated) or CPT for 1 h (7.5 μM for experiments (Exp) I and II; 5 and 7.5 μM for Exp III). (G) Representative pictures of nuclei from Exp I. (H) Quantification of neutral Comet tail moments for three independent experiments (95–133 nuclei were analyzed for each treatment in each experiment). ***P < 0.001; ****P < 0.0001. The untreated and CPT data from Exp I are from the same experiment as that of Supplementary Figure S3D. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/26578593), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

$S100A7 is secreted and acts as a chemotactic factor of cell migration and invasionA. Cells were cultured in serum-free medium for 2 days, then the medium was collected, fractioned, followed by Western Blot analysis. B&C. Transwell migration and Matrigel invasion assays were performed in C33A and SiHa cells. Cell suspension was placed into the upper chamber in 0.1 ml of DMEM serum-free medium, and conditioned medium from S100A7-overexpressed C33A and SiHa cells and their corresponding control cells was placed in the lower chamber as a chemoattractant. The stained cells were manually counted from 4 randomly selected fields and normalized with cell proliferation [2-sided t test; *P < 0.05; ***P < 0.001]. Representative image and quantitative results of cell migration and invasion were shown (B. C33A cells; C. SiHa cells; ×10, bars:100μm). Image collected and cropped by CiteAb from the following open publication (//www.oncotarget.com/lookup/doi/10.18632/oncotarget.15329), licensed under a CC-BY license. Not internally tested by Novus Biologicals.$

Increased expression of HIF alpha and/or Twist in A549 and H441 cells induced by the inhibition of PIMT and Thapsigargin(A) Immunoblotting of Slug, ZEB1, Snail1, Twist, and HIF1 alpha in A549 sh-PIMT and sh-control cells. (B, C) Immunoblotting and relative intensity of HIF1 alpha in A549 cells treated with Tg. (D) Immunoblotting of Slug, ZEB1, Snail1, Twist, and HIF1 alpha in si-control cells and si-PIMT H441 cells. (E, F) Immunoblotting and relative intensity of HIF1 alpha in H441 cells treated with Tg. #1 and #2 indicates si-RNA of J-010000-05-0002 and J-010000-07-0002, respectively. Image collected and cropped by CiteAb from the following open publication (//www.oncotarget.com/lookup/doi/10.18632/oncotarget.24324), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Role of inflammasome in glucose fluctuation-induced myocardial fibrosis. (A) Immunofluorescence staining of intracellular NLRP3–ASC interaction examined by confocal microscopy. The NRCFs were labeled with anti-NLRP3 (red), anti-ASC (green), and DAPI (blue) (n = 3 per group). (B–G) After siRNA targeting NLRP3 transfection, the protein expressions of NLRP3, cleaved caspase-1 and collagen I were measured by western blot (n = 3 per group). (H) Representative images of immunofluorescence staining of intracellular alpha -SMA in the NG, HG, GF, and GF + siRNA groups (n = 3 per group). Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/35592403), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

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NBP1-04676

PGC1 alpha Antibody - BSA Free

(11 Reviews)

(261 Publications)

0.1 ml

NBP1-04676

Mitochondrial content and biogenesis. Immunoblot analysis of PGC1 alpha in MEFs (n = 7; t = 5.764; df = 6). Image collected and cropped by CiteAb from the following publication (//www.nature.com/articles/s41598-017-12662-3), licensed under a CC-BY license.

Analysis of a FFPE section of mouse prostate using rabbit polyclonal PGC1 alpha Antibody at 1:200 dilution. The antibody generated an expected strong nuclear (punctate in some cells) and a weak cytoplasmic staining in the glandular cells lining of tubule-alveolar gland.

An intracellular stain was performed on A431 cells with PGC1 alpha Antibody NBP1-04676 (blue) and matched isotype control NBP2-24891 (orange). Cells were fixed with 4% PFA and then permeabilized with 0.1% saponin. Cells were incubated in an antibody dilution of 1.0 ug/mL for 30 minutes at room temperature, followed by Rabbit IgG (H+L) Cross-Adsorbed Secondary Antibody, Dylight 550 (SA5-10033, Thermo Fisher).

<b>Biological Strategies Validation. </b>Vehicle or RU 486 (5 mg/kg) injected mice were presented with/without corticosterone (10 mg/kg) for 3 days. The expressions of peroxisome proliferator-activated receptor gamma coactivator 1-alpha (PGC1 alpha NBP1-04676) and NIX (BNIP3L NBP1-88558) were visualized via western blotting. Loading control is beta-actin. n = 5. Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/33473105/) licensed under a CC-BY license.

Total protein from human adipose and skeletal muscle tissue, HeLa and A431 cells lines was separated on a 7.5% gel by SDS-PAGE, transferred to PVDF membrane and blocked in 5% non-fat milk in TBST. The membrane was probed with 2.0 ug/mL PGC1 alpha Antibody (Molecular weight: 91 KDa) in 1% non-fat milk in TBST and detected with an anti-rabbit HRP secondary antibody using chemiluminescence

Western Blot of total protein from murine skeletal muscle tissue using PGC1 alpha Antibody. Image from verified customer review.

HeLa cells were fixed for 10 minutes using 10% formalin and then permeabilized for 5 minutes using 1X TBS + 0.5% Triton X-100. The cells were incubated with PGC1 alpha Antibody [NBP1-04676] at a 1:200 dilution overnight at 4C and detected with an anti-rabbit DyLight 488 (Green) at a 1:500 dilution. Alpha tubulin (DM1A) [NB100-690] was used as a co-stain at a 1:1000 dilution and detected with an anti-mouse DyLight 550 (Red) at a 1:500 dilution. Nuclei were counterstained with DAPI (Blue). Cells were imaged using a 40X objective.

Analysis of PGC1 alpha Antibody in mouse prostate using DAB with hematoxylin counterstain.

An intracellular stain was performed on HeLa cells with NBP1-04676AF647 (blue) and a matched isotype control (orange). Cells were fixed with 4% PFA and then permeabilized with 0.1% saponin. Cells were incubated in an antibody dilution of 2.5 ug/mL for 30 minutes at room temperature. Both antibodies were conjugated to Alexa Fluor 647.

An intracellular stain was performed on HepG2 cells with PGC1 alpha Antibody and a matched isotype control. Cells were fixed with 4% PFA and then permeablized with 0.1% saponin. Cells were incubated in an antibody dilution of 2.5 ug/mL for 30 minutes at room temperature, followed by Rabbit IgG (H+L) Cross-Adsorbed Secondary Antibody.

Western blot shows lysates of A431 human squamous carcinoma parental cell line and PGC1 alpha knockout (KO) A431 cell line. PVDF membrane was probed with 1:1000 of Rabbit Polyclonal PGC1 alpha Antibody (Catalog # NBP1-04676) followed by HRP-conjugated Anti-Rabbit IgG Secondary Antibody (Catalog #HAF008). Specific band was detected for PGC1 alpha at approximately 105 kDa (as indicated) in the parental A431 cell line, but is not detectable in the knockout A431 cell line. This experiment was conducted under reducing conditions.

DM1-derived fibroblasts have no changes in mitochondria biogenesis. (A, B) Representative images of immunofluorescence of TOMM20, and PGC1-alpha in DM1 and control fibroblasts (n=3). (C) Medium fluorescence intensity of MitoTracker Red FM in control (n=3) and DM1 cells (n=5) and (D) of Rhodamine 123 in DM1 and control fibroblasts (n=3). (E) mRNA levels of TFAM transcription factor (n=3). (F) mRNA levels of OPA1, MFN1, MFN2, DRP1 and PARKIN in DM1 and control fibroblasts (n≥2).

Feeding the diabetes mellitus (DM) mice with the RSV-enriched diet improved mitochondrial biogenesis in the quadriceps muscle. A) Representative western blots using antibodies against nuclear respiratory factor (NRF-1), ATP synthase, H+ transporting, mitochondrial F1 complex, beta polypeptide (ATP5B), cytochrome c oxidase subunit IV (Cox IV), peroxisome proliferator-activated receptor-gamma coactivator 1-alpha (PGC-1alpha), and GAPDH. Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/29578301), licensed under a CC-BY licence.

