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NB100-304

53BP1 Antibody - BSA Free

(14 Reviews)

(712 Publications)

0.1 mg

NB100-304

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

Reactivity:

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

Species Glossary

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

Applications:

, , , , , , , , , ,

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

Host:

Rabbit Polyclonal

Host: Rabbit Polyclonal

Sizes:

Sample Size Available

Sizes: Sample Size Available

Conjugate:

Unconjugated

Available Conjugates:

Validated by:

Validated by:

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

Available Formulations

Formulation	Catalog #	Availability	Price
BSA Free	NB100-304SS

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NB100-142

Mre11 Antibody

(4 Reviews)

(234 Publications)

0.05 ml

NB100-142

<b>Genetic Strategies Validation. </b>Knockdown Validated: Mre11 Antibody [NB100-142] - Mre11 and NBS1 contribute to OriP replication and EBV episome stability. D98/HR1 cells were transfected with siRNA for Mre11 or NBS1, or Luciferase control and assayed by immunoblot (IB) with antibodies specific for Mre11 (left pane) or NBS1 (right panel), or PCNA (lower panel) as a loading control. Image collected and cropped by CiteAb from the following publication (//journals.plos.org/plosone/article?id=10.1371/journal.pone.0001257) licensed under a CC-BY license.

Immunohistochemistry: Mre11 Antibody [NB100-142] - Immunohistochemical staining of MRE11 in a human epidermis cross section.

Western Blot: Mre11 Antibody [NB100-142] - Western blot analysis of Mre11 on 50 ug of HeLa and MEF lysates, displaying bands at the molecular weight of 81 kDa.

Immunocytochemistry/Immunofluorescence: Mre11 Antibody [NB100-142] - HeLa cells were fixed for 10 minutes using 10% formalin and then permeabilized for 5 minutes using 1X TBS + 0.5% Triton X-100. The cells were incubated with anti-Mre11 [NB100-142] at a 1:500 dilution overnight at 4C and detected with an anti-rabbit DyLight 488 (Green) at a 1:500 dilution. Actin was detected with Phalloidin 568 (Red) at a 1:200 dilution. Nuclei were counterstained with DAPI (Blue). Cells were imaged using a 40X objective.

Chromatin Immunoprecipitation: Mre11 Antibody [NB100-142] - Aggregated END-seq signal and MRE11 ChIP-seq RPM in WT (left) and Atm -/- (right). To fairly compare ChIP-seq signal between WT and Atm -/-, MRE11 scale is proportional to spike-in normalized END-seq RPM for each genotype. Individual hotspot examples (chr12:34,592,264-34,598,265) are shown below. Note that decreased MRE11 coverage is observed within NDR of Atm -/-. Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/32051414/) licensed under a CC-BY license.

Knockdown Validated: Mre11 Antibody [NB100-142] - TIG-1 human primary fibroblasts, whole cell lysate (30 ug). Image from verified customer review.

ATM coordinates multiple levels of resection machinery. d Aggregated END-seq signal and MRE11 ChIP-seq RPM in WT (left) and Atm-/- (right). To fairly compare ChIP-seq signal between WT and Atm-/-, MRE11 scale is proportional to spike-in normalized END-seq RPM for each genotype. Individual hotspot examples (chr12:34,592,264-34,598,265) are shown below. Note that decreased MRE11 coverage is observed within NDR of Atm-/-. e Aggregate plot overlapping WT END-seq and Atm-/- MRE11 ChIP-seq, normalized to the same height. MRE11 shows prominent localization to the WT END-seq read-less gap. Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/32051414), licensed under a CC-BY licence.

Elevated levels of various proteins in MEC and in dentate gyrus of MPS IIIA brain.Staining was performed with antibodies against the proteins shown in a 7 months-old MPS IIIA mouse brain. The first 3 rows are for the MEC region and the bottom row for dentate gyrus. Age-matched C57BL6 mice, used as controls, showed no staining in the MEC region (not shown). The dentate gyrus showed AT270 inclusions in MPS IIIA (−/−) mouse brain (arrows) but not in the C57BL/6 (control) brain (bottom row). Image collected and cropped by CiteAb from the following open publication (//dx.plos.org/10.1371/journal.pone.0027461), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

