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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

compare

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

NB100-305

53BP1 Antibody - BSA Free

(6 Reviews)

(139 Publications)

0.1 mg

NB100-305

<b>Biological Strategies Validation. </b>Immunocytochemistry/Immunofluorescence: 53BP1 Antibody - BSA Free [NB100-305] - 53BP1 Antibody [NB100-305] - Exosomes modulate the repair of DNA DSBs in irradiated recipient cells. Representative images of 53BP1 foci in BHY cells 6 hours after 2 Gy and transfer of BHY exosomes isolated 24 hours after irradiation with 0, 3, 6 or 9 Gy (53BP1 foci green, nuclei blue). Image collected and cropped by CiteAb from the following publication (//dx.plos.org/10.1371/journal.pone.0152213), licensed under a CC-BY license.

Immunohistochemistry: 53BP1 Antibody [NB100-305] - Immunohistochemical staining of placental villi with 53BP1 Antibody (Catalog #NB100-305) at 40X magnification.

Western Blot: 53BP1 Antibody [NB100-305] - Western blot of whole cell lysate (20 ug/lane) from U2Os cells resolved on a 3 to 8 percent trisacetate gel. A band appears at approximately the theoretical molecular weight of 214 kDa.

Immunocytochemistry/Immunofluorescence: 53BP1 Antibody [NB100-305] - HCC1937 cells (human) were treated with PARPi for 96 h. Nuclei are stained in blue (DAPI) and 53BP1 antibody (foci in green). ICC/IF image submitted by a verified customer review.

Flow Cytometry: 53BP1 Antibody [NB100-305] - An intracellular stain was performed on Ntera2 cells with 53BP1 Antibody NB100-305 (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).

Immunocytochemistry/Immunofluorescence: 53BP1 Antibody [NB100-305] - Paraformaldehyde (4%) fixed Saos-2 cells (human osteosarcoma cell line) were stained with anti-53BP1 antibody followed by Alexa Fluor 488 secondary antibody. ICC/IF image submitted by a verified customer review.

Immunocytochemistry/Immunofluorescence: 53BP1 Antibody [NB100-305] - 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- NB100-305 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.

Flow Cytometry: 53BP1 Antibody [NB100-305] - An intracellular stain was performed on HeLa cells with 53BP1 Antibody (Catalog #NB100-305AF488) (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 488.

Inhibition of ACLY exacerbates radiation induced DNA damage in HNSCC cells and impairs homologous recombination. (C,D) Quantification of cells positive for 53BP1 foci (>5 53BP1 foci/nucleus in a single plane of view) in UM-SCC-6 (C) and UT-SCC-5 (D) cells. Shown are mean percentages of three biological replicates. Immunofluorescent representative images of examples of UM-SCC-6 or UT-SCC-5 cells, 24 h post irradiation, with or without 5 uM BMS303141 pre-treatment. Nuclei in blue, 53BP1 foci in red. Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31817870), licensed under a CC-BY licence.

Exosomes modulate the repair of DNA DSBs in irradiated recipient cells. (B) Representative images of 53BP1 foci in BHY cells 6 hours after 2 Gy and transfer of BHY exosomes isolated 24 hours after irradiation with 0, 3, 6 or 9 Gy (53BP1 foci green, nuclei blue). Image collected and cropped by CiteAb from the following publication (//dx.plos.org/10.1371/journal.pone.0152213), licensed under a CC-BY licence.

$RAP1 protects telomeres against DNA damageWestern blotting showing the expression of RAP1 and TRF2 in MRC-5 cells of different population doublings (PD). Senescent cells (PD 72) were left in culture for at least 4 weeks before harvesting for analysis.ChIP analysis of young (PD 30) and senescent (PD 72) MRC-5 cells performed with either anti-RAP1, anti-TRF2, or an IgG antibody. The immunoprecipitated and input products were loaded into a slot blot membrane and hybridized with a telomere probe, and stripped and hybridized to an Alu probe in order to determine unspecific binding. Quantification was performed by normalizing the telomere signal of the immunoprecipitated to that of the input. Data represent mean +/- SD of three biological replicates.Immunofluorescence detection of 53BP1 (red) and a FISH probe staining telomeres (green) in young (PD 26), pre-senescent (PD 66), and senescent (PD 72 + 4 weeks) MRC-5 fibroblasts. The upper graph shows the percentage of telomere co-localizing with 53BP1 (TIFs). Total DNA damage was measured by immunofluorescence detection of 53BP1. The lower graph shows the total number of 53BP1 foci per nucleus. Approximately 40-50 cells were analyzed per replicate and per condition. Bars represent SEM of two biological replicates.Data information: Statistical analyses were performed using Mann-Whitney U-test (*P 0.05, n = 18; group (mean % of cells with more than five 53BP1 ionizing radiation-induced foci +/−SE); unpaired t test]. See text for details. (C) 53BP1 accumulates at infrequent endogenous chromosomal breaks (indicated by asterisks; no ionizing radiation treatment) in presence or absence of TPX2. (D) Cell cycle profiles of control and TPX2 miRNA expressing HeLa cell cultures obtained via flow cytometry (n = 2). Note that the slight ∼5% increase in the G2/M fraction upon TPX2 depletion can not account for the defect in 53BP1 ionizing radiation-induced foci formation exhibited by ∼55% of TPX2 miRNA expressing cells. See text for details. Error bars represent SE in (B) and SDEV in (D). n = # of independent experiments; NS: non-significant, * p<0.05, ** p<0.01, *** p<0.001; IR: ionizing radiation. Image collected and cropped by CiteAb from the following open publication (//dx.plos.org/10.1371/journal.pone.0110994), licensed under a CC-BY license. Not internally tested by Novus Biologicals.$

Hypoxia, blood vessel and proliferation staining. IHC staining in the Biopsy 23 and Biopsy 3 respectively for CA-9, EF5, CD31, Ki67 and LYVE1. 15× Magnification. Image collected and cropped by CiteAb from the following open publication (//www.mdpi.com/2072-6694/4/3/821), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Reactivity:

Hu, Mu, Rt, Bt, Bv, Ca, Nm, Po, Pm, Eq, Fe, Ha, Pm-Or, Pm, Rb, Sh

Species Glossary

Reactivity: Hu, Mu, Rt, Bt, Bv, Ca, Nm, Po, Pm, Eq, Fe, Ha, Pm-Or, Pm, 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	NB100-305AF350
Alexa Fluor 405	NB100-305AF405
Alexa Fluor 488	NB100-305AF488
Alexa Fluor 532	NB100-305AF532
Alexa Fluor 594	NB100-305AF594
Alexa Fluor 647	NB100-305AF647
Alexa Fluor 700	NB100-305AF700
Alexa Fluor 750	NB100-305AF750
Allophycocyanin	NB100-305APC
Biotin	NB100-305B
DyLight 350	NB100-305UV
DyLight 405	NB100-305V
DyLight 488	NB100-305G
DyLight 550	NB100-305R
DyLight 594	NB100-305DL594
DyLight 650	NB100-305C
DyLight 680	NB100-305FR
DyLight 755	NB100-305IR
FITC	NB100-305F
HRP	NB100-305H
Janelia Fluor 549	NB100-305JF549
Janelia Fluor 646	NB100-305JF646
PE	NB100-305PE
PerCP	NB100-305PCP
mFluor Violet 450 SE	NB100-305MFV450
mFluor Violet 500 SE	NB100-305MFV500
mFluor Violet 610 SE	NB100-305MFV610

Available Formulations

Formulation	Catalog #	Availability	Price
BSA Free	NB100-305SS

compare

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

NB100-904

53BP1 Antibody - BSA Free

(4 Reviews)

(120 Publications)

0.1 ml

NB100-904

Immunohistochemistry: 53BP1 Antibody - BSA Free [NB100-904] - Staining of 53BP1 in human renal cancer cells using DAB with hematoxylin counterstain.

Flow Cytometry: 53BP1 Antibody - BSA Free [NB100-904] - An intracellular stain was performed on Ntera2 cells with 53BP1 Antibody NB100-904 (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).

Western Blot: 53BP1 Antibody - BSA Free [NB100-904] - Western blot analysis of untreated U2OS cell lysate blotted with 53BP1 Antibody. The observed molecular weight here is ~220 kDa, and the theoretical molecular weight is 214 kDa.

<b>Biological Strategies Validation. </b>Immunocytochemistry/Immunofluorescence: 53BP1 Antibody - BSA Free [NB100-904] - AR suppression treatment suppresses DNA damage repair. (A) Cells were treated with AR suppression for 24 h followed by 2 Gy of IR treatment. Representative images of phospho-H2A histone family member X ( -H2AX) and p53-binding protein 1 (53BP1) staining 24 h post-IR of LNCaP cells (scale bar 10 um). Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31635359/) licensed under a CC-BY license.

Immunocytochemistry/Immunofluorescence: 53BP1 Antibody - BSA Free [NB100-904] - Immunofluorescence of 53BP1 Antibody in HeLa cells. Image from verified customer review.

Immunocytochemistry/Immunofluorescence: 53BP1 Antibody - BSA Free [NB100-904] - Immunofluorescence of 53BP1 Antibody in C33A cells. Image from verified customer review.