Mitochondrial content and biogenesis. (d) Immunoblot analysis of PGC1alpha in MEFs (n = 7; t = 5.764; df = 6). Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/28970491), licensed under a CC-BY licence.

Atg7 deficiency in vascular smooth muscle cells (VSMCs) alters mitochondrial quality control and enhances apoptosis. c) Western blot analyses of the expression of TFEB and PGC-1-alpha proteins in aortic VSMCs isolated from Atg7+/+Tagln-Cre+, ApoE-/- and Atg7F/FTagln-Cre+, ApoE-/- mice after 10 weeks of HFD. Cells were incubated either with or without oxidized LDL (200 ug ApoB/mL) for 8 h. beta-Actin was used as the loading control. The graph represents the densitometric analysis of the expression level of TFEB and PGC-1-alpha proteins. The data are expressed as mean +/- SEM of four independent experiments from different primary VSMC cultures. *P 12 in each group. (B) Western blot images using S100 beta , tubulin beta‐3, and beta ‐actin antibodies to total protein lysate in hippocampal area. The statistical results of internal standardized S100 beta / beta ‐tubulin ratio by beta ‐actin levels relative to young adult wild‐type C57BL/6J. White and black bars indicate the wild‐type C57BL/6J and Tet‐mev‐1 mice, respectively. Data are expressed as mean ± SD; *P 12 in each group. (C) Micrographs of immunohistochemical analysis on paraffined hippocampal tissue sections using GFAP and S100 beta antibody. Brown cells indicate GFAP‐stained astrocytes. Scale bar = 100 μm. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/27623715), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

At the time of second passage, vessels in successfully growing xenografts of four different tumor types surveyed were of murine origin: A-C Colon; D-F Lung; G-I Pancreatic; J-L Renal Cell Carcinoma. For each tumor type, a representative section of an original patient specimen labeled with anti-huCD31 is shown (A, D, G, J). For each tumor, sections of the first passage xenografted tumor when it was resected are also shown; while no huCD31(+) vessels were identified in the xenografts (B, E, H, K), msCD34(+) vessels were abundant (C, F, I, L). (bars = 50 μ). Image collected and cropped by CiteAb from the following open publication (//translational-medicine.biomedcentral.com/articles/10.1186/1479-5876-11-110), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Knockdown of autophagy-related gene 5 (ATG5) inhibits trehalose-induced autophagy in normal human primary airway epithelial cells.Normal human tracheobronchial epithelial cells were transfected with Naito1 chimera RNAi (control siRNA) or ATG5 chimera siRNA (ATG5 siRNA). Twenty-four hours after siRNA transfection, cells were treated with medium or trehalose (TRE, 100 mM) for 48 h. ATG5 protein (A) and LC3 I and LC3 II proteins (B) were examined by Western blot analysis with GAPDH protein used as loading control. The representative Western blot picture was shown from 2 independent experiments with each being performed in triplicate wells. Image collected and cropped by CiteAb from the following open publication (//dx.plos.org/10.1371/journal.pone.0124524), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

$Expression of ER stress associated protein and autophagy related protein in the C28I2 chondrocyte infected with Ad-ATG5 or Ad-ATG7. a The ATG5 and ATG7 mRNA level were analysed by RT-PCR in C28I2 cells. b Analysis of ATG5 and ATG7 mRNA level with Q-PCR in C28I2 cells. Ad-ATG5(a), Ad-ATG7(b). c The ATG5 protein expression was analysed by western blotting in the Ad-ATG5 infected C28I2 cells. The level of ATG5 was normalized to beta -actin. d The ATG7 protein expression was analysed by western blotting in the Ad-ATG7 infected C28I2 cells. The level of ATG7 was normalized to beta -actin. e The expression levels of LC3, P62, PERK, p-PERK, Nrf2 proteins after infected with Ad-ATG5 in C28I2 cells for 24 h by western blotting. The levels of related proteins were normalized to beta -actin. f The expression levels of LC3, P62, PERK, p-PERK, Nrf2 proteins after infected with Ad-ATG7 in C28I2 cells for 24 h by western blotting. The levels of related proteins were normalized to beta -actin. *P 100 mitochondria). Data analysis was performed by using one-way ANOVA (∗P 250 cells/chains per sample). c Representative whole-mount IF of adult Plzf-mC/CreER; Z/EG tubules D3 post-TAM (n = 2 mice). Arrowheads: PDX1+ As. Inset shows detail of indicated area. Scale bar, 50 μm. d Representative IF of adult WT testis sections (n = 4 mice). Insets: details of selected areas. EOMES+ GFR alpha 1+ (arrowheads) and EOMES− GFR alpha 1+ cells (bracket) are shown. Tubule stage is indicated. Scale bar, 50 μm. e Representative IF of adult Oct4-GFP testis section (n = 2 mice). Insets: immunostaining within indicated area. EOMES+ GFP− (arrowheads) and EOMES− GFP+ (bracket) spermatogonia are indicated. Asterisks: autofluorescent interstitium. Scale bar, 50 μm. f Representative flow cytometry of fixed and permeabilized testis cells from Oct4-GFP adults (n = 2). PLZF+ cells shown. g Representative IF of adult WT testis sections (n = 4 mice). Insets: immunostaining within indicated area. PDX1+ EOMES+ spermatogonia are indicated (arrowheads). Tubule stage is shown. Asterisk: autofluorescent interstitium. Scale bar, 50 μm. h Representative flow cytometry of fixed and permeabilized WT adult testis cells (n = 4). Mean numbers of EOMES+ and PDX1+ cells in PDX1+ and EOMES+ gates respectively are shown ± s.e.m. i Representative flow cytometry for KI67 in indicated PLZF+ populations of fixed and permeabilized adult WT testis cells (n = 4 mice). j Quantification of flow cytometry from i. Percentage of indicated PLZF+ fractions KI67+ . Horizontal bars: mean values (n = 4 mice). k Representative IF of adult WT testis sections demonstrating PDX1+ Aundiff localisation (arrowheads) within tubules (n = 4 mice). Asterisks: autofluorescent interstitium. Tubule stages are shown. Scale bar, 50 μm. l Quantification of spermatogonial localisation from k. Mean values ± s.e.m. are shown (n = 4 mice, 56–95 tubule sections per mouse). Significance vs. tubule-tubule localisation is indicated. m Representative IF of Id4IRES-GFP adult testis sections (n = 4 mice). Insets show immunostaining within indicated area. Arrowheads: PDX1+ EOMES+ GFP+ spermatogonia. Asterisk: PDX1low EOMES+ GFP+ cell. Tubule stage is shown. Scale bar, 50 μm. n Representative flow cytometry of indicated PLZF+ populations of fixed and permeabilized adult Id4IRES-GFP testis cells (n = 4 mice). Mean numbers of PDX1+ and EOMES+ Aundiff expressing GFP ± s.e.m. o Flow cytometry of Id4IRES-GFP testis cells as in n. PLZF+ fractions are shown. Mean numbers of PLZF+ GFP+ cells positive for EOMES and PDX1 are indicated ± s.e.m. (n = 4 mice). Significance was calculated by two-tailed Student’s t-test (***P < 0.001, ****P < 0.0001) Image collected and cropped by CiteAb from the following open publication (//www.nature.com/articles/s41467-018-04827-z), licensed under a CC-BY license. Not internally tested by Novus Biologicals.$

Reactivity:

Hu, Mu, Rt, Po, Gt, Ha, Sh, Sq, Ca, Eq, Pm

Species Glossary

Reactivity: Hu, Mu, Rt, Po, Gt, Ha, Sh, Sq, Ca, Eq, Pm

Applications:

, , , , , , , ,

Applications: , , , , , , , ,

Host:

Rabbit Polyclonal

Host: Rabbit Polyclonal

Sizes:

Sample Size Available

Sizes: Sample Size Available

Conjugate:

Unconjugated

Available Conjugates:

Validated by:

Validated by:

Conjugate	Catalog #	Availability	Size	Price
Alexa Fluor 350	NBP1-04676AF350
Alexa Fluor 405	NBP1-04676AF405
Alexa Fluor 488	NBP1-04676AF488
Alexa Fluor 532	NBP1-04676AF532
Alexa Fluor 594	NBP1-04676AF594
Alexa Fluor 647	NBP1-04676AF647
Alexa Fluor 700	NBP1-04676AF700
Alexa Fluor 750	NBP1-04676AF750
Allophycocyanin	NBP1-04676APC
Biotin	NBP1-04676B
DyLight 350	NBP1-04676UV
DyLight 405	NBP1-04676V
DyLight 488	NBP1-04676G
DyLight 550	NBP1-04676R
DyLight 594	NBP1-04676DL594
DyLight 650	NBP1-04676C
DyLight 680	NBP1-04676FR
DyLight 755	NBP1-04676IR
FITC	NBP1-04676F
HRP	NBP1-04676H
Janelia Fluor 549	NBP1-04676JF549
Janelia Fluor 646	NBP1-04676JF646
PE	NBP1-04676PE
PerCP	NBP1-04676PCP
mFluor Violet 450 SE	NBP1-04676MFV450
mFluor Violet 500 SE	NBP1-04676MFV500
mFluor Violet 610 SE	NBP1-04676MFV610

Available Formulations

Formulation	Catalog #	Availability	Price
BSA Free	NBP1-04676SS

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NB100-690

alpha Tubulin Antibody (DM1A) - BSA Free

(14 Reviews)

(134 Publications)

0.1 ml

NB100-690

Immunohistochemistry: alpha Tubulin Antibody (DM1A) [NB100-690] - Analysis of colon tissue. Sections were formalin fixed and embedded with paraffin. Sodium citrate heat mediated antigen retrieval for 20 min. Incubated with primary antibody for 15 min at a 5 ug/ml concentration. Corner image is staining with secondary only.

Immunohistochemistry: alpha Tubulin Antibody (DM1A) [NB100-690] - Analysis of formalin fixed paraffin embedded heart sections. Used at a dilution of 1:500.

Western Blot: alpha Tubulin Antibody (DM1A) [NB100-690] - Analsis of alpha tubulin in 9 cell lysates. Lane 1. HeLa; Lane 2. JURKAT; Lane 3. COS7; Lane 4. NIH-3T3; Lane 5. PC-12; Lane 6. RAT2; Lane 7. CHO; Lane 8. MDBK; Lane 9. MDCK

Flow Cytometry: alpha Tubulin Antibody (DM1A) [NB100-690] - Intracellular flow cytometric staining of 1 x 10^6 CHO (A) and HEK-293 (B) cells using alpha Tubulin antibody (dark blue). Isotype control shown in orange. An antibody concentration of 1 ug/1x10^6 cells was used.

Immunomicroscopy: alpha Tubulin Antibody (DM1A) [NB100-690] - Analysis of HeLa cells, green staining is alpha tubulin whereas red is DNA stained with propidium iodide.

Western Blot: alpha Tubulin Antibody (DM1A) [NB100-690] - GS treatment increases markers of beiging in 3T3-L1 adipocytes. GS treatment upregulates markers of beiging, including beta-3AR (C) proteins. Data presented as mean +/- SEM from n = 4 replicates per group. * p < 0.05, *** p < 0.001 vs. control. Abbreviations: beta-3 adrenergic receptor (beta-3AR). Image collected and cropped by CiteAb from the following publication (//www.mdpi.com/2305-6320/6/1/22), licensed under a CC-BY license.

Immunocytochemistry/Immunofluorescence: alpha Tubulin Antibody (DM1A) - BSA Free [NB100-690] - Mouse MS1 cells were fixed in 4% paraformaldehyde for 10 minutes and permeabilized in 0.05% Triton X-100 in PBS for 5 minutes. The cells were incubated with alpha Tubulin Antibody [DM1A] conjugated to Alexa Fluor 647 (NB100-690AF647) at 2 ug/ml for 1 hour at room temperature. Nuclei were counterstained with DAPI (Blue). Cells were imaged using a 100X objective and digitally deconvolved.

Immunohistochemistry-Paraffin: alpha Tubulin Antibody (DM1A) [NB100-690] - IHC analysis of a formalin fixed and paraffin embedded tissue section of mouse prostate using alpha Tubulin Antibody (DM1A) at 1:200 dilution. The signal was developed using HRP labelled secondary and DAB reagent which followed counterstaining with hematoxylin. The antibody generated a specific cytoplasmic/cytoskeletal staining in the prostate epithelial cells.

Flow Cytometry: alpha Tubulin Antibody (DM1A) [NB100-690] - An intracellular stain was performed on HeLa cells with alpha Tubulin [DM1A] Antibody NB100-690AF700 (blue) and a matched isotype control (orange). Cells were fixed with 4% PFA and then permeabilized with 0.1% saponin. Cells were incubated in an antibody dilution of 5 ug/mL for 30 minutes at room temperature. Both antibodies were conjugated to Alexa Fluor 700.

Western Blot: alpha Tubulin Antibody (DM1A) [NB100-690] - Western blot analysis of extracts from HeLa, COS and C6 cells using alpha Tubulin antibody (NB100-690, 1:1000, Alpha tubulin molecular weight: 50 kDa)

Western Blot: alpha Tubulin Antibody (DM1A) [NB100-690] - Analysis of alpha tubulin (molecular weight of 50 kDa) in 9 cell lysates. Lane 1. HeLa; Lane 2. JURKAT; Lane 3. COS7; Lane 4. NIH-3T3; Lane 5. PC-12; Lane 6. RAT2; Lane 7. CHO; Lane 8. MDBK; Lane 9. MDCK

Western Blot: alpha Tubulin Antibody (DM1A) [NB100-690] - Analysis of HeLa and COS-7 lysates. Alpha tubulin molecular weight: 50 kDa.

Immunocytochemistry/Immunofluorescence: alpha Tubulin Antibody (DM1A) [NB100-690] - IF Confocal analysis of C6 cells using alpha Tubulin antibody (NB100-690, 1:50). An Alexa Fluor 488-conjugated Goat to mouse IgG was used as secondary antibody (green, A). Actin filaments were labeled with Alexa Fluor 568 phalloidin (red, B). DAPI was used to stain the cell nuclei (blue, C).

Immunocytochemistry/Immunofluorescence: alpha Tubulin Antibody (DM1A) [NB100-690] - HeLa cells were fixed for 10 minutes using 10% formalin and then permeabilized for 5 minutes using 1X TBS + 0.5% Triton-X100. The cells were incubated with anti-alpha Tubulin (DM1A) (NB100-690) at a 1:200 dilution overnight at 4C and detected with an anti-mouse Dylight 488 (Green) at a 1:500 dilution. Nuclei were counterstained with DAPI (Blue). Cells were imaged using a 40X objective.

Immunocytochemistry/Immunofluorescence: alpha Tubulin Antibody (DM1A) [NB100-690] - Staining of skin fibroblasts.

Immunocytochemistry/Immunofluorescence: alpha Tubulin Antibody (DM1A) [NB100-690] - Analysis of embryonic fibroblasts in the anaphase portion of mitosis.

Immunocytochemistry/Immunofluorescence: alpha Tubulin Antibody (DM1A) [NB100-690] - U-251 MG cells were fixed in 4% paraformaldehyde for 10 minutes and permeabilized in 0.05% Triton X-100 in PBS for 5 minutes. The cells were incubated with anti-alpha Tubulin Antibody [DM1A] conjugated to Alexa Fluor 488 (NB100-690AF488) at 5 ug/ml for 1 hour at room temperature. Nuclei were counterstained with DAPI (Blue). Cells were imaged using a 100X objective and digitally deconvolved.

Immunocytochemistry/Immunofluorescence: alpha Tubulin Antibody (DM1A) [NB100-690] - A431 cells were fixed in 4% paraformaldehyde for 10 minutes and permeabilized in 0.05% Triton X-100 in PBS for 5 minutes. The cells were incubated with anti-alpha Tubulin Antibody [DM1A] conjugated to Alexa Fluor 488 (NB100-690AF488) at 5 ug/ml for 1 hour at room temperature. Nuclei were counterstained with DAPI (Blue). Cells were imaged using a 100X objective and digitally deconvolved.