$SUMO2-PCNA enriches CAF1 and FACT within the replication complex. a Western blot analysis of the indicated proteins in the CB fractions (left) and the FLAG-PCNA complexes purified from CB fractions (right) prepared from cells expressing the indicated FLAG-tagged proteins. Ub-KR indicates the FLAG-ubiquitin-PCNA (KR) fusion protein. b Western blot analysis of the indicated proteins in the CB input (left panels) used for the in vitro pull-down experiments of purified recombinant strep-tagged PCNA, SUMO2-conjugated PCNA, and GFP anchored to Strep-Tactin resins (right panels). SUMO2-modified PCNA was generated by the in vitro SUMOylation reaction using strep-PCNA and His-SUMO2 shown in Supplementary Fig. 6a, b. c Western blot analysis of the input levels of recombinant strep-PCNA and strep-SUMO2-PCNA fusion (S2-PCNA) purified from E. coli (left panel) and of strep-PCNA and strep-S2-PCNA pulled down by WT or SIM mutant FLAG-CAF1A proteins purified and anchored on FLAG M2 agarose beads from HEK293T cells expressing the corresponding constructs (right panels). d Western blot analysis of strep-S2-PCNA (upper 2 panels) and strep-PCNA (lower 2 panels) pulled down by FLAG-CAF1A purified from E. coli and anchored on FLAG M2 agarose beads. e Western blot analysis of the indicated proteins in the CB input prepared from HEK293T cells expressing FLAG-SSRP1 WT or SIM mutant (left panels) and of FLAG-SSRP1 and SPT16 pulled down from the CB fractions in vitro using purified recombinant strep-tagged PCNA, S2-PCNA, and GFP anchored to Strep-Tactin resins (right panels) Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/30006506), licensed under a CC-BY license. Not internally tested by Novus Biologicals.$

Restoration of nuclear PTEN-mediated DNA damage signalling by restraining CK2 impairs tumour but not normal neural stem cell survival.(a) Immunoblot analysis displaying the impact of TBB treatment (25 μM/24 h) on CK2 beta , PTEN, p-PTEN (S380/T382/T383), p-AKT (S473) and p-PRAS40 (T246) in GXP GBM3 & 4, with beta -actin used as loading control. (b) IF of PTEN with DAPI nuclear staining in dimethylsulfoxide (DMSO)- or TBB (25 μM/24 h)-treated cells in the absence of DOX or after 5 h of exposure to DOX (0.5 μM). DOX was added 5 h before the end point of DMSO or TBB treatment. Representative images are shown. Scale bars, 20 μm. (c) Co-IF of gamma H2AX and 53BP1 foci formation with DAPI nuclear staining in DMSO- or TBB (25 μM/24 h)-treated GXP NS or GBM2 with DOX−, or 1 h or 5 h of DOX (0.5 μM) exposure followed by 5 or 24 h of recovery time. Scale bars, 10 μm. A graph quantifying the percent of gamma H2AX-positive GXP NS or GBM2 cells (y axis) with DMSO or TBB treatment at indicated time points of DOX treatment (x axis) is summarized in the graph in (d). Error bars represent mean±s.d. Representative 100 cells were randomly selected for quantification. Cells with ≥5 foci were considered as gamma H2AX positive. (e) Co-IF of FANCD2 and gamma H2AX with DAPI nuclear staining in TBB (25 μM/24 h)-treated GXP GBM2 exposed to DOX (0.5 μM) 5 h before fixation. Scale bars, 10 μm. The percent of FANCD2/ gamma H2AX-positive foci at DSB sites (y axis) in TBB− or TBB+ (x axis) in GXP GBM2 is summarized in the graph shown in (f). Error bars represent mean±s.e.m. See also Supplementary Fig. 4. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/28094268), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

GRPs enhance axonal growth in DRGs in vitro. A–C, Representative montage images are shown for control dissociated DRG culture (A), dissociated DRGs cocultured with rat GRPs (B), and dissociated DRGs cultures exposed to conditioned medium from alkaline phosphatase-expressing rat GRPs (C). beta III-tubulin (red) immunofluorescence highlights the neurons; GRPs are visualized by immunostaining for alkaline phosphatase (green). D shows quantification for the average length of the longest axon per neuron ± SEM (n ≥ 30 neurons in three separate experiments; **p ≤ 0.01 by Student’s t test). Scale bar, 250 μm. Image collected and cropped by CiteAb from the following open publication (//www.eneuro.org/lookup/doi/10.1523/ENEURO.0171-16.2017), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Reactivity:

Hu, Mu, Rt, Ch, Ha, Bt, Bv, Ca, Pm, Eq, Fe, Pm

Species Glossary

Reactivity: Hu, Mu, Rt, Ch, Ha, Bt, Bv, Ca, Pm, Eq, Fe, Pm

Applications:

, , , , , , , , , , ,

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

Host:

Rabbit Polyclonal

Host: Rabbit Polyclonal

Sizes:

Sample Size Available

Sizes: Sample Size Available

Conjugate:

Unconjugated

Validated by:

Validated by:

Available Formulations

Formulation	Catalog #	Availability	Price
Purified	NBP3-25349-0.025mg
Purified	NBP3-25349-0.05mg

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NB100-182

FANCD2 Antibody - BSA Free

(8 Reviews)

(215 Publications)

0.05 ml

NB100-182

<b>Biological Strategies Validation. </b>Western Blot: FANCD2 Antibody - BSA Free [NB100-182] - FANCD2 Antibody [NB100-182] - AMPK-activating AICAR treatment activates FANCD2, a pivotal molecule of Fanconi anemia DNA damage signaling pathway. AICAR treatment induces FANCD2 monoubiquitination in transformed normal fibroblasts (GM00637I). GM00637I cells were treated with 1 mm 2-deoxyglucose, 0.25 mM AICAR, or 1 mm phenformin for 24 h. Lysates were subjected to western blotting with FANCD2 Antibody, phospho-AMPKalpha1 (T172), and AMPKalpha and beta-actin. In FANCD2 blots, the position of monoubiquitinated FANCD2 (Ub-FANCD2) is indicated by an arrow. Image collected and cropped by CiteAb from the following publication (//doi.wiley.com/10.1002/2211-5463.12185) licensed under a CC-BY license.

Simple Western: FANCD2 Antibody - BSA Free [NB100-182] - FANCD2 Antibody [NB100-182] - Simple Western lane view shows a specific band for FANCD2 in 0.1 mg/ml of HeLa lysate using FANCD2 Antibody. This experiment was performed under reducing conditions using the 12-230 kDa separation system.

Immunocytochemistry/Immunofluorescence: FANCD2 Antibody - BSA Free [NB100-182] - FANCD2 Antibody [NB100-182] - Analysis using the Biotin conjugate of FANCD2 Antibody. FANCD2 colocalizes in vivo with another protein in SiHa cells after cell exposure to IR. Proliferating SiHa cells were exposed to 10 Gy of IR and double color immunofluorescence staining was performed after 8 h. Images were captured in a Kodak digital image system on a Leica fluorescence microscope.

<b>Biological Strategies Validation. </b>Western Blot: FANCD2 Antibody - BSA Free [NB100-182] - FANCD2 Antibody [NB100-182] - AICAR-induced FANCD2 monoubiquitination is dependent on AMPK. Inhibitor of AMPK blocks AICAR-induced FANCD2 monoubiquitination in GM00637I normal fibroblasts. Cells were pretreated with 5 um of Compound C (an AMPK inhibitor) 1 h before treatment with 0.25 mm AICAR for 24 h. Cell lysates were subjected to immunoblotting with FANCD2 Antibody to visualize monoubiquitinated FANCD2 (Ub-ANCD2). Image collected and cropped by CiteAb from the following publication (//doi.wiley.com/10.1002/2211-5463.12185) licensed under a CC-BY license.

Western Blot: FANCD2 Antibody - BSA Free [NB100-182] - FANCD2 Antibody [NB100-182] - The FA-BRCA Pathway Is Activated on the Sex Chromosomes during Meiosis. Schematic of the FA-BRCA pathway. FA proteins analyzed in this study are shown in color. Western blot analysis with three independent anti-FANCD2 antibodies (G33, E33, and Novus NB100-182 antibody: NB). K561R, PD20 cells expressing a mutated form of FANCD2 incapable of monoubiquitination; WT, PD20 cells complemented with wild-type FANCD2; Vector, PD20 cells containing empty vector. Image collected and cropped by CiteAb from the following publication (//linkinghub.elsevier.com/retrieve/pii/S2211124716313298), licensed under a CC-BY license.

<b>Biological Strategies Validation. </b>Immunocytochemistry/Immunofluorescence: FANCD2 Antibody - BSA Free [NB100-182] - FANCD2 Antibody [NB100-182] - HES1K109E mutation does not impair MMC-induced HES1 foci formation. HeLa cells transfected with HA-tagged HES1 or HES1K109E coding vectors were processed for immunofluorescence 16 h following treatment with MMC (120 ng/ml). Cells were double-stained with anti-HA and anti-FANCD2 antibodies (mouse anti-HA at 1:500; rabbit anti-FANCD2, Novus Biologicals NB100-182 at 1:2000) followed with secondary antibodies (Goat anti-mouse Alexafluor-555, ThermoScientific A-32727 and goat anti-rabbit Alexafluor-488, ThermoScientific, A-11008). Cell nuclei were labelled with TO-PRO-3 Iodide stain (1:400, ThermoScientific, T3605). Cells were visualized at 100x magnification. Image collected and cropped by CiteAb from the following publication (//bmcresnotes.biomedcentral.com/articles/10.1186/s13104-018-3243-7), licensed under a CC-BY license.