Immunocytochemistry/Immunofluorescence: 53BP1 Antibody - BSA Free [NB100-904] - HeLa cells were fixed for 10 minutes using 10% formalin and then permeabilized for 5 minutes using 1X PBS + 0.5% Triton X-100. The cells were incubated with 53BP1 Antibody conjugated to Alexa Fluor 488 (Catalog #NB100-904AF488) at 10ug/mL for 1 hour at room temperature. Nuclei were counterstained with DAPI (Blue). Cells were imaged using a 40X objective.

Immunocytochemistry/Immunofluorescence: 53BP1 Antibody - BSA Free [NB100-904] - 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 NB100-904 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.

Flow Cytometry: 53BP1 Antibody - BSA Free [NB100-904] - An intracellular stain was performed on HeLa cells (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 DyLight 550.

Flow Cytometry: 53BP1 Antibody - BSA Free [NB100-904] - An intracellular stain was performed on HeLa cells with 53BP1 Antibody (Catalog #NB100-904AF647) (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.

Flow Cytometry: 53BP1 Antibody - BSA Free [NB100-904] - An intracellular stain was performed on HeLa cells with 53BP1 Antibody (Catalog #NB100-904C) (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 DyLight 650.

Cellular RER and not enzyme activity against RNA:DNA hybrids correlates with DNA damage and proinflammatory responseAOverexpression of RNase H1 in Rnaseh2b-/- cells restores RNase H activity against RNA:DNA hybrids to 81 +/- 10% of wild-type levels, while overexpression of RNASEH2B restores cellular enzyme activity for cleavage of both RNA:DNA and DRD:DNA substrates (RER). Rnaseh2b-/- MEFs were complemented with Rnaseh1 (+H1), Rnaseh2b (+H2B) or EGFP by retroviral infection. Mean of n = 3 independent experiments +/- SEM.B, CDNA damage is reduced to wild-type levels by complementation with Rnaseh2b but not Rnaseh1, measured by 53BP1 foci formation in detergent-extracted fixed cells. (B) Representative images (scale bar, 10 um). (C) At least 150 cells were counted for each cell line in three independent experiments. Mean +/- SEM, ****P =10 53BP1 foci with the error bars depicting the s.d. (n = 4). e HeLa cells were transfected with siRNA for 8 h; followed by transfection with the GFP plasmids indicated for another 16 h; irradiated with 2 Gy; and after 24 h of recovery, immunostained for gammaH2AX. The graph shows the percentage of 100 GFP-transfected cells in each experiment whose nuclei contained >=10 gammaH2AX foci with the error bars depicting the s.d. (n = 3). *p < 0.05, **p < 0.01, ns (not significant) as determined by Student's t-test. Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/32303682), licensed under a CC-BY licence.

AR suppression treatment suppresses DNA damage repair. (A) Cells were treated with AR suppression for 24 h followed by 2 Gy of IR treatment. Representative images of phospho-H2A histone family member X (gamma-H2AX) and p53-binding protein 1 (53BP1) staining 24 h post-IR of LNCaP cells (scale bar 10 um). Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31635359), licensed under a CC-BY licence.

hWDR76 interaction network and subnuclear localization suggest conservation of Cmr1 function.(c) Human WDR76 localizes into nuclear foci. Twenty-four hours after GFP-WDR76 transfection, U2OS cells were treated with 10 uM MG132 or 1.5 mM MMS for 2 h. Immunofluorescence analyses of 53BP1 were performed with anti-53BP1 antibody. DAPI was used to stain nuclei. Scale bar, 20 um. Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/25817432), licensed under a CC-BY licence.

NF kappa B upregulates human PINK1 gene expression. (A) NF kappa B increases the endogenous human PINK1 mRNA level. HEK293 cells were transfected with either the NF kappa B expression vector or empty vector pMTF. RT-PCRs were performed using either primers specific to the human PINK1 coding sequence or the human beta -actin coding sequence. (B) NF kappa B increases the endogenous human PINK1 protein levels. HEK293 cells transfected with NF kappa B were harvested 48 h after transfection for protein detection. Cell lysates were run on 10% glycine gel and images were collected by Licor. A significant increase of endogenous PINK1 was observed. (C) The endogenous human PINK1 protein level was dramatically increased by NF kappa B in SH-SY5Y cells. SH-SY5Y cells were transfected with NF kappa B p65 plasmids or the control vector pMTF and then harvested for protein detections. The human PINK1 protein and its proteolysis products ∆1-PINK1 (55kD) and ∆2-PINK1 (45kD) were all increased. beta -actin acted as the internal control. (D) LPS treatment facilitated PINK1 expression in SH-SY5Y cells. Cells were harvested after being treated for 16 h and then subjected to Western blot. The human beta -actin level was served as a control. Quantification was performed by Image J software. Values indicate means ± SEM. n = 3, *p <0.01 by Student’s t-test. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/25108683), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Initial characterization of the OS-9 protein.(A) OS-9 expression in various human cell lines. Equal protein amounts of total cell lysates were used for SDS-PAGE and subsequent Western blotting. For each cell line, two independent samples are shown. Endogenous OS-9 was detected with a polyclonal antibody raised against a peptide corresponding to amino acids 600–667 of isoform 1 of OS-9. (B) Protein stability assay of endogenous OS-9. U2OS cells were treated with the translational inhibitor cycloheximide (100 µM). At indicated time points, whole cell lysates were analysed by immunoblotting. (C) Effect of hypoxia on OS-9 expression. For hypoxia, UT-7 cells were exposed to 1% O2 for 24 h prior to Western blot analysis. To determine any influence of HIF-1 alpha on OS-9 expression under normoxia, cells were incubated with the prolyl hydroxylase inhibitor DMOG (0.5 mM) for 24 h. (D) Protein interaction between OS-9 and PHD2 in vitro. For co-immunoprecipitation, U2OS cells were transiently co-transfected with the plasmids pOS-9-V5 and pPHD2-His, lysed in NP40 buffer, and subjected to immunoisolation with anti-V5 antibody recognizing OS-9 by its V5-tag. OS-9 and its associated proteins were separated by SDS-PAGE and analyzed by Western blot (lane 2). As controls, samples of untransfected (lane 1) cells or cells transfected with a single plasmid (lanes 3–4) were loaded. Representative Western blots are shown for each subfigure. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/21559462), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

PHD3 depletion stabilizes hypoxic p27 expression by increasing p27 half-life. a Cell cycle arrest at G0 and subsequent release shows an increase of p27 expression in siPHD3 exposed cells. b Quantification for p27 expression under PHD3 depletion at indicated time points after cell cycle release in HeLa and 786-O cells. Asterisk indicates significant difference (p < 0,05; n = 3). c Cell cycle arrest at G0 and inhibition of protein synthesis with cycloheximide indicate increased p27 stability in PHD3 depleted HeLa cells. d Quantification of p27 expression using siPHD3 or control at indicated time points. Four independent experiments (± SEM) are shown (p < 0,05; n = 4). e Analysis of p27 stability in 786–0 cells by cycloheximide chase during reoxygenation after 24 h hypoxia demonstrates markedly increased half-life of p27 upon PHD3 depletion Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/26223520), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

$LRRK2 inhibition does not reduce insoluble alpha -synuclein in wildtype hippocampal neurons. a Primary hippocampal neurons from CD1 pups were treated with 30 nM LRRK2 inhibitors PF-475, PF-360 or DMSO as a vehicle control, then transduced with 2.5 μg/mL alpha -synuclein PFFs and allowed to age a further 14 days prior to sequential detergent fractionation. TX-100-insoluble alpha -synuclein and p62 are similar in both LRRK2 inhibitor treated and untreated neurons. b Quantification of soluble proteins show some reduction of LRRK2 protein levels PF-475 treatment and ~ 75% inhibition of LRRK2 activity (as assayed by pS935 LRRK2) by both PF-475 and PF-360. c Insoluble pS129 alpha -synuclein was slightly, but significantly elevated by PF-360 treatment, while alpha -synuclein and p62 were unchanged by one-way ANOVA. (N = 5 biological replicates for each protein). Means + s.e.m.; *P < 0.05, ****p < 0.0001 by one-way ANOVA with Dunnett’s multiple comparison test. All values are normalized first to GAPDH, as a loading control, then to DMSO-treated neurons Image collected and cropped by CiteAb from the following open publication (//actaneurocomms.biomedcentral.com/articles/10.1186/s40478-018-0550-0), licensed under a CC-BY license. Not internally tested by Novus Biologicals.$