Immunocytochemistry/Immunofluorescence: alpha Tubulin Antibody (DM1A) [NB100-690] - NIH3T3 cells were fixed in 4% paraformaldehyde for 10 minutes and permeabilized in 0.05% Triton X-100 in PBS for 5 minutes. The cells were incubated with anti-alpha Tubulin Antibody [DM1A] conjugated to Alexa Fluor 488 (NB100-690AF488) at 5 ug/ml for 1 hour at room temperature. Nuclei were counterstained with DAPI (Blue). Cells were imaged using a 100X objective and digitally deconvolved.

Immunocytochemistry/Immunofluorescence: alpha Tubulin Antibody (DM1A) [NB100-690] - HeLa cells were fixed in 4% paraformaldehyde for 10 minutes and permeabilized in 0.05% Triton X-100 in PBS for 5 minutes. The cells were incubated with alpha Tubulin Antibody [DM1A] conjugated to Janelia Fluor 549 (NB100-690JF549) at 5 ug/ml for 1 hour at room temperature. Nuclei were counterstained with DAPI (Blue). Cells were imaged using a 100X objective and digitally deconvolved.

Immunohistochemistry: alpha Tubulin Antibody (DM1A) [NB100-690] - Analysis of paraffin embedded colon sections.

Immunohistochemistry: alpha Tubulin Antibody (DM1A) [NB100-690] - Analysis of small intestine tissue fixed with formalin and paraffin embedded showing cytoplasmic and cytoskeletal staining of glandular cells.

Immunohistochemistry-Paraffin: alpha Tubulin Antibody (DM1A) [NB100-690] - IHC analysis of a formalin fixed paraffin embedded tissue section of mouse skeletal muscle using alpha Tubulin Antibody (DM1A) at 1:100 dilution with HRP-DAB detection and hematoxylin counterstaining. The antibody generated a strong cytoplasmic signal in the muscle cells with cytoplasmic-nuclear signal in the endothelial cells.

Flow Cytometry: alpha Tubulin Antibody (DM1A) [NB100-690] - Analysis of PE conjugate of NB100-690. An intracellular stain was performed on RAW 246.7 cells with Alpha Tubulin antibody (DM1A) NB100-690PE (blue) and a matched isotype control NBP2-27287PE (orange). Cells were fixed with 4% PFA and then permeablized wi

Flow Cytometry: alpha Tubulin Antibody (DM1A) [NB100-690] - Analysis of PE conjugate of NB100-690. An intracellular stain was performed on SH-SY5Y cells with Alpha Tubulin antibody (DM1A) NB100-690PE (blue) and a matched isotype control NBP2-27287PE (orange). Cells were fixed with 4% PFA and then permeablized with

Flow (Intracellular): alpha Tubulin Antibody (DM1A) [NB100-690] - An intracellular stain was performed on HeLa cells with alpha Tubulin Antibody (DM1A) NB100-690AF488 (blue) and a matched isotype control (orange). Cells were fixed with 4% PFA and then permeablized with 0.1% saponin. Cells were incubated in an antibody dilution of 5 ug/mL for 30 minutes at room temperature. Both antibodies were conjugated to Alexa Fluor 488. Image from the Alexa Fluor 488 version of this antibody.

Immunomicroscopy: alpha Tubulin Antibody (DM1A) [NB100-690] - Staining of the marine parasite Cryptocaryon irritans mouth. Large bundles of microtubules form a cytophyrigeal basket.

GS treatment increases markers of beiging in 3T3-L1 adipocytes. GS treatment upregulates markers of beiging, including UCP1 (A), TBX1 (B), and beta -3AR (C) proteins. Data presented as mean ± SEM from n = 4 replicates per group. * p < 0.05, *** p < 0.001 vs. control. Abbreviations: isoproterenol (ISO), uncoupling protein 1 (UCP1), glyceraldehyde 3-phosphate dehydrogenase (GAPDH), T-box protein 1 (TBX1), beta -3 adrenergic receptor ( beta -3AR).

Simvastatin increases cytotoxicity in lung cancer cells. (F) Western blots of indicated proteins involved in apoptosis and autophagy in both Bm7 and HCC827 cells with control (shGFP) and p53 knockdown (shTP53) treated with simvastatin is shown. MDM2, murine double minute 2; AKT, serine-threonine kinase; PARP, poly (ADP-ribose) polymerase; mTOR, mammalian target of rapamycin; WT, wild type. Full-length blots/gels are presented in Supplementary Fig. 1. Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31892709), licensed under a CC-BY licence.

$Role of HIF-1 alpha , FOXO3 in hypoxia-induced BNIP3 expression. (A) UCB-hMSCs were incubated with various durations of hypoxia (0–48 h). The protein expressions of HIF-1 alpha and beta -actin were detected by western blot. n = 4. (B) UCB-hMSCs were pretreated with NAC (5 mM) for 30 min prior to hypoxia incubation for 24 h. The protein expressions of HIF-1 alpha , lamin A/C and beta -tubulin in non-nuclear and nuclear fractionized cell samples were assessed by using western blot. n = 3. (C) UCB-hMSCs were immuno-stained with HIF-1 alpha and PI (magnification ×600). Scale bars, 37.5 µm. (D) HIF1A siRNA or NT siRNA was transfected to cells prior to hypoxia treatment for 24 h. The mRNA expression of BNIP3 was analyzed by qPCR. n = 6. (E) The protein expressions of BNIP3 and HIF-1 alpha were detected by western blot. n = 4. (F) NAC (5 mM) was pretreated to UCB-hMSCs prior to hypoxia treatment for 24 h. FOXO3, lamin A/C and beta -tubulin proteins expressions were assessed by western blot. n = 3. (G) FOXO3 siRNA transfected to UCB-hMSCs prior to hypoxia treatment for 24 h. The FOXO3 mRNA expression was measured by qPCR. n = 6. (H) BNIP3, FOXO3 and beta -actin expressions were detected by western blot. n = 3. Western blot data were normalized by beta -actin, and qPCR data were normalized by ACTB mRNA expression level. Lamin A/C and beta -tubulin were used as nuclear and non-nuclear protein controls, respectively. Quantitative data are presented as a mean ± S.E.M. All blots and confocal images are representative. *p < 0.05 versus control, #p < 0.05 versus hypoxia. Image collected and cropped by CiteAb from the following open publication (//linkinghub.elsevier.com/retrieve/pii/S2213231717303804), licensed under a CC-BY license. Not internally tested by Novus Biologicals.$

Elevated levels of additional proteins and GM3 ganglioside in the MEC of MPS IIIB brain.Staining performed with antibodies to the indicated substances was observed in the MEC region of 3 month-old MPS IIIB mice (for total ubiquitin and polyubiquitin) and 6 months for all others. Staining was not seen in the MEC region of age-matched control mice (Naglu +/−) nor in the LEC region of MPS IIIB mice (the latter not shown). Image collected and cropped by CiteAb from the following open publication (//dx.plos.org/10.1371/journal.pone.0027461), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Alpha Tubulin (DM1A) was detected in immersion fixed U-251 MG human glioblastoma cell line using Mouse anti-alpha Tubulin (DM1A) Protein-G purified Monoclonal Antibody conjugated to Alexa Fluor® 647 (Catalog # NB100-690AF647) (light blue) at 2 µg/mL overnight at 4C. Cells were counterstained with DAPI (dark blue). Cells were imaged using 100X objective and digitally deconvolved.