Immunohistochemistry: FANCD2 Antibody - BSA Free [NB100-182] - FANCD2 Antibody [NB100-182] - The tissue sections were incubated with a primary antibody cocktail of FANCD2 Antibody (NB100-182) at a dilution of 1:1000 & a monoclonal anti-Ki67 mouse antibody at a dilution of 1:150 for 1 h at room temperature. Then the slides were incubated with a secondary antibody cocktail containing FITC conjugated anti-rabbit IgG and Alexafluor 594 donkey anti-mouse secondary. The sections were mounted on glass slides using a DAPI-containing embedding medium (Vysis Dapi 1, Abbott Laboratories, Downers Grove, IL, USA), then analyzed under a fluorescence microscope. FANCD2 (top) foci positive NSCL tumor, and FANCD2 (bottom)foci negative NSCL tumor. Magnification: 1000x. Image collected and cropped by CiteAb from the following publication (//journal.frontiersin.org/article/10.3389/fonc.2014.00368/abstract), licensed under a CC-BY license.

Western Blot: FANCD2 Antibody [NB100-182] - Analysis of FANCD2 (Molecular weight: 164.1 KDa) using the HRP conjugate of FANCD2 Antibody (lot C) in HeLa WCE.

Western Blot: FANCD2 Antibody [NB100-182] - Functional assessment of Fanconi anemia pathway. Western blot with FANCD2 Antibody of non-FA control lymphoblasts (LCL), proband LCL-A-2017, proband LCL-B-2017, FANCB mutant (null) LCL, and FANCD2 mutant (null) LCL. Image collected and cropped by CiteAb from the following publication (//doi.wiley.com/10.1002/mgg3.350), licensed under a CC-BY license.

Immunocytochemistry/Immunofluorescence: FANCD2 Antibody [NB100-182] - Mouse Embryonic Fibroblasts Untreated and treated with Mitomycin C for 24hr with FANCD2 Antibody diluted 1:500 in 15%BCS+0.3% Triton X 100 in PBS. This image was submitted via customer Review.

Immunohistochemistry: FANCD2 Antibody [NB100-182] - Staining of human prostate, glandular epithelium using FANCD2 Antibody. Image using the Biotin format of this antibody.

Representative images of the cellular response to RS (induced by a low dose of hydroxyurea; HU) in U2OS cells, as determined by IF staining for gamma H2AX and FANCD2A selected cell is defined by the yellow arrow, and is enlarged in the bottom panel. Scale bars are indicated.

Chemical library screening for small molecules that inhibit the Fanconi anemia pathway. (A) Schematic of the screening for small molecules that inhibit IR-induced FANCD2 foci formation. (B) Representative photomicrographs of EGFP-FANCD2 foci in PD20F-EGFP-FANCD2 cells untreated and treated with the indicated compounds at the indicated concentration. The cells were treated with compounds immediately before irradiation (15 Gy), and fixed after 12 hours. (C) FANCD2 foci in HeLa cells untreated and treated with the indicated compounds at the indicated concentration. The cells were fixed 8 hours after irradiation (10 Gy) and immunostained with anti-FANCD2 antibody. Scale bar = 20 um. Image collected and cropped by CiteAb from the following publication (//molecular-cancer.biomedcentral.com/articles/10.1186/1476-4598-11-26), licensed under a CC-BY licence.

The FA-BRCA Pathway Is Activated on the Sex Chromosomes during Meiosis. (F) Western blot analysis with three independent anti-FANCD2 antibodies (G33, E33, and Novus NB100-182 antibody: NB). K561R, PD20 cells expressing a mutated form of FANCD2 incapable of monoubiquitination; WT, PD20 cells complemented with wild-type FANCD2; Vector, PD20 cells containing empty vector. Image collected and cropped by CiteAb from the following publication (//linkinghub.elsevier.com/retrieve/pii/S2211124716313298), licensed under a CC-BY licence.