TRS functions similarly to eIF4G and acts as an eIF4F analog. a Pull-down assay of co-expressed TRS-Strep with eIF4A- or eIF4G-FLAG in 293 T cells. TRS-Strep was pulled down with Strep-Tactin beads, and co-precipitation of eIF4A or 4 G was determined by immunoblotting with anti-FLAG antibody. EV, empty vector. * indicates a nonspecific band. b Immunoassay of the co-expression of different combinations of plasmids in 293T cells. Myc-TRS was immunoprecipitated with anti-Myc antibody, and co-precipitation of other proteins was determined using tag-specific antibodies. c Immunoassay of co-expressed eIF4A-FLAG with GST-fused full-length TRS or its various domains in 293T cells. eIF4A-FLAG was immunoprecipitated with anti-FLAG antibody, and co-precipitated TRS proteins were determined by immunoblotting with anti-GST antibody. d Pull-down assay of endogenous translation initiation factors with m7GTP-Sepharose beads in 293 T cells transfected with siRNAs against TRS, 4EHP, or a non-targeting control (siCont). Cap-bound proteins were eluted from beads and immunoblotted with the indicated antibodies. Sepharose beads were used as a negative control. e Pull-down assay of endogenous translation initiation factors with m7GTP-Sepharose beads in 293T cells transfected with siRNAs against eIF4G, eIF4E, or siCont, and their suppression effects on cap-binding of other components, were determined as in (d). The data are representative of at least three experiments, each with similar results Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/30902983), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

The Neutralizing antibody against nucleolin eliminate HDGF-stimulated AKT/HIF-1 alpha /NF-kappa B/VEGF signaling in SCC4 oral cancer cells. a-d SCC4 cells were treated with recombinant HDGF protein (100 ng/ml) in the presence of anti-NCL or anti-IgG antibody (5 μg/ml) for 24 h before total protein extraction. Cell lysates were subjected to Western blotting with the indicated antibodies. beta -actin was used as an internal control for loading and transfer. Data were mean of three experiments. *, P < 0.05; **, P < 0.01; ns, not statistically significant Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/31711427), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

CIP2A is an inhibitor of PP2A-mediated DAPK dephosphorylationRSC96 cells were transfected with control, CIP2A siRNA (A), DKK-CIP2A (B), or DAPK siRNA (C) for 48 h and then exposed to GAS6 (100 ng/ml) for 30 min. PP2A activity and immunoblotting evaluations of DKK, CIP2A, pDAPK, and DAPK were performed. (D) RSC96 cells were incubated with GAS6 (100 ng/ml) for 30 min and co-immunoprecipitation between CIP2A, pDAPK and PP2A was evaluated. Immunoprecipitated PP2A activity was measured. Data are the mean ± SD, and n = 3 for each time point. * p < 0.05, ** p < 0.01, vs. control. Image collected and cropped by CiteAb from the following open publication (//www.oncotarget.com/lookup/doi/10.18632/oncotarget.23978), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Reactivity:

Hu, Mu, Other, Pm, Pm-Or, Pm

Species Glossary

Reactivity: Hu, Mu, Other, Pm, Pm-Or, 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	NB100-904AF350
Alexa Fluor 405	NB100-904AF405
Alexa Fluor 488	NB100-904AF488
Alexa Fluor 532	NB100-904AF532
Alexa Fluor 594	NB100-904AF594
Alexa Fluor 647	NB100-904AF647
Alexa Fluor 700	NB100-904AF700
Alexa Fluor 750	NB100-904AF750
Allophycocyanin	NB100-904APC
Allophycocyanin/Cy7	NB100-904APCCY7
Biotin	NB100-904B
DyLight 350	NB100-904UV
DyLight 405	NB100-904V
DyLight 488	NB100-904G
DyLight 550	NB100-904R
DyLight 594	NB100-904DL594
DyLight 650	NB100-904C
DyLight 680	NB100-904FR
DyLight 755	NB100-904IR
FITC	NB100-904F
HRP	NB100-904H
Janelia Fluor 549	NB100-904JF549
Janelia Fluor 646	NB100-904JF646
PE	NB100-904PE
PE/Atto594	NB100-904PEATT594
PE/Cy5.5	NB100-904PECY55
PE/Cy7	NB100-904PECY7
PerCP	NB100-904PCP
mFluor Violet 450 SE	NB100-904MFV450
mFluor Violet 500 SE	NB100-904MFV500
mFluor Violet 610 SE	NB100-904MFV610

Available Formulations

Formulation	Catalog #	Availability	Price
BSA Free	NB100-904SS

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NB100-137

EGLN1/PHD2 Antibody

(12 Reviews)

(87 Publications)

0.1 mg

NB100-137

Western Blot: EGLN1/PHD2 Antibody [NB100-137] - Analysis of PHD2 expression in human prostate cancer cell lines. Western blot image submitted by a verified customer review.

Immunocytochemistry/Immunofluorescence: EGLN1/PHD2 Antibody [NB100-137] - Staining of endogenous PHD2 in U2OS cells. ICC/IF image submitted by a verified customer review.

<b>Genetic Strategies Validation. </b>Knockdown Validated: EGLN1/PHD2 Antibody [NB100-137] - Detection of PHD2 in human glioblastoma cell lysates. Image submitted by a verified customer review.

Western Blot: EGLN1/PHD2 Antibody [NB100-137] - Detection of human PHD2 by Western blot. Recombinant epitope-tagged PHD1, PHD2 or PHD3 (10 ng/lane) or whole cell lysate from HeLa cells. EGLN1/PHD2 antibody used at 1 ug/mL. Detection by chemiluminescence.

Immunohistochemistry: EGLN1/PHD2 Antibody [NB100-137] - EGLN1/PHD2 and EGFR expression levels positively correlate in breast cancer. Processed tissue microarrays of breast cancer biopsies from 313 patients were stained with EGLN1/PHD2 and EGFR antibodies. Four representative immunohistochemistries of human breast cancer with low and high expression of EGLN1/PHD2 and EGFR are shown. Magnification 10x. Image collected and cropped by CiteAb from the following publication (//www.oncotarget.com/article/14241/text/) licensed under a CC-BY license.

Western Blot: EGLN1/PHD2 Antibody [NB100-137] - Exogenous PHD2 has no impact on the gene expression of HIF-1alpha and HIF-2alpha. U87MG cells were transfected with empty vector (pcDNA) or PHD2 plasmid. Twenty-four hours after transfection, PHD2 was detected by immunoblotting. beta-Actin was used as loading control. The results are representative for three independent experiments. Image collected and cropped by CiteAb from the following publication (//www.nature.com/articles/cddis2014295), licensed under a CC-BY license.

Flow Cytometry: EGLN1/PHD2 Antibody [NB100-137] - An intracellular stain was performed on Jurkat cells with NB100-137AF647 (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.

Western Blot: EGLN1/PHD2 Antibody [NB100-137] - Analysis of PHD2 in normoxia (lane 1) or hypoxia (lane 2) treated SK-N-BE(2) cells using anti-EGLN1/PHD2 antibody. Western blot image submitted by a verified customer review.

Immunocytochemistry/Immunofluorescence: EGLN1/PHD2 Antibody [NB100-137] - Staining of PHD2 in HeLa cells with DyLight 488 (green). Nuclei and alpha-tubulin were counterstained with DAPI (blue) and DyLight 550 (red).

Immunohistochemistry: EGLN1/PHD2 Antibody [NB100-137] - Staining of lung vascular endothelium with EGLN1/PHD2 antibody. Image at 40X.

Flow Cytometry: EGLN1/PHD2 Antibody [NB100-137] - Detection of PHD2 in Jurkat cells. One million Jurkat cells were fixed, permeabilized, and stained with 3.0 ug/mL anti-EGLN1/PHD2 antibody in a 150 uL reaction. Isotype control (black), anti-MLL1 (red).

PHD2 and EGFR expression levels positively correlate in breast cancerProcessed tissue microarrays of breast cancer biopsies from 313 patients were stained with PHD2 and EGFR antibodies (cf Materials and methods). Four representative immunohistochemistries of human breast cancer with low and high expression of PHD2 and EGFR are shown. Magnification 10x.

PHD3 expression correlates with a mesenchymal-like morphology in pancreatic ductal adenocarcinoma cell lines.NHF-1 (Fibroblast) MiaPaca2, Panc1, CAPAN1 and BxPC3 cells were harvested for RNA and protein following 24 hours exposure to normoxia (21% O2) or hypoxia (1% O2). (C) Whole cell lysate was resolved by SDS-PAGE and blotted for beta-tubulin PHD3 and PHD2. N = normoxia, H = hypoxia (1% O2). Image collected and cropped by CiteAb from the following publication (//dx.plos.org/10.1371/journal.pone.0083021), licensed under a CC-BY licence.

Iron supplementation restores HIF-1alpha levels to normal following ATP6V0E1 inhibition in HeLa cells. (D) Immunoblot analysis for HIF-1alpha and PHD2 levels in HIFalpha-GFPODD reporter cells with either ATP6V0E1 or PHD2 depleted or treated with 10 nM BafA. The cells were treated with 100 uM Fe (III) citrate for 24 h. beta actin was used as a control. Results validated findings observed by flow cytometry, whereby HIF-1alpha levels were upregulated following ATP6V0E1 knock-down or inhibition and levels were re-normalized upon Fe (III) citrate treatment. Treatment of Fe (III) citrate in PHD2 depleted cells did not alter HIF-1alpha levels. All experiments were performed in biological duplicate. Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/32984302), licensed under a CC-BY licence.