Reactivity:

Hu, Mu, Rt, Po, Av, Bv, Ca, Ch, ChHa, Dr, Fu, Gp, Gt, Ha, Pa, Pm, Pm, Rb, Xp, Ye

Species Glossary

Reactivity: Hu, Mu, Rt, Po, Av, Bv, Ca, Ch, ChHa, Dr, Fu, Gp, Gt, Ha, Pa, Pm, Pm, Rb, Xp, Ye

Applications:

, , , , , ,

Applications: , , , , , ,

Host:

Mouse Monoclonal

Host: Mouse Monoclonal

Sizes:

Sample Size Available

Sizes: Sample Size Available

Conjugate:

Unconjugated

Available Conjugates:

Conjugate	Catalog #	Availability	Size	Price
Alexa Fluor 350	NB100-690AF350
Alexa Fluor 405	NB100-690AF405
Alexa Fluor 488	NB100-690AF488
Alexa Fluor 532	NB100-690AF532
Alexa Fluor 594	NB100-690AF594
Alexa Fluor 647	NB100-690AF647
Alexa Fluor 700	NB100-690AF700
Alexa Fluor 750	NB100-690AF750
Allophycocyanin	NB100-690APC
Biotin	NB100-690B
DyLight 350	NB100-690UV
DyLight 405	NB100-690V
DyLight 488	NB100-690G
DyLight 550	NB100-690R
DyLight 594	NB100-690DL594
DyLight 650	NB100-690C
DyLight 680	NB100-690FR
DyLight 755	NB100-690IR
FITC	NB100-690F
HRP	NB100-690H
Janelia Fluor 549	NB100-690JF549
Janelia Fluor 646	NB100-690JF646
PE	NB100-690PE
PerCP	NB100-690PCP
mFluor Violet 450 SE	NB100-690MFV450
mFluor Violet 500 SE	NB100-690MFV500
mFluor Violet 610 SE	NB100-690MFV610

Available Formulations

Formulation	Catalog #	Availability	Price
BSA Free	NB100-690SS
Azide and BSA Free	NBP2-80570

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NBP1-30054

Collagen I alpha 1 Antibody - Azide and BSA Free

(2 Reviews)

(67 Publications)

0.1 ml

NBP1-30054

Immunohistochemistry: Collagen I alpha 1 Antibody - Azide and BSA Free [NBP1-30054] - Collagen I Antibody [NBP1-30054] - Formaldehyde-fixed fibrotic mouse lung tissue. The antibody recognizes mature collagen I (red) that has formed fibrils in the extracellular matrix.

Simple Western: Collagen I alpha 1 Antibody - Azide and BSA Free [NBP1-30054] - Simple Western lane view shows a specific band for Collagen I Alpha 1 in 0.5 mg/ml of Human Lung (left) and Human Kidney (right) lysate. This experiment was performed under reducing conditions using the 66-440 kDa separation system. * Non-specific interaction with the 230 kDa Simple Western standard may be seen with this antibody

TNC deficiency reduced kidney fibrosis in animal models. D) Western blot showed that the proteins of collagen Ialpha and alpha-SMA were also significantly reduced in TNC-/- mice at UUO day 7 (C, n = 7, p < 0.05). Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/36522320), licensed under a CC-BY licence.

Immunohistochemistry staining for type I collagen. Immunohistochemical staining targeting type I collagen revealed severe disorganization of the annulus fibrosus (AF), and a decrease in staining intensity for group D. On the contrary, the arc-shaped and layered AF structure with immunoreactivity for type I collagen staining were mostly maintained in group S when compared to group C. Presented images show the AF at site of surgery, defect, and transplant. Abbreviations: D: AF defect only group, S: AF defect treated with sheet transplantation group, C: sham group, NC: negative control of sample stained without primary antibody (scale bar = 300 um) Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31463464), licensed under a CC-BY licence.

Reactivity:

Hu, Mu, Rt, Am, Av, Ma, Sh, Bv, Ca, Ch, Eq, Fe, Av-Bi, Gt, Gp, Ha, Pm, Rb, Xp

Species Glossary

Reactivity: Hu, Mu, Rt, Am, Av, Ma, Sh, Bv, Ca, Ch, Eq, Fe, Av-Bi, Gt, Gp, Ha, Pm, Rb, Xp

Applications:

, , ,

Applications: , , ,

Host:

Rabbit Polyclonal

Host: Rabbit Polyclonal

Sizes:

Sample Size Available

Sizes: Sample Size Available

Conjugate:

Unconjugated

Available Formulations

Formulation	Catalog #	Availability	Price
Azide and BSA Free	NBP1-30054-0.02ml

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NBP2-33006

alpha-Smooth Muscle Actin Antibody (1A4/asm-1) - BSA Free

(2 Reviews)

(51 Publications)

0.1 mg

NBP2-33006

Western blot shows lysates of human heart tissue and iBJ6 human induced pluripotent stem cell line undifferentiated or cardiac differentiated. PVDF membrane was probed with 0.25 ug/mL of Mouse Anti-alpha-Smooth Muscle Actin Monoclonal Antibody (Catalog # NBP2-33006) followed by HRP-conjugated Anti-Mouse IgG Secondary Antibody (Catalog # HAF018). The observed molecular weight was detected for alpha Smooth Muscle Actin at approximately 40 kDa (as indicated). This experiment was conducted under reducing conditions.

Feline tissue stained with alpha-Smooth Muscle Actin Antibody at dilution of 1:600. Vascular wall was stained. IHC image submitted by a verified customer review.

Simple Western lane view shows a specific band for an observed molecular weight at ~45 kDa for alpha-Smooth Muscle Actin in 0.2 mg/ml of h. Aorta lysate. This experiment was performed under reducing conditions using the 12-230 kDa separation system.

An intracellular stain was performed on HeLa cells with NBP2-34522AF700 (blue) and a matched isotype control (orange). Cells were fixed with 4% PFA and then permeabilized with 0.1% saponin. Cells were incubated in an antibody dilution of 10 ug/mL for 30 minutes at room temperature. Both antibodies were conjugated to Alexa Fluor 700.

Canine brain/spinal cord section. Alpha-Smooth Muscle Actin Antibody (1A4/asm-1) staining in red. Endothelial cell marker in green. DAPI in blue. Alexa Fluor conjugated antibodies used for secondary antibodies. IHC image submitted by a verified customer review.

Whole cell lysates from SUM159, MDA-MB-231 and MCF-7 cells were loaded with 50 ug/lane. 10% SDS-PAGE. Alpha-Smooth Muscle Actin antibody (NBP2-33006) was used for primary antibody: 1:1000, 4C, overnight. Image from verified customer review.

M2 macrophage-related protein expression and the co-location of M2-macrophages and GC-MSCs within tumor tissues. Representative immunofluorescence images of the co-location of GC-MSCs (alpha-Smooth Muscle Actin; green) and M2-macrophages (CD204; red) in gastric cancer tissues detected by confocal microscopy. scale bar, 100 um. **P < 0.01 vs. gastric cancer tissue. T: tumor; N: non-cancerous tissues. Image collected and cropped by CiteAb from the following publication (//www.nature.com/articles/s41419-019-2131-y), licensed under a CC-BY license.

An intracellular stain was performed on HeLa cells with alpha-Smooth Muscle Actin Antibody (1A4/asm-1) NBP2-34522APC (blue) and a matched isotype control (orange). Cells were fixed with 4% PFA and then permeabilized with 0.1% saponin. Cells were incubated in an antibody dilution of 1 ug/mL for 30 minutes at room temperature. Both antibodies were conjugated to Allophycocyanin.

Staining of human Leiomyosarcoma statined with the Azide and BSA-free version of alpha-Smooth Muscle Actin Antibody (1A4/asm-1).

An intracellular stain was performed on HeLa cells with alpha-Smooth Muscle Actin Antibody (1A4/asm-1) NBP2-34522AF647 (blue) and a matched isotype control (orange). Cells were fixed with 4% PFA and then permeabilized with 0.1% saponin. Cells were incubated in an antibody dilution of 2.5 ug/mL for 30 minutes at room temperature. Both antibodies were conjugated to Alexa Fluor 647. Image from the Alexa Fluor 647 version of this antibody.

Simple Western lane view shows a specific band for an observed molecular weight for Smooth Muscle Actin in 0.2 mg/ml of h. Uterus lysate. This experiment was performed under reducing conditions using the 12-230 kDa separation system.