HES1 mono-ubiquitination is not required for foci formation. a HES1K109E mutation does not impair MMC-induced HES1 foci formation. HeLa cells transfected with HA-tagged HES1 or HES1K109E coding vectors were processed for immunofluorescence 16 h following treatment with MMC (120 ng/ml). Cells were double-stained with anti-HA and anti-FANCD2 antibodies (mouse anti-HA at 1:500; rabbit anti-FANCD2, Novus Biologicals NB100-182 at 1:2000) followed with secondary antibodies (Goat anti-mouse Alexafluor-555, ThermoScientific A-32727 and goat anti-rabbit Alexafluor-488, ThermoScientific, A-11008). Cell nuclei were labelled with TO-PRO-3 Iodide stain (1:400, ThermoScientific, T3605). Cells were visualized at 100x magnification. b HES1 lysine 109 plays a role in MMC-induced activation of the HES1 promoter. COS-1 cells transfected with pHES1pro-Luc and HES1 or HES1K109E coding vectors (0.034 ug) were treated with 120 ng/ml MMC. Empty vectors were used as controls. Experiments were done twice in triplicates. 2-way ANOVA with Bonferroni correction test, *p 10 larvae/sample). The blots were probed with antibodies against Lc3 and Actin as a loading control and Lc3-II/Lc3-I ratios are indicated below. Western blots were repeated twice with independent extracts. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/30818338), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Ddx19 is specifically required for the nuclear localization of MKL1.(a) Western blotting (WB) of cells treated with control (Ctrl) or Ddx19 siRNAs (si). (b) Localization of MKL1-GFP (left panels) and endogenous MKL1 ( alpha -MKL1; right panel) in serum (FBS)-stimulated NIH 3T3 cells. Scale bars, 20 μm. (c) Quantification of MKL1-GFP localization in serum-starved (0.3% FBS), serum-stimulated (15% FBS) and LMB-treated control (−) or Ddx19 (+) siRNA-transfected cells. C, cytoplasmic; N/C, pancellular; N, nuclear. One hundred cells per point; n=3; error bars are s.e.m. (d) Localization of nuclear proteins in NIH 3T3 cells transfected with control (−) or Ddx19 (+) siRNA. SRF (serum response factor), RanBPI-delta NES (Ran binding protein 1 lacking nuclear export signal), hnRNPU (heterogeneous nuclear ribonucleoprotein U), Smad4+LMB (Smad4 stimulated with leptomycin B), MC (myocardin). More than fifty cells per point; n=2; error bars are s.d. (e) Localization of NLS-2GFP-NES in serum-starved (0.3% FBS) or LMB-treated cells transfected with control (−) or Ddx19 (+) siRNAs. One hundred cells per point; n=2; error bars are s.d. Image collected and cropped by CiteAb from the following open publication (//www.nature.com/articles/ncomms6978), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Reactivity:

Hu, Mu, Rt, Av, Ca, Ma, Pm, Ze

Species Glossary

Reactivity: Hu, Mu, Rt, Av, Ca, Ma, Pm, Ze

Applications:

, , , , , , , , , , ,

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

Host:

Rabbit Polyclonal

Host: Rabbit Polyclonal

Sizes:

Sample Size Available

Sizes: Sample Size Available

Conjugate:

Unconjugated

Available Conjugates:

Validated by:

Validated by:

Conjugate	Catalog #	Availability	Size	Price
Alexa Fluor 405	NB100-182AF405
Alexa Fluor 488	NB100-182AF488
Alexa Fluor 647	NB100-182AF647
Alexa Fluor 700	NB100-182AF700
Biotin	NB100-182B
DyLight 405	NB100-182V
DyLight 488	NB100-182G
DyLight 550	NB100-182R
DyLight 650	NB100-182C
FITC	NB100-182F
HRP	NB100-182H

Available Formulations

Formulation	Catalog #	Availability	Price
BSA Free	NB100-182SS

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NB100-143

Nbs1 Antibody

(8 Reviews)

(199 Publications)

0.05 ml

NB100-143

Immunocytochemistry/Immunofluorescence: Nbs1 Antibody [NB100-143] - ICC/IF analysis of Nbs1 in HeLa cells with Nbs1 Antibody [NB100-143]. Image from verified customer review.

Immunohistochemistry-Paraffin: Nbs1 Antibody [NB100-143] - FFPE human testis using Nbs1 antibody [NB100-143] at 1:200 on a Bond Rx autostainer (Leica Biosystems). The assay involved 20 minutes of heat induced antigen retrieval (HIER) using 10 mM sodium citrate buffer (pH 6.0) and endogenous peroxidase quenching with peroxide block. The sections were incubated with primary antibody for 30 minutes and Bond Polymer Refine Detection (Leica Biosystems) with DAB was used for signal development followed by counterstaining with hematoxylin. Whole slide scanning and capturing of representative images was performed using Aperio AT2 (Leica Biosystems). Staining was performed by Histowiz.