Rapamycin reduces the accumulation of BMAL1 in Per2 knockout miceA. As shown in the left panel, tissue samples from Per2 knockout mice (mPER−/−) depict robust accumulation of nuclear BMAL1 (arrow) compared to control littermates (arrowhead)(*** p0.05). Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/27285754), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Reactivity:

Hu, Mu, Rt, Pm, Pm-Or, Rb, RM

Species Glossary

Reactivity: Hu, Mu, Rt, Pm, Pm-Or, Rb, RM

Applications:

, , , , , , ,

Applications: , , , , , , ,

Host:

Rabbit Polyclonal

Host: Rabbit Polyclonal

Conjugate:

Unconjugated

Available Conjugates:

Validated by:

Validated by:

Conjugate	Catalog #	Availability	Size	Price
Alexa Fluor 405	NB100-137AF405
Alexa Fluor 488	NB100-137AF488
Alexa Fluor 532	NB100-137AF532
Alexa Fluor 647	NB100-137AF647
Alexa Fluor 700	NB100-137AF700
Biotin	NB100-137B
DyLight 350	NB100-137UV
DyLight 405	NB100-137V
DyLight 488	NB100-137G
DyLight 550	NB100-137R
DyLight 594	NB100-137DL594
DyLight 650	NB100-137C
DyLight 680	NB100-137FR
DyLight 755	NB100-137IR
FITC	NB100-137F
HRP	NB100-137H
Janelia Fluor 549	NB100-137JF549
Janelia Fluor 646	NB100-137JF646
PE	NB100-137PE
mFluor Violet 450 SE	NB100-137MFV450
mFluor Violet 500 SE	NB100-137MFV500
mFluor Violet 610 SE	NB100-137MFV610

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NB110-87318

Beclin 1 Antibody - BSA Free

(4 Reviews)

(61 Publications)

0.05 ml

NB110-87318

Immunohistochemistry-Paraffin: Beclin 1 Antibody [NB110-87318] - Analysis of a FFPE tissue section of human breast cancer using Beclin 1 antibody (Lot 71917) at 1:300 dilution. The primary antibody bound to Beclin 1 antigen in the tissue section was detected using a HRP labeled secondary antibody and DAB reagent. Nuclei of the cells were counterstained with hematoxylin. Cytoplasmic staining can be seen in the cancer as well as the stromal cells. The signal was strongest in a subset of stromal cells which appears to be the cancer associated fibroblasts.

Western Blot: Beclin 1 Antibody [NB110-87318] - Basal levels of autophagy in the hypothalamus of BACHD mice. The expression levels of selected autophagy markers were analyzed by Western blot in hypothalamic tissue from BACHD mice at 2, 6 and 12 months of age and compared with gender- and age-matched controls (n=3-6/group). The data showed a substantial maintenance of the autophagy flux, despite the presence of a metabolic phenotype in the BACHD mice already at early time points. The data in the graphs are expressed as mean +/- SEM, relative to the 2 months wt controls. The Western blots are representative of one sample for each group. Image collected and cropped by CiteAb from the following publication (//dx.plos.org/10.1371/journal.pone.0083050), licensed under a CC-BY license.

Immunocytochemistry/Immunofluorescence: Beclin 1 Antibody [NB110-87318] - Beclin 1/ATG6 Antibody [NB110-87318] - Beclin1 antibody was tested in HeLa cells with FITC (green). Nuclei and alpha-tubulin were counterstained with DAPI (blue) and DyLight 550 (red).

Western Blot: Beclin 1 Antibody [NB110-87318] - Image from verified customer review.

Immunohistochemistry: Beclin 1/ATG6 Antibody [NB110-87318] - Staining of normal breast tissue.

Maintenance of basal levels of autophagy in mice overexpressing htt fragments in the hypothalamus.The expression levels of selected autophagy markers were analyzed by Western blot in mice bilaterally injected with rAAV5-htt853-18Q or rAAV5-htt853-79Q and compared to uninjected controls 8 weeks post injection (n = 6-7/group). The data displayed maintenance of the autophagy flux, despite the presence of a clear metabolic phenotype in the injected mice. The data in the graphs are expressed as mean +/- SEM relative to the uninjected controls. The Western blots are representative of one sample for each group. Image collected and cropped by CiteAb from the following publication (//dx.plos.org/10.1371/journal.pone.0083050), licensed under a CC-BY licence.

Reactivity:

Hu, Mu, Rt, Po, Al, Ca, Pm, Bv, Ch, Pm-Or

Species Glossary

Reactivity: Hu, Mu, Rt, Po, Al, Ca, Pm, Bv, Ch, Pm-Or

Applications:

, , , ,

Applications: , , , ,

Host:

Rabbit Polyclonal

Host: Rabbit Polyclonal

Sizes:

Sample Size Available

Sizes: Sample Size Available

Conjugate:

Unconjugated

Available Conjugates:

Conjugate	Catalog #	Availability	Size	Price
Alexa Fluor 405	NB110-87318AF405
Alexa Fluor 488	NB110-87318AF488
Alexa Fluor 647	NB110-87318AF647
Alexa Fluor 700	NB110-87318AF700
Biotin	NB110-87318B
DyLight 488	NB110-87318G
DyLight 550	NB110-87318R
DyLight 650	NB110-87318C
HRP	NB110-87318H

Available Formulations

Formulation	Catalog #	Availability	Price
BSA Free	NB110-87318SS

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NB600-532

beta-Actin Antibody

(6 Reviews)

(63 Publications)

0.1 mg

NB600-532

Western Blot: beta-Actin Antibody [NB600-532] - Detection of human and mouse Cytoskeletal Actin by western blot. Samples: Whole cell lysate (50 ug) from HeLa, HEK293T, Jurkat, mouse TCMK-1, and mouse NIH 3T3 cells prepared using NETN lysis buffer. Antibody: Affinity purified rabbit anti-Cytoskeletal Actin antibody NB600-532 used for WB at 0.1 ug/ml. Detection: Chemiluminescence with an exposure time of 1 second.

Western Blot: beta-Actin Antibody [NB600-532] - Mouse colon whole cell lysate. PVDF membrane was probed with Rabbit Anti-B actin Antibody (Catalog # NB600-532) followed by HRP-conjugated Anti-Rabbit IgG Secondary Antibody. WB image submitted by a verified customer review.

Immunohistochemistry: beta-Actin Antibody [NB600-532] - Detection of human Cytoskeletal Actin by immunohistochemistry. Sample: FFPE section of human ovarian cancer. Antibody: Affinity purified rabbit anti-Cytoskeletal Actin (NB600-532). Detection: DAB

Western Blot: beta-Actin Antibody [NB600-532] - Western blot analysis of Actin (NB600-532) using RCC4 whole cell lysate [NBP1-30412].

Western Blot: beta-Actin Antibody [NB600-532] - Western blot analysis of Actin (NB600-532) using HepG2 whole cell lysate [NBP1-42569].

Western Blot: beta-Actin Antibody [NB600-532] - Analysis using the HRP conjugate of NB600-532. Detection of Beta Actin in MCF-7 cell lysate (20ug) using anti-Beta Actin antibody. WB image submitted by a verified customer review.

Western Blot: beta-Actin Antibody [NB600-532] - Treatments of periplocin and/or TRAIL activate DR4, FADD, and proapoptotic proteins in HCC cells. The effect of periplocin treatment on the expression of DR4, DR5, and FADD was analyzed by western blot. Image collected and cropped by CiteAb from the following publication (//www.hindawi.com/journals/ecam/2013/958025/), licensed under a CC-BY license.

Western Blot: beta-Actin Antibody [NB600-532] - Hypoxic preconditioning increases PBMNC sensitivity to apelin-13 via upregulation of APJ expression, leading to growth factor secretion.(a) APJ protein expression was significantly increased in hypoxic PBMNCs. *p <0.05 vs. N-PBMNCs. Image collected and cropped by CiteAb from the following publication (//www.nature.com/articles/srep19379), licensed under a CC-BY license.

Immunohistochemistry: beta-Actin Antibody [NB600-532] - Sample: FFPE section of human lung carcinoma. Antibody: Affinity purified rabbit anti-Cytoskeletal Actin used at a dilution of 1:1,000 (1ug/ml). Detection: DAB

Hypoxic preconditioning increases PBMNC sensitivity to apelin-13 via upregulation of APJ expression, leading to growth factor secretion.(a) APJ protein expression was significantly increased in hypoxic PBMNCs. *p < 0.05 vs. N-PBMNCs. Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/26763337), licensed under a CC-BY licence.