Electropherogram image of the corresponding Simple Western lane. alpha-Smooth Muscle Actin antibody was used at 10 ug/ml dilution of h. Aorta and h. Uterus lysates(s) respectively.

M2 macrophage-related protein expression and the co-location of M2-macrophages and GC-MSCs within tumor tissues.c) Representative immumofluoresence images of the co-location of GC-MSCs (alpha-SMA; green) and M2-macrophages (CD204; red) in gastric cancer tissues detected by confocal microscopy. scale bar, 100 um. **P < 0.01 vs. gastric cancer tissue. T: tumor; N: non-cancerous tissues. Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31801938), licensed under a CC-BY licence.

Reactivity:

Hu, Mu, Rt, Po, Bv, Ca, Ch, Fe, Gp, Gt, Pm, Pm, Rb, Sh

Species Glossary

Reactivity: Hu, Mu, Rt, Po, Bv, Ca, Ch, Fe, Gp, Gt, Pm, Pm, Rb, Sh

Applications:

, , , , ,

Applications: , , , , ,

Host:

Mouse Monoclonal

Host: Mouse Monoclonal

Sizes:

Sample Size Available

Sizes: Sample Size Available

Conjugate:

Unconjugated

Available Conjugates:

Conjugate	Catalog #	Availability	Size	Price
Alexa Fluor 350	NBP2-33006AF350
Alexa Fluor 405	NBP2-34522AF405
Alexa Fluor 488	NBP2-34522AF488
Alexa Fluor 532	NBP2-33006AF532
Alexa Fluor 594	NBP2-33006AF594
Alexa Fluor 647	NBP2-34522AF647
Alexa Fluor 700	NBP2-34522AF700
Alexa Fluor 750	NBP2-33006AF750
Allophycocyanin	NBP2-34522APC
Biotin	NBP2-34522B
DyLight 350	NBP2-34522UV
DyLight 405	NBP2-34522V
DyLight 488	NBP2-34522G
DyLight 550	NBP2-34522R
DyLight 594	NBP2-33006DL594
DyLight 650	NBP2-34522C
DyLight 680	NBP2-34522FR
DyLight 755	NBP2-34522IR
FITC	NBP2-34522F
HRP	NBP2-34522H
Janelia Fluor 549	NBP2-34522JF549
Janelia Fluor 646	NBP2-34522JF646
PE	NBP2-34522PE
PerCP	NBP2-34522PCP

Available Formulations

Formulation	Catalog #	Availability	Price
BSA Free	NBP2-33006-0.2mg
BSA Free	NBP2-33006-0.02mg
Azide and BSA Free	NBP2-34522-0.2mg
Azide and BSA Free	NBP2-34522-0.1mg

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NB100-1992

SOD2/Mn-SOD Antibody

(42 Publications)

0.05 mg

NB100-1992

Western Blot: SOD2/Mn-SOD Antibody [NB100-1992] - Western blot analysis of Rat Tissue lysates showing detection of SOD2/Mn-SOD protein using Rabbit Anti-SOD2/Mn-SOD Polyclonal Antibody (NB100-1992). Load: 15 ugprotein. Block: 1.5% BSA for 30 minutes at RT. Primary Antibody: Rabbit Anti-SOD2/Mn-SOD Polyclonal Antibody (NB100-1992) at 1:1000 for 2 hours at RT. Secondary Antibody: Donkey Anti-Rabbit IgG: HRP for 1 hour at RT.

Immunocytochemistry/Immunofluorescence: SOD2/Mn-SOD Antibody [NB100-1992] - Analysis using Rabbit Anti-SOD (Mn) Polyclonal Antibody. Tissue: HeLa Cells. Species: Human. Fixation: 2% Formaldehyde for 20 min at RT. Primary Antibody: Rabbit Anti-SOD (Mn) Polyclonal Antibody at 1:120 for 12 hours at 4 degrees C. Secondary Antibody: APC Goat Anti-Rabbit (red) at 1:200 for 120 min at RT. Counterstain: DAPI (blue) nuclear stain at 1:40000 for 120 min at RT. Localization: Mitochondrion matrix. Magnification: 20x. (A) DAPI (blue) nuclear stain. (B) Anti-SOD (Mn) Antibody. (C) Composite.

Immunohistochemistry: SOD2/Mn-SOD Antibody [NB100-1992] - Immunohistochemistry analysis using Rabbit Anti-SOD2/Mn-SOD Polyclonal Antibody (NB100-1992). Tissue: backskin. Species: Mouse. Fixation: Bouin's Fixative Solution. Primary Antibody: Rabbit Anti-SOD2/Mn-SOD Polyclonal Antibody (NB100-1992) at 1:100 for 1 hour at RT. Secondary Antibody: FITC Goat Anti-Rabbit (green) at 1:50 for 1 hour at RT. Localization: Mitochondrion matrix.

The effects of a high calcium/phosphate diet, of 1,25(OH)2D3, and of antioxidant supplementation on oxidative stress, DNA damage, and protein expression of oncogenes and tumor suppressive genes in 1alpha(OH)ase-/- mice. Mice from each group were treated as described in Figure 1. Representative micrographs of skin sections stained immunohistochemically for (d) SOD2 and (f) gamma-H2AX. Scale bars represent 50 um in d and f. Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/30907059), licensed under a CC-BY licence.

CAV-1 preserves mitochondrial respiratory function through regulation of OXPHOS expression. (C) Representative immunoblot displaying levels of CAV-1, CyPA, mitochondrial biogenesis markers, and antioxidant enzymes in the NC, HC, and HCAV-1 groups. Image collected and cropped by CiteAb from the following publication (//dx.plos.org/10.1371/journal.pone.0154210), licensed under a CC-BY licence.

IHC-P analysis of hOGG1 protein expression in serous ovarian cancer: (A) Normal ovarian tissue treated with anti-hOGG1 antibody, biotinylated anti-rabbit IgG secondary antibody, and avidin-biotin-peroxidase complex, and counterstained with p-dimethylaminobenzaldehyde reagent (magnification 100 x); (B) serous cystadenoma with positive staining (magnification 200 x); (C) LG-SOC tissue with moderate positive staining (magnification 200 x); and (D) HG-SOC with negative staining (magnification 200 x). Black arrow pointed at the immunostained epithelial cells. Image collected and cropped by CiteAb from the following open publication (//ovarianresearch.biomedcentral.com/articles/10.1186/1757-2215-6-74), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

$BRCA2 deficiency causes DNA under replication that results in abnormal mitoses. a–cBRCA2∆Ex3-4/– cells were released for 22 h from serum starvation to increase mitotic cells, incubated with EdU for 1 h, and then analyzed for mitotic DNA synthesis. Early mitotic cells defined as being in prophase, prometaphase, or metaphase were analyzed for EdU foci that co-localize with FANCD2 foci pairs. a Representative images of mitotic DNA synthesis. Scale bars 10 µm. b Percent early mitotic cells containing EdU foci, analyzed by an unpaired two-tailed t-test. n = 3. c FANCD2 foci pairs with or without EdU foci co-localization. Graphs represent the pooled results of three independent experiments, each analyzed by a two-tailed Mann–Whitney test. Median FANCD2 foci pair number, red bars. d FANCD2 foci pair analysis in early mitotic cells. Cells were untreated, or treated with the CDK1 inhibitor RO-3306 (10 µM, 24 h) to delay mitotic entry, and released for 1 h before analysis of FANCD2 foci pairs in early mitotic cells. Analysis is by an unpaired two-tailed t-test. n = 4. e–h Anaphase cells were analyzed for DAPI bridges (e, g) and lagging chromosomes (f, h). RO-3306 treatment (10 µM, 24 h with release for 1 h) was applied where indicated. Representative deconvolved images are shown on the left of e and f. n = 3. Statistical analysis was by an unpaired two-tailed t-test. FD2, FANCD2. Scale bars 10 µm. i, j. 53BP1 nuclear body analysis with RO-3306 (10 µM, i) or nocodazole (100 ng ml−1, j) treatment and released as in the schematic on the left. The fraction of EdU+ cells in G1 at the time of harvest that contains ≥3 53BP1 nuclear bodies (NBs) is shown in the graph on the right. Analysis is by an unpaired two-tailed t-test. n ≥ 3. Error bars s.d. ns, not significant; *p 0.9999, ****P < 0.0001 with 95% confidence interval. n = 75 (wildtype), 48 (R57D), 74 ( delta 143-144), 53 (R57D/ delta 143-144) over 3 independent experiments. Source data are provided as Source Data file. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/32424115), licensed under a CC-BY license. Not internally tested by Novus Biologicals.$