Western Blot: Nbs1 Antibody [NB100-143] - Analysis of HeLa whole cell lysate [NB800-PC1] using rabbit polyclonal NBS1 antibody [NB100-143]. Observed Molecular Weight at ~95 kDa.

<b>Genetic Strategies Validation. </b>Western Blot: Nbs1 Antibody [NB100-143] - Detection of NBS1 in Human Bone Osteosarcoma Epithelial Cells (U2OS whole cell lysate) using Nbs1 Antibody [NB100-143] at a dilution of 1:1000. Specificity was confirmed using a siRNA anti-NBS1 (targeting sequence: GGAAGAAACGUGAACUCAA). Image provided by Sebastien Britton of the Institute of Pharmacology and Structural Biology.

Western Blot: Nbs1 Antibody [NB100-143] - Western Blot with Nbs1 Antibody [NB100-143]. TIG-1 human primary fibroblasts, whole cell lysate (30 ug). Image from verified customer review.

Immunocytochemistry/Immunofluorescence: Nbs1 Antibody [NB100-143] - Staining of HeLa cells using Nbs1 Antibody [NB100-143].

<b>Genetic Strategies Validation. </b>Knockdown Validated: Nbs1 Antibody [NB100-143] - TOPBP1 recruitment in response to rDNA breaks. TOPBP1 localization 2 h after I-Ppo1 transfection in NBS1-delta-N cells and NBS1-delta-N cells complemented with wild-type and mutant NBS1-mNG (percentage of cells with > 2 TOPBP1 caps are indicated; one of two experiments is shown). Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31913317/) licensed under a CC-BY license.

HPV16 E2 partially colocalizes with the MRN complex proteins Mre11 and Nbs1. C33a cells were transfected with an HPV16 E2 expression plasmid, fixed in ice-cold methanol, and stained with an E2-specific antibody (green). DNA was stained with Hoechst 33342 (blue). (A) Endogenous Nbs1 was detected with an Nbs1-specific antibody (red/gray). (B) Endogenous Mre11 was detected with an Mre11-specific rabbit antibody (red/gray). Bar, 5 μm. Digital zoom is shown at the bottom.

TOPBP1 recruitment in response to rDNA breaks. b) TOPBP1 localization 2 h after I-Ppo1 transfection in NBS1deltaN cells and NBS1deltaN cells complemented with wild-type and mutant NBS1-mNG (percentage of cells with > 2 TOPBP1 caps are indicated; one of two experiments is shown). Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31913317), licensed under a CC-BY licence.

ATM promotes cell migration and invasion independently of DNA DSB signaling in MDA-MB-231 cells.(B and C) Quantification of wound healing (B) and siRNA depletions (C) in (A). Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/26030852), licensed under a CC-BY licence.

KSHV LANA recruits MRN (Mre11-Rad50-NBS1) complex.(A) Co-immunoprecipitation of endogenous LANA and MRN proteins in BC3 cells. Cells were lysed using TBS-T buffer and the cell lysate was incubated with benzonase. After centrifugation, supernatant was incubated overnight with anti-LANA or IgG-control beads. The precipitated complexes were analyzed for the presence of endogenous Rad50, Mre11 and NBS1 by SDS-PAGE and immunoblotting. For the input, see Materials and methods. Image collected and cropped by CiteAb from the following publication (//dx.plos.org/10.1371/journal.ppat.1006335), licensed under a CC-BY licence.

Replication centers of the integrated HPV recruit Mre11-Nbs1-Rad50 complex and Ku70/80 heterodimer.HeLa cells were transfected and analyzed as described previously. Co-immunostaining of HPV18 E1 (Alexa Fluor 568, second column) and the following proteins are presented: Mre11, Nbs1, Rad50, and Ku70/80 proteins (Alexa Fluor 488, first column). The localizations of the E1 and the respective DNA repair proteins are also shown in the third column as a merged image and DAPI stained nuclei are presented in the fourth column. Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/19390600), licensed under a CC-BY licence.