L. donovani infection induces HIF-1 alpha expression in CD11chi splenic DCs in an IRF-5 dependent manner.Mice were infected with 2x107 amastigotes intravenously. (A) Real-time PCR analysis of HIF-1 alpha mRNA expression in CD11c+ cells purified from C57BL/6 mice at various time points after infection. (B) Immunoblot analysis of HIF-1 alpha expression in CD11c+ cells from C57BL/6 mice (upper panel) and densitometric analysis normalized to beta -actin expression and expressed as fold increase to results obtained with naïve mice (lower panel). (C) Real-time PCR analysis of HIF-1 alpha expression in sorted CD11c+ cells from Irf-5flox/floxCre- and Irf-5flox/floxCMV-Cre+. (D) Immunoblot analysis of Hif-1 alpha expression in CD11c+ cells population of Irf5flox/floxCre- (left upper panel) and Irf-5flox/floxCMV-Cre+ (right upper panel), and densitometric analysis normalized to beta -actin expression and expressed as fold increase to results obtained with naïve mice (lower panels). (E) Real-time PCR analysis of Hif-1 alpha expression in CD11c- splenocytes from Irf-5flox/floxCre- and Irf-5flox/floxCMV-Cre+. (F) Real-time PCR analysis of HIF-1 alpha mRNA expression in BMDC from Irf-5flox/floxCMV-Cre+ and Cre- mice. All data represent mean ± SEM combined from 3 independent experiments. Image collected and cropped by CiteAb from the following open publication (//dx.plos.org/10.1371/journal.ppat.1004938), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Effects of autophagy inhibitors in combination with IFN-gamma on expression of PD-L1 in gastric cancer cell lines. a The effect of chloroquine (CQ) or 3-MA on expression of PD-L1 with or without INF-gamma for 24 h was determined by flow cytometry assays. In AGS and NCI-n87 cells, MFI as the indication of PD-L1 expression level can be further increased by the treatment of INF-gamma . b Levels of LC3B-I/II, p62/SQSTM1 and PD-L1 were determined by Western blots in AGS and NCI-n87 cells treated by CQ, 3-MA, bafilomycin A1 (Baf) or rapamycin (Rap) for 24 h. c Positive staining of PD-L1 (red) and LC3 positive puncta (green) was determined by immunofluorescence in AGS and NCI-n87 cells treated by autophagy inhibitors and activator as in (b). d Rapamycin decreased the levels of PD-L1 protein in AGS and NCI-n87 cells as shown by flow cytometry. Results were averaged and blots were representative of 4 independent experiments, *p < 0.05, **p < 0.01 Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/30925913), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Reactivity:

Hu, Mu, Rt, Po, Bv, Ca, Ch, Pm, SyHa, Gp, Pm-Or, Rb, Sh, Xp

Species Glossary

Reactivity: Hu, Mu, Rt, Po, Bv, Ca, Ch, Pm, SyHa, Gp, Pm-Or, Rb, Sh, Xp

Applications:

, , , ,

Applications: , , , ,

Host:

Rabbit Polyclonal

Host: Rabbit Polyclonal

Conjugate:

Unconjugated

Available Conjugates:

Conjugate	Catalog #	Availability	Size	Price
Alexa Fluor 350	NB600-532AF350
Alexa Fluor 405	NB600-532AF405
Alexa Fluor 488	NB600-532AF488
Alexa Fluor 532	NB600-532AF532
Alexa Fluor 594	NB600-532AF594
Alexa Fluor 647	NB600-532AF647
Alexa Fluor 700	NB600-532AF700
Alexa Fluor 750	NB600-532AF750
Biotin	NB600-532B
DyLight 350	NB600-532UV
DyLight 405	NB600-532V
DyLight 488	NB600-532G
DyLight 550	NB600-532R
DyLight 594	NB600-532DL594
DyLight 650	NB600-532C
DyLight 680	NB600-532FR
DyLight 755	NB600-532IR
FITC	NB600-532F
HRP	NB600-532H
Janelia Fluor 549	NB600-532JF549
Janelia Fluor 646	NB600-532JF646

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NB200-191

DDX6 Antibody

(1 Review)

(43 Publications)

0.1 ml

NB200-191

Immunohistochemistry-Paraffin: DDX6 Antibody [NB200-191] - Section of human colon carcinoma (left) and mouse renal cell carcinoma(right). Antibody: Affinity purified rabbit anti-DDX6 used at a dilution of 1:200 (1ug/ml). Detection: DAB.

Immunoprecipitation: DDX6 Antibody [NB200-191] - Detection of human DDX6 by Western Blot and Immunoprecipitation. Samples: Whole cell lysate (15 and 50 ug) from HeLa cells. Antibodies: Affinity purified rabbit anti-DDX6 antibody NB200-191 used at 0.04 ug/ml for WB (A and B) and at 3 ug/mg lysate for IP. DDX6 was also immunoprecipitated using rabbit anti-DDX6 antibody NB200-192, but not with 'DDX6 Ab', which is to another epitope from DDX6. Normal rabbit IgG was used as a negative control. Detection: Chemiluminescence with an exposure time of 1 second (A & B).

Orally administered lemongrass and white tea extract reduce tumor size in lymphoma xenograft model in immunocompromised miceImmunocompromised mice were subcutaneously injected with cancerous cells and tumors were allowed to establish. Treatments occurred every other day and the studied compound or the equivalent vehicle control administered orally for three weeks. (A, B) The tumors were photographed before and after extraction from the animals. (C) Tumor volume and mass were measured two times per week. (D) Immunohistochemistry analysis of sectioned tumor tissues from the lymphoma study. Each section was subjected to the specified antibody followed by a biotinylated secondary antibody. Detection was done using a DAB Peroxidase HRP Substrate Kit (brown) followed by Hematoxylin counterstaining (purple). Images were obtained using inverted bright field microscopy. Sectioning results are representative of three individual tumors. Scale bar is 50 microns. Statistical analysis using One-Way ANOVA. *p < 0.05 vs tumor volume of the control. Image collected and cropped by CiteAb from the following open publication (//www.oncotarget.com/lookup/doi/10.18632/oncotarget.22502), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Reactivity:

Hu, Mu, Ha, Ch, Pm-Or

Species Glossary

Reactivity: Hu, Mu, Ha, Ch, Pm-Or

Applications:

, , ,

Applications: , , ,

Host:

Rabbit Polyclonal

Host: Rabbit Polyclonal

Conjugate:

Unconjugated

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NBP1-23017

RPA2 [p Ser4, p Ser8] Antibody

(40 Publications)

100 ul

NBP1-23017

Immunohistochemistry-Paraffin: RPA2 [p Ser4, p Ser8] Antibody [NBP1-23017] - Section of mouse gut, MOCK treatment (left) and CIP treatment (right).Antibody: Affinity purified rabbit anti-Phospho RPA32 (S4/S8) used at a dilution of 1:1,000 (1ug/ml). Detection: DAB

Western Blot: RPA2 [p Ser4, p Ser8] Antibody [NBP1-23017] - Samples: Whole cell lysate (50 ug for WB in A; 1 mg for IP, 20% of IP loaded in B) from HeLa Cells that had been treated with EPE (+) or mock treated (-). In B, immunoprecipitated RPA32 was either treated with phosphatase (+) or mock treated (-). Antibodies: Phosphorylated RPA32 was detected using rabbit anti-phospho RPA32 Ser4/Ser8 antibody NBP1-23017 lot 2 at 1 ug/ml. Total RPA32 was detected using rabbit anti-RPA32 antibody NB100-332 at 1 ug/ml. RPA32 was immunoprecipitated using NB100-332 at 3 ug/mg lysate. Detection: Chemiluminescence with exposure times of 30 seconds for phospho RPA32 Ser4/Ser8 (A and B) and 1 second for total RPA32 (A and B).

<b>Biological Strategies Validation. </b>Western Blot: RPA2 [p Ser4, p Ser8] Antibody [NBP1-23017] - Detection of Human Phospho RPA32 (S4/S8) by Western Blot. Samples: Whole cell lysate (50 ug) from HeLa cells treated with 100 uM EPE for 4 hours (+) or mock treated (-) cells. Antibodies: Affinity purified rabbit anti-Phospho RPA32 (S4/S8) antibody NBP1-23017 used for WB at 0.1 ug/ml. Detection: Chemiluminescence with an exposure time of 30 seconds. Lower panel shows Westen Blot for total RPA32 using affinity purified rabbit anti-RPA32 antibody A300-244A at 0.1 ug/ml with an exposure time of 30 seconds.

Immunohistochemistry-Paraffin: RPA2 [p Ser4, p Ser8] Antibody [NBP1-23017] - Section of human breast carcinoma, MOCK treatment (left) and CIP treatment(right). Antibody: Affinity purified rabbit anti-Phospho RPA32 (S4/S8) (used at a dilution of 1:1,000 (1ug/ml). Detection: DAB

<b>Independent Antibodies Validation. </b>Immunoprecipitation: RPA2 [p Ser4, p Ser8] Antibody [NBP1-23017] - Detection of human Phospho RPA32 (S4/S8) by western blot of immunoprecipitates. Samples: Whole cell lysate (1.0 mg per IP reaction; 20% of IP loaded) from HeLa cells treated with EPE (+) and/or Lambda PP (+) or mock treated (-). Antibodies: RPA32 (S4/S8) was immunoprecipitated using affinity purified rabbit anti-RPA32 antibody NB100-332. For blotting immunoprecipitated Phospho RPA32 (S4/S8), rabbit anti-Phospho RPA32 (S4/S8) antibody NBP1-23017 was used at 0.1 ug/ml. Lower Panel: Rabbit anti-RPA antibody NB100-332. Detection: Chemiluminescence with an exposure time of 75 seconds.