Reactivity:

Hu, Mu, Rt, Po, Bv, Ca, Ch, Dr, Gp, Gt, Ha, Pm, Rb, Sh, Sq, Xp

Species Glossary

Reactivity: Hu, Mu, Rt, Po, Bv, Ca, Ch, Dr, Gp, Gt, Ha, Pm, Rb, Sh, Sq, Xp

Applications:

, , , ,

Applications: , , , ,

Host:

Rabbit Polyclonal

Host: Rabbit Polyclonal

Sizes:

Sample Size Available

Sizes: Sample Size Available

Conjugate:

Unconjugated

Validated by:

Validated by:

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NBP1-30042

Periostin/OSF-2 Antibody - C-terminus - Azide and BSA Free

(2 Reviews)

(36 Publications)

0.1 ml

NBP1-30042

Immunohistochemistry: Periostin/OSF-2 Antibody - C-terminus - Azide and BSA Free [NBP1-30042] - Analysis of periostin in rabbit periosteum. Image courtesy of product review submitted by Samer Zaky.

Western Blot: Periostin/OSF-2 Antibody - C-terminus - Azide and BSA Free [NBP1-30042] - Rat lung lysate showing specific immunolabeling of the ~ 93 kDa periostin protein doublet.

Western Blot: Periostin/OSF-2 Antibody - C-terminus - Azide and BSA Free [NBP1-30042] - Cardiac muscle phenotypes of mice at 12 weeks of age. Western blot analyses of periostin. The graph shows the quantification of periostin levels normalized to GAPDH (n = 3). Image collected and cropped by CiteAb from the following publication (dx.plos.org/10.1371/journal.pone.0221512), licensed under a CC-BY license.

Immunocytochemistry/Immunofluorescence: Periostin/OSF-2 Antibody - C-terminus - Azide and BSA Free [NBP1-30042] - Cardiac muscle phenotypes of mice at 12 weeks of age. Immunostaining of laminin a2 (green) and periostin (red) with DAPI (blue) from cardiac muscle. Image collected and cropped by CiteAb from the following publication (dx.plos.org/10.1371/journal.pone.0221512), licensed under a CC-BY license.

<b>Genetic Strategies Validation. </b>Immunohistochemistry: Periostin/OSF-2 Antibody - C-terminus - Azide and BSA Free [NBP1-30042] - Representative IHC images from 3 separate hearts analyzed for Periostin/OSF-2 protein expression within the infarct region of hearts from Postn^MCM/+; R26^EGFP mice versus Postn^MCM/MCM; R26^EGFP mice 2 weeks after MI. Nuclei are shown with DAPI (blue). Scale bars: 20 um. Postn lineage-traced cells (EGFP+) cells are also shown. Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/29664017/) licensed under a CC-BY license.

Knockout Validated: Periostin/OSF-2 Antibody - C-terminus - Azide and BSA Free [NBP1-30042] - Loss of Tgfbi does not alter disease progression after MI. Western blot analysis for TGFBI and periostin from isolated infarct areas of the hearts of the indicated groups of mice 7 days after MI. GAPDH was used as a loading control. Image collected and cropped by CiteAb from the following publication (journals.plos.org/plosone/article?id=10.1371/journal.pone.0181945), licensed under a CC-BY license.

Effect of ECM maturation on alphaSMA expression in myofibroblasts. (D) Representative IHC images from 3 separate hearts analyzed for Postn protein expression within the infarct region of hearts from PostnMCM/+;R26EGFP mice versus PostnMCM/MCM;R26EGFP mice 2 weeks after MI. Nuclei are shown with DAPI (blue). Scale bars: 20 um. Postn lineage-traced cells (EGFP+) cells are also shown. (E) Representative IHC images from 3 separate hearts analyzed showing alphaSMA+ (red) and Postn lineage-traced (EGFP+) fibroblasts in the infarct region of hearts from PostnMCM/+;R26EGFP mice and PostnMCM/MCM;R26EGFP mice 2 weeks after MI. Nuclei are shown with DAPI (blue). Scale bars: 50 um. Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/29664017), licensed under a CC-BY licence.

Selective addiction of EOC to the SIX4 homeobox transcription factorImmunoblots indicate miR‐124‐induced SIX4 depletion. siSIX4 is shown as an antibody control.Consequence of SIX4 depletion on EOC cell viability (as in Fig 2A, N, normal cell lines: HOSE, HBEC30).In vivo knockdown of SIX4 using neutral liposome‐incorporated siRNA reduced tumor burden and ascites volume in an orthotopic xenograft mouse model. Box‐and‐whisker plot of tumor weight (left panel) or ascites volume (right panel) from n = 7 or 8 mice per condition as indicated. *P‐value from Student's t‐test.Consequence of SIX4 depletion in PEO1 cells on E‐cadherin plasma membrane accumulation 48 h after transfection. Cells were counterstained with phalloidin and DAPI.Immunoblots indicate consequence of SIX4 depletion on LKB1 accumulation and AMPK pathway activation.Source data are available online for this figure. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/26655797), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Both regorafenib and SC-78 targeted autocrine and paracrine regulation of VEGF-A in TNBCs.(A) Cells were treated with SC-78 or regorafenib for 24 h. After that, the medium was replaced with fresh medium and incubated for another 24 h. Then, the medium was collected and ELISA was used to measure the VEGF-A level in the CM harvested from TNBC cells w/wo treatment of SC-78 or regorafenib. *p < 0.05, **p < 0.01. (B) Top, For IP-western assay, MDA-MB-231 cells were incubated with CM for 24 h and total lysate was immunoprecipitated using anti-NRP-1 antibody, and western blotting was performed using the indicated antibodies. Bottom, the methods to collect CM described above were followed, and the VEGF165 recombinant protein was re-added into CM harvested from MDA-MB-231 cells w/wo treatment of SC-78 or regorafenib for 24 h, then cells were further analyzed by IP-western assay. (C) The co-localization of VEGF-A (green) and NRP-1 (red) in MDA-MB-231 cells treated with CM harvested from MDA-MB-231cells w/wo treatment of SC-78 or regorafenib was examined under a confocal microscope after immunofluorescent staining. DAPI stains the nuclei. (D) Left, MDA-MB-231 cells were seeded and treated with VEGF165 at the indicated concentration (upper chamber of the Transwell plate). The migrated cells were stained with DAPI and counted after 18 h by immunofluorescence microscope. MDA-MB-231 cells were exposed to regorafenib (middle) or SC-78 (right) w/wo the addition of VEGF165. Cells were subjected to Transwell migration assay as mentioned above. *p < 0.05, **p < 0.01. (E) CM was harvested from TNBC cells w/wo treatment of regorafenib or SC-78. EA.hy926 cells (5 × 104) in CM were seeded and tube-formation ability was examined after incubation for 24 h. (F) For DIVAA, mice were implanted with silicone tubes containing Matrigel and supplemented with angiogenic factors and CM harvested from cells treated with various doses of regorafenib or SC-78 (n = 3). Neovascularization in the angioreactors was quantified using a spectrofluorometer 14 days after implantation. *p < 0.05, **p < 0.01. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/27364975), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Analysis of phosphorylated P-IKK alpha , and human and mouse IKK alpha in tumors of the three groupsA, D, G. P-IKK alpha expression. P-IKK alpha / beta (Ser 180/Ser 181) antibody is used. B, E, H. Specific staining of human IKK alpha -using the NB100-56704 antibody. C, F, I. Staining with the sc-7182 antibody that recognizes both human and mouse IKK alpha . Observe that as expected, in the N-IKK alpha tumors the signal of this antibody is detected both in cytoplasmic and nuclear localization; by contrast, in the Control tumors the endogenous IKK alpha is mainly observed in the cytosolic compartment, although some nuclear staining is also observed. In the C-IKK alpha tumors little nuclear staining is observed. Scale bar: 70μm. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/27121058), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