TRIB3 suppresses the functions of the UBE3B:MYC axis to attenuate lymphomagenesis.a Occupancy heatmap of genome-wide MYC peaks in MYCWT and MYCK427R Raji cells in a window of ±10 kb surrounding the transcription start site (TSS). b Distribution of MYC tags in MYCWT and MYCK427A Raji cells. Binding is shown for a window of ±2 kb around MYC tags as reference coordinates. c GSEA shows global downregulation of MYC target genes in Ad-UBE3B versus Ad-CTRL Raji cells. d Metagene plots of global RNAPII occupancy at gene bodies in Raji cells with or without UBE3B overexpression. e Colony-forming capacity of Raji cells with or without UBE3B overexpression. The data are presented as the means ± S.E.M from three independent experiments. Statistical significance was determined by two-tailed Student’s t test. P value: 0.00047. f Relative cell viabilities of Raji cells with overexpression of the indicated genes for the indicated times. The colors represent different time points; the diameter indicates the relative cell viability. The data are presented as the means ± S.E.M from three independent experiments. g Schematic strategy for studying BCL development in MycEμ mice with the indicated infection of Ad-GFP, Ad-Ube3b, Ad-Trib3, or Ad-Ube3b plus Ad-Trib3 in vivo. h Data are the spleen weights of MycEμ mice (n = 8 per group) with overexpression of the indicated genes. Data are represented as means ± SEM. Statistical significance was determined by two-tailed Student’s t test. P values: 2.077 × 10−5, 0.0009. i Data are representative LNs in MycEμ mice overexpressing Ad-GFP, Ad-Ube3b, Ad-Trib3, or Ad-Ube3b plus Ad-Trib3. Scale bar, 0.5 cm. j Cell proliferation was determined by Ki67 staining in the spleens of the indicated mice (n = 6 per group). Data are representative images of Ki67 staining and statistical analyses of Ki67-positive cells. Data are represented as means ± SEM. Statistical significance was determined by two-tailed Student’s t test. P values: 1.352 × 10−12, 3.674 × 10−8. Scale bar, 50 μm. k Approaches to defining the self-renewal ability of mouse LCs from the indicated mice (5 months old). l Colony-forming ability of BCL cells isolated from MycEμ mice (n = 6 per group) overexpressing Ad-GFP, Ad-Ube3b, Ad-Trib3, or Ad-Ube3b plus Ad-Trib3. Data are represented as means ± SEM. Statistical significance was determined by two-tailed Student’s t test. P values: 4.318 × 10−5, 0.0001. m The tumorigenicity of BCL cells from the indicated mice was compared by limiting dilution transplantation into NSG mice; n = 8 mice per group. n Schematic strategy for studying BCL development in MycEμCD19CreTrib3F/+ mice infected with or without lentivirus Ube3bCas9. o Kaplan–Meier survival curves for MycEμCD19CreTrib3F/+ mice infected with or without lentivirus Ube3bCas9 (n = 8 per group). Statistical difference was determined by two-sided log-rank test. P value: 0.0002. p Expression of MYC in the spleens of MycEμCD19CreTrib3F/+ mice (5 months old) infected with or without lentivirus Ube3bCas9. The data are presented as presentative from three independent experiments. q Colony-forming ability of BCL cells isolated from the LNs of the indicated mice (n = 6 per group). The data are representative or the means ± SEM of three assays. Statistical significance was determined by two-tailed Student’s t test. P value: 5.417 × 10−5, 0.0042. The MycEμCreCD19Trib3F/+ mice are heterozygous for the MycEμ allele. 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/33298911), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

$The BNIP3 C-terminus can be phosphorylated.(A) Western blot detection of immunoprecipitated BNIP3 using an alpha -PKA substrate antibody specific to the phosphorylated RRXS/T sequence, located at the BNIP3 C-terminus and adjacent to the transmembrane (TM) domain. Results shown for 4 cell types: (left to right) HEK 293 cells expressing exogenous BNIP3 (dimer, 60 kD), and A549, MDA-MD-231, and AU565 cells expressing endogenous BNIP3 (monomer, 30kD). Lane 1 of each Western blot contains the whole cell lysate (WCL). (B) LC-MS/MS analysis of BNIP3 phosphorylation in HEK 293 cells with normal or elevated cAMP (8-Bromo-cAMP), showing peptide coverage (gray) and phosphorylation sites (red). The TM domain is underlined. (C) Table of BNIP3 phosphopeptides identified by LC-MS/MS, showing the percent probability, ion charge, actual and observed masses, and mass error (Da and ppm) for each peptide. Peptides shown are from analysis of BNIP3 purified from HEK 293 cells with elevated cAMP levels. (D) Schematic of the BNIP3 protein sequence, showing each C-terminal mutation representing phosphomimetic or nonphosphorylated BNIP3. (E) Expression of BNIP3 phosphomutants from stable doxycycline-inducible HEK 293 Tet On cells, treated with doxycycline (Dox) for 48 hr. (F) Subcellular localization of BNIP3 phosphomutants, showing Western blot of cytosolic and mitochondrial fractions. (G) Alkaline extraction of mitochondria-associated proteins, showing alkaline extract of the mitochondrial pellet and the alkaline-resistant mitochondrial pellet from cells expressing each BNIP3 phosphomutant. All blots are representative of at least 3 independent experiments. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/26102349), licensed under a CC-BY license. Not internally tested by Novus Biologicals.$