Reactivity:

Hu, Mu, Pm-Or

Species Glossary

Reactivity: Hu, Mu, Pm-Or

Applications:

, , , , ,

Applications: , , , , ,

Host:

Rabbit Polyclonal

Host: Rabbit Polyclonal

Conjugate:

Unconjugated

Available Conjugates:

Validated by:

Validated by:

Conjugate	Catalog #	Availability	Size	Price
Alexa Fluor 350	NBP1-23017AF350
Alexa Fluor 405	NBP1-23017AF405
Alexa Fluor 488	NBP1-23017AF488
Alexa Fluor 532	NBP1-23017AF532
Alexa Fluor 594	NBP1-23017AF594
Alexa Fluor 647	NBP1-23017AF647
Alexa Fluor 700	NBP1-23017AF700
Alexa Fluor 750	NBP1-23017AF750
DyLight 405	NBP1-23017V
DyLight 488	NBP1-23017G
DyLight 550	NBP1-23017R
DyLight 594	NBP1-23017DL594
DyLight 680	NBP1-23017FR
DyLight 755	NBP1-23017IR
Janelia Fluor 549	NBP1-23017JF549
Janelia Fluor 646	NBP1-23017JF646
PE	NBP1-23017PE

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NB100-544

RPA2 [p Ser33] Antibody

(1 Review)

(25 Publications)

100 ul

NB100-544

Immunocytochemistry/Immunofluorescence: RPA2 [p Ser33] Antibody [NB100-544] - L.36 PDAC cells were treated two hours using 5 mM hydroxyurea to induce RPA32 Ser33 phosphorylation. The antibody produces clear nuclear staining of treated cells. ICC/IF image submitted by a verified customer review.

Immunocytochemistry/Immunofluorescence: RPA2 [p Ser33] Antibody [NB100-544] - Active DNA end processing in late micronuclei compartments. Detection and quantification of RPA2 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). Image collected and cropped by CiteAb from the following publication (//bmccancer.biomedcentral.com/articles/10.1186/s12885-018-4347-0), licensed under a CC-BY license.

$Cellular localization of OS-9 and PHD2.(A) A lectin gel-shift assay was conducted to test for glycosylated proteins. Total cell lysates of U2OS cells were incubated in the presence or absence of the endoglycosidases EndoH and PNGaseF for 6 h at 37°C. Digest products were separated on a reducing 10% SDS-PAGE gel which contained concanavalin A co-polymerized in the top layer of the separating gel to retard mobility of glycosylated proteins [56]. Glycosylated OS-9 is indicated as ‘g’, deglycosylated OS-9 as ‘d’. (B) Detection of OS-9 and PHD2 in the nuclear fraction. HEK293 cells with and without transfection of the plasmid pcDNA3-OS-9 were separated into nuclear fraction (N) and postnuclear supernatant (PS), the latter containing cytoplasm and organelles. Western blot analysis included BiP, GAPDH and lamin A as typical marker proteins for the ER, the cytoplasm and the nucleus, respectively. (C) Detection of OS-9 and PHD2 in the cytoplasm. HEK293 cells were co-transfected with pcDNA3-OS-9 and pPHD2-V5. For hypoxia, cells were exposed to 3% O2 for 4 h. Cells were treated with 50 µg/ml digitonin and centrifuged to obtain a cytoplasmic (C) and an organelle fraction (O) and subjected to immunoblotting. (D) Isolation of cellular endomembranes. HEK293 cells were lysed mechanically by several passages through a 30½G needle. The postnuclear supernatant was processed further by ultra-centrifugation to separate the organelles (O) from the cytosol (C). High salt treatment (1 M KCl) of the organelle fraction produced a wash fraction (W) that contained dissociated peripheral membrane proteins. For immunoblot analysis of subcellular fractionations, cell aliquots were normalized for cell number prior to loading (B–D). Representative Western blots are shown for each subfigure. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/21559462), licensed under a CC-BY license. Not internally tested by Novus Biologicals.$

Reactivity:

Hu, Mu, Pm-Or

Species Glossary

Reactivity: Hu, Mu, Pm-Or

Applications:

, ,

Applications: , ,

Host:

Rabbit Polyclonal

Host: Rabbit Polyclonal

Conjugate:

Unconjugated

Available Conjugates:

Validated by:

Validated by:

Conjugate	Catalog #	Availability	Size	Price
Alexa Fluor 594	NB100-544AF594

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NB200-192

DDX6 Antibody

(24 Publications)

100 ul

NB200-192

<b>Independent Antibodies Validation. </b>Immunoprecipitation: DDX6 Antibody [NB200-192] - Detection of human DDX6 by western blot of immunoprecipitates. Samples: Whole cell lysate (0.5 or 1.0 mg per IP reaction; 20% of IP loaded) from HeLa cells prepared using NETN lysis buffer. Antibodies: Affinity purified rabbit anti-DDX6 antibody NB200-192 (lot NB200-192-3) used for IP at 6 ug per reaction. DDX6 was also immunoprecipitated by a previous lot of this antibody (NB200-192-2) and rabbit anti-DDX6 antibody NB200-191. For blotting immunoprecipitated DDX6, NB200-192 was used at 1 ug/ml. Detection: Chemiluminescence with an exposure time of 1 second.

<b>Genetic Strategies Validation. </b>Knockdown Validated: DDX6 Antibody [NB200-192] - Western blot analysis of HNRNPK and DDX6 protein levels upon HNRNPK or DDX6 knockdown. Image collected and cropped by CiteAb from the following publication (nature.com/articles/s41467-019-12238-x), licensed under a CC-BY license.

Hypoxia and HIF-1 alpha /VEGF induction upon S. pneumoniae infection in brain ECs. a Control and S. pneumoniae infected bEnd5 cells treated with pimonidazole hydrochloride (Hypoxyprobe 200 mM) and visualized for cellular hypoxia by red 549-linked mouse anti-pimonidazole monoclonal antibodies. D39 and TIGR4 strains infected cells show significantly high number of hypoxic cells compared to control cells which is however not present in the top row without the probe indicating specificity of the staining (scale bar 10 µm). b Oxygen levels (%) were quantified in the medium of control and S. pneumoniae infected bEnd5 cells using the SensorDish® Reader (SDR) for non-invasive measurement of O2 levels through the transparent well bottom. O2 concentration (pO2% air saturation) was obtained at 60-s intervals and average values at several different time points shown indicate a significant reduction in O2 levels within minutes post-infection and to hypoxic levels by 2 h (N = 3, 2-tailed paired t test compared to control for each condition at the corresponding time point, mean ± SEM, **p < 0.01, ***p < 0.001), which was however not present either in control or deferoxamine (DFO, 200 µM), an iron chelator that induces HIF-1 alpha independent of hypoxia. c Control and S. pneumoniae infected bEnd5 cells were analyzed for HIF-1 alpha protein induction by Western blotting. The result shows a significant increase in HIF-1 alpha levels in both D39 and TIGR4 infected cells compared to control conditions when the band pixel intensity is quantified by normalizing to the housekeeping protein beta -actin band. DFO served as a positive control for HIF-1 alpha induction (N = 4, *p < 0.05, 2-tailed paired t test compared to control for each condition). d Quantitative RT-PCR expression analysis (by 2−∆∆Ct method) of control and infected bEnd5 cells shows upregulation of HIF-1 alpha and its transcriptional target gene VEGF upon a S. pneumoniae infection. Expression was normalized to ribosomal protein, large, P0 (RPLP0) that served as a housekeeping gene (N = 6, *p < 0.05, **p < 0.01, 2-tailed paired t test compared to control) 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.

Expression of the cytochrome P450 aromatase in the ovary of control (C; open bar; n = 6) and hypothyroid (Hypo; solid bar; n = 6) rabbits. Representative immunoblot showing the expression of aromatase (a) and Ponceau's Red stained membrane (b). Relative expression of aromatase in C and Hypo groups (c). Data are mean ± SEM. ∗∗P < 0.01. Immunoreactivity of antiaromatase (+) was identified in granulosa cells of antral follicles (tertiary, tf; Graafian, gf) of control (d, e) and hypothyroid (f, g) ovaries. Nonlabeling was observed when the primary antibody was omitted (negative control; h). Bars: (d) 200 μm; (f) and (h) 100 μm; and (e) and (g) 20 μm. Granulose cells, gc; theca cells, tc. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/28133606), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

$Subcellular localization of TM6SF2.A, primary hepatocytes from 8-week-old female mice on a chow diet were plated on collagen-coated coverslips for 4 h, fixed, and stained with antibodies against markers for the ER (calnexin (CANX)), cis-Golgi (receptor-binding cancer antigen expressed on SiSo cells (RCAS1)), and Golgi (Giantin (GOLGBI) (green, left column) and TM6SF2 (red, middle column)). The merged signal from both channels (yellow, right column) shows subcellular co-localization. All images were taken using a ×63 oil immersion objective. Scale bar, 10 μm. B, immunoaffinity isolation of ER and Golgi complex from mouse liver. ER and Golgi fractions were prepared from mouse liver microsomes by immunoaffinity chromatography as described under “Experimental Procedures.” Microsome membranes were dissolved in RIPA buffer, and equal volumes were separated on 10% SDS-PAGE and immunoblotting as described under “Experimental Procedures.” BiP, binding immunoglobulin protein; Gos28, Golgi SNAP receptor complex member 1; *, nonspecific band. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/27013658), licensed under a CC-BY license. Not internally tested by Novus Biologicals.$