ER stress is induced by OGR1 via IRE1 alpha /JNK signalling. (A) Caco-2 cells were subjected to different pH medium, with or without an OGR1 inhibitor (10 µM), following 4–6 h in pH 7.6 serum free medium. After 24 h pH shift, total protein was isolated and Western blot performed. Results are representative of two independent experiments. (B) Caco-2 cells were subjected to different pH medium After 24 h pH shift, total protein was isolated and Western blot performed. Results are representative of two independent experiments. (C) Caco-2 cells were subjected to different pH medium with or without a JNK inhibitor (10 µM) following 4–6 h in pH 7.6 serum free medium. After 24 h pH shift, total protein was isolated and Western blot performed. Results are representative of two independent experiments. (D) Caco-2 cells were starved and subjected to an acidic pH with or without a JNK inhibitor as described in (C). After 24 h pH shift, total RNA was isolated and mRNA expression was investigated by qPCR. Statistical analysis was performed using one-way ANOVA followed by Tukey’s post-test. Data are presented as means ± SE of three independent experiments (***p < 0.001). (E) Caco-2 cells were starved and subjected to different pH medium following 4–6 h in pH 7.6 serum free medium. After 24 h pH shift, total protein was isolated and co-IP using IRE1 alpha antibody and JNK antibody was performed, followed by immunoblotting. Results are representative of two independent experiments. pH conditions: High pH 7.5–7.8; Normal pH 7.2–7.4; Low pH 6.6–6.8. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/31996710), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Thapsigargin treatment induces calpain activation and autophagy. (A) Control and shCAPNS1 cells were treated with 100 nM thapsigargin for 10, 20 and 30 min and the lysates subjected to western blot analysis to quantify the precursor and active form of CAPN1. The ratio between active CAPN1 and tubulin is reported below each lane. (B) Time course measurement of intracellular calcium concentration. The plot indicates the ratio of mean Indo Violet/Indo Blue emission values of each cell population at individual time points (minutes). The ratio corresponds to the relative calcium concentration of control and shCAPNS1 U2OS cells before and after addition of thapsigargin (100 nm final). Moving average was used as smoothing method. (C) shCAPNS1 cells were treated with 100 nM thapsigargin for 30, 60 and 120 min and the lysates subjected to western blot analysis to detect LC3, p62, pIRE, CAPNS1 and tubulin. (D) Levels of p62 and LC3 normalized to tubulin levels. Image collected and cropped by CiteAb from the following open publication (//journals.biologists.com/bio/article/doi/10.1242/bio.022806/256614/Calpain-mobilizes-Atg9-Bif-1-vesicles-from-Golgi), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

DSC restores redox balance in colonic tissues. A, Colitis was induced as described in Materials and Methods and treated with or without DSC (50 mg/kg). Representative bands and densitometry analysis of Nrf2 nuclear translocation and HO‐1 expression in colonic tissues. Histone H3 and beta ‐actin were used as loading control, respectively. B, Colitis was induced as described in Materials and Methods and treated with lentiviral Nox4 shRNA or lentiviral scrambled shRNA. Representative bands and densitometry analysis of Nrf2 nuclear translocation and HO‐1 expression in colonic tissues. Histone H3 and beta ‐actin were used as loading control, respectively. BMDM was stimulated with or without DSC (50 μmol/L) as described in Materials and Methods. C, Representative bands and densitometry analysis of Nox4. beta ‐actin was used as loading control. D, Representative bands and densitometry analysis of Nrf2 nuclear translocation and cytoplasmic HO‐1 expression in BMDM. beta ‐actin or histone H3 was used as loading control. Data shown are means ± SEM of n = 8 in each group. *P < 0.05 vs Control cell or mice (CTL), #P < 0.05 vs DSS‐treated mice or LPS‐stimulated cells Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/32945118), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Reactivity:

Hu, Mu, Rt, Ch, Bv, Ca, Eq, Fe, Av-Bi, Gt, Gp, Ha, Pm, Rb, Sh

Species Glossary

Reactivity: Hu, Mu, Rt, Ch, Bv, Ca, Eq, Fe, Av-Bi, Gt, Gp, Ha, Pm, Rb, Sh

Applications:

, , ,

Applications: , , ,

Host:

Rabbit Polyclonal

Host: Rabbit Polyclonal

Sizes:

Sample Size Available

Sizes: Sample Size Available

Conjugate:

Unconjugated

Validated by:

Validated by:

Available Formulations

Formulation	Catalog #	Availability	Price
Azide and BSA Free	NBP1-30042SS

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HAF019

Chicken anti-Goat IgG Secondary Antibody [HRP]

(1 Review)

(37 Publications)

1 mL

HAF019

Western blot shows detection of Goat Anti-Human/Mouse/Rat Carboxylesterase 1/CES1 Polyclonal Antibody (AF4920) using a 1:1000 dilution of HRP-conjugated Anti-Goat IgG Secondary Antibody (Catalog # HAF019). This experiment was conducted under reducing conditions and using Immunoblot Buffer Group 1.

Detection of Vimentin in human kidney using 5 ug/mL of Goat anti-human Vimentin primary antibody (AF2105) followed by 30 min incubation with Donkey Anti-Goat HRP conjugated secondary antibodies (Catalog# HAF019) at 1:20 dilution + DAB chromogen (brown). The tissue was counterstained with Hematoxylin (blue). Control was done by omitting primary antibody.

Reactivity:

Gt

Species Glossary

Reactivity: Gt

Applications:

,

Applications: ,

Host:

Chicken Polyclonal

Host: Chicken Polyclonal

Conjugate:

HRP

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Category

Protein/Target

Applications

Reactivity

Citation

Antibody Validation

Reviews

Host

Available Conjugates

Format

Marker

Modification

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Clone

Gene Symbol

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Promotional Item

Species Glossary

53BP1 Antibody - BSA Free

Goat IgG Isotype Control [Unconjugated]

HIF-1 alpha Antibody - BSA Free

IRE1 alpha [p Ser724] Antibody - BSA Free

HIF-1 alpha Antibody

PGC1 alpha Antibody - BSA Free

alpha Tubulin Antibody (DM1A) - BSA Free

Collagen I alpha 1 Antibody - Azide and BSA Free

alpha-Smooth Muscle Actin Antibody (1A4/asm-1) - BSA Free

SOD2/Mn-SOD Antibody

Periostin/OSF-2 Antibody - C-terminus - Azide and BSA Free

Chicken anti-Goat IgG Secondary Antibody [HRP]

At	=	A. thaliana	SyHa	=	Golden Syrian Hamster
All	=	All Species	Ha	=	Hamster
An	=	Animal	Hu	=	Human
ArHa	=	Armenian Hamster	I	=	Insect
Av	=	Avian	Ll	=	Llama
Bb	=	Baboon	Ma	=	Mammal
Ba	=	Bacteria	Mk	=	Monkey
Bv	=	Bovine	Mu	=	Mouse
Ca	=	Canine	Multi	=	Multi-species
Ce	=	C. Elegans	NA	=	Non-species specific
Ch	=	Chicken	Or	=	Orangutan
ChHa	=	Chinese Hamster	Pl	=	Plant
Cm	=	Cynomolgus Monkey	Pm	=	Primate
Do	=	Donkey	Po	=	Porcine
Dr	=	Drosophilia	Rb	=	Rabbit
Ec	=	E. Coli	Rt	=	Rat
Eq	=	Equine	RM	=	Rhesus Macaque
Fe	=	Feline	Sh	=	Sheep
Ft	=	Ferret	Vb	=	Vertebrate
Fi	=	Fish	Vi	=	Virus
Fu	=	Fungi	Xp	=	Xenopus
Ge	=	Gerbil	Ye	=	Yeast
GP	=	Guinea Pig	Ze	=	Zebrafish
Gt	=	Goat