Reactivity:

Hu, Mu, Gp, Pm-Or

Species Glossary

Reactivity: Hu, Mu, Gp, Pm-Or

Applications:

, , , ,

Applications: , , , ,

Host:

Rabbit Polyclonal

Host: Rabbit Polyclonal

Conjugate:

Unconjugated

Available Conjugates:

Validated by:

Validated by:

Conjugate	Catalog #	Availability	Size	Price
Alexa Fluor 350	NB200-192AF350
Alexa Fluor 405	NB200-192AF405
Alexa Fluor 488	NB200-192AF488
Alexa Fluor 532	NB200-192AF532
Alexa Fluor 594	NB200-192AF594
Alexa Fluor 647	NB200-192AF647
Alexa Fluor 700	NB200-192AF700
Alexa Fluor 750	NB200-192AF750
Allophycocyanin	NB200-192APC
Biotin	NB200-192B
DyLight 350	NB200-192UV
DyLight 405	NB200-192V
DyLight 488	NB200-192G
DyLight 550	NB200-192R
DyLight 594	NB200-192DL594
DyLight 650	NB200-192C
DyLight 680	NB200-192FR
DyLight 755	NB200-192IR
FITC	NB200-192F
HRP	NB200-192H
Janelia Fluor 549	NB200-192JF549
Janelia Fluor 646	NB200-192JF646
PE	NB200-192PE
PerCP	NB200-192PCP

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NB100-1974

Calnexin Antibody - BSA Free

(1 Review)

(11 Publications)

0.1 ml

NB100-1974

Immunocytochemistry/Immunofluorescence: Calnexin Antibody [NB100-1974] - Rat FR 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 (NB100-1974) at 1 ug/ml overnight at 4C and detected with an anti-rabbit DyLight 488 (Green) at a 1:1000 dilution for 60 minutes. Nuclei were counterstained with DAPI (Blue). Cells were imaged using a 100X objective and digitally deconvolved.

Western Blot: Calnexin Antibody [NB100-1974] - Identification of plasma exosomes and differentially expressed exosomal miRNAs. Confirmation of the exosomes markers with Western blotting indicated the presence of CD63 but the absence of calnexin in exosomes. Image collected and cropped by CiteAb from the following publication (//www.frontiersin.org/article/10.3389/fonc.2019.00459/full), licensed under a CC-BY license.

Immunohistochemistry: Calnexin Antibody [NB100-1974] - Analysis of Calnexin in mouse bladder using DAB with hematoxylin counterstain.

Flow Cytometry: Calnexin Antibody [NB100-1974] - An intracellular stain was performed on rat FR cells with Calnexin Antibody NB100-1974 (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).

Western Blot: Calnexin Antibody [NB100-1974] - Analysis of Calnexin in HeLa whole cell lysate.

Immunocytochemistry/Immunofluorescence: Calnexin Antibody [NB100-1974] - Zebrafish Vwf forms pseudo-Weibel-Palade bodies (pseudo-WPBs) in mammalian cell culture. pzVwf/Myc-HIS (zebrafish Vwf) plasmids were transfected into HEK293T cells. Anti-Myc antibody conjugated to Alexa Fluor 488 (green channel) was used for detection and anti-calnexin antibody conjugated to Alexa Fluor 594 (red channel) labeled endoplasmic reticulum (ER). Both constructs demonstrate formation of elongated Myc positive and ER negative structures (absence of yellow signal in the merged panels) characteristic of pseudo-WPBs. Scale bars, 2.5 um. Image collected and cropped by CiteAb from the following publication (//www.hindawi.com/journals/ah/2012/214209/), licensed under a CC-BY license.

Flow Cytometry: Calnexin Antibody [NB100-1974] - Analysis of Alexa Fluor (R) 488 conjugate of NB100-1974. An intracellular stain was performed on Jurkat cells with Calnexin antibody NB100-1974AF488 (blue) and a matched isotype control NBP2-24893AF488 (orange).

Flow Cytometry: Calnexin Antibody [NB100-1974] - An intracellular stain was performed on HeLa cells with Calnexin antibody NB100-1974AF488 (blue) and a matched isotype control NBP2-24893AF488 (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 using the Alexa Fluor 488 form of this antibody.

Flow Cytometry: Calnexin Antibody [NB100-1974] - An intracellular stain was performed on Daudi cells with Calnexin Antibody NB100-1974 (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).

Flow Cytometry: Calnexin Antibody [NB100-1974] - An intracellular stain was performed on NIH3T3 cells with Calnexin Antibody NB100-1974 (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).

Simple Western: Calnexin Antibody [NB100-1974] - Image shows a specific band for Calnexin in 0.1 mg/mL of HeLa lysate. This experiment was performed under reducing conditions using the 12-230 kDa separation system.

Identification of plasma exosomes and differentially expressed exosomal miRNAs. (D) Confirmation of the exosomes markers with Western blotting indicated the presence of CD63 but the absence of calnexin in exosomes. Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31249805), licensed under a CC-BY licence.

EMPA treatment attenuated cardiomyocyte overproduction of reactive oxygen species (ROS) induced by TAC. (A) Left, Mitosox staining of cardiomyocytes in sham, sham + EMPA, TAC and TAC + EMPA groups and Right, quantitative results. (B) Representative blots of NRF-2 and HO-1, and quantitative results. (C) The relative mRNA levels of genes related to endogenous antioxidants. Results are expressed as mean ± SEM, n = 5–7, *p < 0.05 vs. corresponding sham group, †p < 0.05 vs. corresponding TAC vehicle group. One-way ANOVA and Tukey post hoc test. EMPA, empagliflozin; SEM, standard error of the mean; TAC, transverse aortic constriction; NRF-2, the nuclear factor erythroid 2–related factor 2; HO-1, heme oxygenase-1; GCLM, glutamate-cysteine ligase modifier subunit; GAPDH, glyceraldehyde 3-phosphate dehydrogenase. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/35647080), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

HIF‐2 alpha depletion counteracts tumour growth and non‐canonical glutamine metabolism in vivo. (A) Representative images of tumour‐bearing mice and tumours removed from the mice. (B) Tumour volumes were measured on the indicated days. (C) Tumour weights were shown as the means ± S.D. when the tumours were harvested. (D) Representative images (×200) of H&E and IHC staining of the tumours. Ki67 was used as proliferation index. (E and F) qRT‐PCR and Western blot analysed the expression of HIF‐2 alpha and GOT1 in tumour tissues from sh‐HIF‐2 alpha Panc‐1 group compared with control group, *P < 0.05, **P < 0.01. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/28544376), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Bmal1 regulates tumor-associated macrophage polarization.(A) Bmal1 gene expression (left panel) and protein levels (right panel) in WT macrophages treated with control medium or increasing doses of B16-F10 tumor-conditioned medium (T-CM, diluted 1:3 or 1:1 with control medium) for 8 hr. N = 3 biological replicates for qPCR, statistical analysis was performed using Student’s T test. (B) Measurement of mROS using MitoSox Red (mean fluorescent intensity, MFI) in mitochondria from macrophages treated with control medium or T-CM diluted 1:1 with control medium for 1 hr. N = 3 biological replicates, statistical analysis was performed using Student’s T test. (C) Hif-1 alpha protein levels in WT and M-BKO macrophages treated with control medium, T-CM diluted 1:1 with control medium, or undiluted T-CM for 4 hr. (D) Glycolytic stress test in macrophages pretreated with control medium or T-CM diluted 1:1 with control medium for 4 hr. N = 5 biological replicates. Statistical analysis was performed using two-way ANOVA comparing T-CM-treated M-BKO with WT cells across the time course. (E) Relative expression of genes involved in amino-acid metabolism and oxidative stress response in macrophages treated with control medium or T-CM diluted 1:3 with control medium for 8 hr, as determined by qPCR. N = 3 biological replicates, statistical analysis was performed using Student’s T test. (F) Tumor volume in male (left) and female (right) WT and M-BKO mice. 300,000 B16-F10 cells were injected subcutaneously into the right flank. N = 18 (male) and 8 (female) mice, statistical analysis was performed using two-way ANOVA for WT vs M-BKO mice across the time course. (G) Gene expression for F4/80+ cells isolated from B16-F10 tumors or spleens of female mice 14 days after injection. Tissues from six mice per genotype were pooled into three groups for leukocyte isolation. Statistical analysis was performed using Student’s T test. Data are presented as mean ± S.E.M. *, p<0.05. Experiments were repeated at least twice.Increased mROS levels and glucose uptake in M-BKO TAMs.(A) Tumor volumes of B16-F10 subcutaneous allografts in 3-month-old female WT and M-BKO mice 14 days after tumor cell injection. Each mouse was injected with 500,000 B16-F10 cells in the right and left flanks, and tumors from each mouse were pooled for immune cell isolation and flow cytometry. N = 4 mice, with two tumors per mouse. (B, C) mROS production and glucose uptake by tumor-associated CD45+F4/80+ cells determined by flow cytometry (mean fluorescent intensities) of Mitosox Red and 2-NBDG staining, respectively. N = 4. Statistical analysis was performed using Student’s T test. Data are presented as mean ± S.E.M. *, p<0.05. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/32396064), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Tau clearance in vivo and autophagy function. Clearance kinetics of photoconverted Dendra-tau measured in neurons of WT-tau and AT152T-tau fish. Measurement of the intensity of the red Dendra-tau signal over time reflects the clearance or degradation of tau protein. (A) Representative images of photoconverted red Dendra-tau signal comparing a single neuron from WT-tau and A152T-tau fish at three different timepoints: immediately after photoconversion (0 h), 24 h and 48 h after photoconversion. (B) Quantification of red Dendra-tau intensity in photoconverted neurons in the spinal cord of WT-tau and A152T-Tau transgenic fish (representative images shown in Supplementary Fig. 8C). The percentage of residual photoconverted red Dendra-tau was measured over 48 h measured at 12-h intervals. Dendra-tagged A152T-tau clears at a significantly lower rate than WT-tau. (n = 30/group shown as mean ± SD; Student-Newman-Keuls one-way ANOVA, **P < 0.01 and ***P < 0.001 versus WT-tau). (C–F) Western blots for LC3-II, a well-characterized marker of autophagosome number, demonstrate that there are no differences in the levels of this protein between WT-tau and A152T-tau fish either at 24 hpf (pre-phenotype; C and D) or 72 hpf (post-phenotype; E and F). (E and F) Measurements of LC3-II levels in the presence or absence of ammonium chloride provides a method for measuring autophagic flux. No differences were observed between the two transgenic lines at 3 dpf, suggesting that autophagy functions normally in both WT-tau and A152T-tau fish (graph represents mean ± SD of four independent clutches per group for E and F and three for C and D; two-tailed t-test). (G and H) Clearance kinetics of Dendra-tau was measured in the presence or absence of ammonium chloride. Treatment with ammonium chloride blocks autophagic flux and delays the clearance of both WT-tau and A152T-tau to the same extent, indicating that flux occurs at the same rate in these two lines (mean ± SD, n = 62 neurons/group; Student-Newman-Keuls one-way ANOVA, **P < 0.01 and ***P < 0.001 versus untreated group). Note in G and H, the ‘WT-tau + NH4Cl’ (denoted by black squares and black dashed line) overlaps with the ‘A152T-tau’ line (denoted by grey triangles and grey solid line). The graphs in G and H are presented with a different line in the foreground and background to aid interpretation. Image collected and cropped by CiteAb from the following open publication (//academic.oup.com/brain/article/140/4/1128/2980948), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Reactivity:

Hu, Mu, Rt, Ha, Ze, Ca, Pm-Or

Species Glossary

Reactivity: Hu, Mu, Rt, Ha, Ze, Ca, Pm-Or

Applications:

, , , , ,

Applications: , , , , ,

Host:

Rabbit Polyclonal

Host: Rabbit Polyclonal

Sizes:

Sample Size Available

Sizes: Sample Size Available

Conjugate:

Unconjugated

Available Conjugates:

Conjugate	Catalog #	Availability	Size	Price
Alexa Fluor 350	NB100-1974AF350
Alexa Fluor 405	NB100-1974AF405
Alexa Fluor 488	NB100-1974AF488
Alexa Fluor 532	NB100-1974AF532
Alexa Fluor 594	NB100-1974AF594
Alexa Fluor 647	NB100-1974AF647
Alexa Fluor 700	NB100-1974AF700
Alexa Fluor 750	NB100-1974AF750
Allophycocyanin	NB100-1974APC
Biotin	NB100-1974B
DyLight 350	NB100-1974UV
DyLight 405	NB100-1974V
DyLight 488	NB100-1974G
DyLight 550	NB100-1974R
DyLight 594	NB100-1974DL594
DyLight 650	NB100-1974C
DyLight 680	NB100-1974FR
DyLight 755	NB100-1974IR
FITC	NB100-1974F
HRP	NB100-1974H
Janelia Fluor 549	NB100-1974JF549
Janelia Fluor 646	NB100-1974JF646
PE	NB100-1974PE
PerCP	NB100-1974PCP
mFluor Violet 450 SE	NB100-1974MFV450
mFluor Violet 500 SE	NB100-1974MFV500
mFluor Violet 610 SE	NB100-1974MFV610

Available Formulations

Formulation	Catalog #	Availability	Price
BSA Free	NB100-1974-0.025ml

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NB100-687

Cytokeratin 19 Antibody - BSA Free

(1 Review)

(9 Publications)

0.1 ml

NB100-687

<b>Biological Strategies Validation. </b>Immunocytochemistry/Immunofluorescence: Cytokeratin 19 Antibody [NB100-687] - TUDCA induces intermediate states of mesenchymal and epithelial cells in primary cultures of rat HSC during hepatic differentiation. Under control conditions HSC remained negative for K19 (Cytokeratin 19) expression, (d) but this epithelial marker protein was induced in HSC cultures after treatment with 2 uM TUDCA for 14 days (red). (f) K19 was found to be co-expressed with desmin (green), which indicated the origin of epithelial progenitor cells from HSC. (I) Cells with different states of maturation were still found after 21 days of TUDCA treatment. Image collected and cropped by CiteAb from the following publication (//www.nature.com/articles/srep13320), licensed under a CC-BY license.

Immunohistochemistry: Cytokeratin 19 Antibody [NB100-687] - Inhibition of MST improves liver regeneration in aged mice. Representative photomicrograph of an aged liver treated with siMST and stained with H&E and by IHC for CK19 and Ki67. Arrows indicate ductal regions with no signs of reaction or oval cell expansion. Image collected and cropped by CiteAb from the following publication (//embomolmed.embopress.org/lookup/doi/10.15252/emmm.201506089), licensed under a CC-BY license.

Immunocytochemistry/Immunofluorescence: Cytokeratin 19 Antibody [NB100-687] - Analysis of Cytokeratin 19 in MCF7 cells using Cytokeratin 19 antibody (green). Nuclei and alpha-tubulin were counterstained with DAPI (blue) and DyLight 550 (red).

Flow Cytometry: Cytokeratin 19 Antibody [NB100-687] - An intracellular stain was performed on MCF7 cells with Cytokeratin 19 Antibody NB100-687AF647 (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.

Western Blot: Cytokeratin 19 Antibody [NB100-687] - Analysis of Cytokeratin 19 in 1) HepG2 and 2) MCF7 lysates.

Immunohistochemistry: Cytokeratin 19 Antibody [NB100-687] - Staining of Cytokeratin 19 in human kidney carcinoma using DAB with hematoxylin counterstain.

TUDCA induces intermediate states of mesenchymal and epithelial cells in primary cultures of rat HSC during hepatic differentiation.Freshly isolated rat HSC. (e-g) K19 was found to be co-expressed with desmin and vimentin (green), which indicated the origin of epithelial progenitor cells from HSC. Image collected and cropped by CiteAb from the following publication (//www.nature.com/articles/srep13320), licensed under a CC-BY licence.

Reactivity:

Hu, Mu, Rt, Pm-Or

Species Glossary

Reactivity: Hu, Mu, Rt, Pm-Or

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	NB100-687AF350
Alexa Fluor 405	NB100-687AF405
Alexa Fluor 488	NB100-687AF488
Alexa Fluor 532	NB100-687AF532
Alexa Fluor 594	NB100-687AF594
Alexa Fluor 647	NB100-687AF647
Alexa Fluor 700	NB100-687AF700
Alexa Fluor 750	NB100-687AF750
Allophycocyanin	NB100-687APC
Biotin	NB100-687B
DyLight 350	NB100-687UV
DyLight 405	NB100-687V
DyLight 488	NB100-687G
DyLight 550	NB100-687R
DyLight 594	NB100-687DL594
DyLight 650	NB100-687C
DyLight 680	NB100-687FR
DyLight 755	NB100-687IR
FITC	NB100-687F
HRP	NB100-687H
Janelia Fluor 549	NB100-687JF549
Janelia Fluor 646	NB100-687JF646
PE	NB100-687PE
PerCP	NB100-687PCP
mFluor Violet 450 SE	NB100-687MFV450
mFluor Violet 500 SE	NB100-687MFV500
mFluor Violet 610 SE	NB100-687MFV610

Available Formulations

Formulation	Catalog #	Availability	Price
BSA Free	NB100-687SS

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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

Category

Protein/Target

Applications

Reactivity

Citation

Antibody Validation

Reviews

Host

Available Conjugates

Format

Marker

Modification

Clonality

Clone

Gene Symbol

Images Type

Isotype

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Has Sample Size

Promotional Item

Species Glossary

53BP1 Antibody - BSA Free

53BP1 Antibody - BSA Free

53BP1 Antibody - BSA Free

EGLN1/PHD2 Antibody

Beclin 1 Antibody - BSA Free

beta-Actin Antibody

DDX6 Antibody

RPA2 [p Ser4, p Ser8] Antibody

RPA2 [p Ser33] Antibody

DDX6 Antibody

Calnexin Antibody - BSA Free

Cytokeratin 19 Antibody - BSA Free