$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.$

mTOR complex protein expressions and rictor phosphorylation at Ser1235.Cardiomyocytes were pretreated for 30 min with 20 nM rapamycin and then stimulated with 10 nM IGF-1 in presence or absence of 10 nM E2 for 24 h. A, shown are representative western blots for mTOR, rictor and raptor and B,C,D, quantitative analysis with mean ± SEM of fold stimulation by IGF-1 of at least 3 independently performed experiments (B,C,D). * p < 0.05, **p < 0.0095. Exposure to rapamycin lead to downregulation of mTOR and rictor, which were more pronounced under culture conditions without E2. E, Western blots for GSK3 beta -pS9, GSK3 beta , rictor pS1235 and rictor and F,G,H,I quantitative analysis of at least 3 independently performed experiments indicate that rictor phosphorylation at S1235 by GSK-3 beta which has been reported to interfere with Akt-substrate binding to mTORC2, thereby downregulating mTORC2 activity. IGF-1 induced strong phosphorylation of GSK-3 beta at Ser9 in the absence and presence of E2, however, rapamycin pretreatment only reduced this increased phosphorylation in E2 co-treated cardiomyocytes, indicating increased activity of GSK-3 beta . This higher activity was not associated with increased phosphorylation of rictor at S1235. Image collected and cropped by CiteAb from the following open publication (//dx.plos.org/10.1371/journal.pone.0123385), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Reactivity:

Hu, Mu, Ha, Ma, Pm

Species Glossary

Reactivity: Hu, Mu, Ha, Ma, Pm

Applications:

, , , , , , , , , , , ,

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

Host:

Rabbit Polyclonal

Host: Rabbit Polyclonal

Sizes:

Sample Size Available

Sizes: Sample Size Available

Conjugate:

Unconjugated

Validated by:

Validated by:

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NB100-384

Histone H2AX [p Ser139] Antibody

(1 Review)

(156 Publications)

0.1 ml

NB100-384

Detection of Human and Mouse Histone H2AX [p Ser139] by Western Blot. Samples: Nuclear extract (50 ug) from human HEK293, human melanoma (G361), mouse wildtype embryonic fibroblasts (+/+) or mouse H2AX knockout embryonic fibroblasts (-/-). Antibody: Affinity purified rabbit Histone H2AX [p Ser139] antibody NB100-384 used at 0.1 ug/ml. Detection: Chemiluminescence with 30 second exposure. (NCS, neocarzinostatin - 200 ng/ml, 30 min). Bands appear at an observed molecular weight of ~15 kDa.

<b>Biological Strategies Validation and Genetic Strategies Validation.</b>Samples: Neocarzinostatin treated asynchronous HeLa cells (left) and untreated asynchronous HeLa cells (right) . Antibody: Affinity purified rabbit Histone H2AX [p Ser139] used at a dilution of 1:5,000 (0.2ug/ml). Detection: Red fluorescent Anti-rabbit IgG-DyLight 594 used at a dilution of 1:100.

Simple Western lane view shows a specific band for Histone H2AX [p Ser139] in 0.2 mg/ml of Jurkat lysate(s). This experiment was performed under reducing conditions using the 12 - 230 kDa separation system.

<b>Biological Strategies Validation. </b>Immunocompromised mice were subcutaneously injected with cancerous cell lines and tumors were allowed to establish. Treatments occurred every other day and the studied compound or the equivalent vehicle control administered intraperitoneally for five weeks. Tumor volume and mass were measured two times per week. IHC analysis of sectioned tumor tissues from the MDA-MB-231 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. Image collected and cropped by CiteAb from the following publication (nature.com/articles/s41598-017-01230-4), licensed under a CC-BY license.

Immunostaining of Histone H2AX [p Ser139] WT1 and 5mC in patients with IgA nephropathy and controls. Examples of PAS staining and immunostaining with Histone H2AX [p Ser139] (green) and WT1 (red), pATM and 5mC in glomeruli of IgA nephropathy and controls. A kidney sample of a 65-year-old male of IgA nephropathy without podocytopathic features. Arrows indicate Histone H2AX [p Ser139] and WT1 double-positive cells. Scale bars: 50um. Image collected and cropped by CiteAb from the following publication (//www.nature.com/articles/s41598-019-57140-0) licensed under a CC-BY license.

<b>Biological Strategies Validation. </b>Samples: Nuclear extract from HeLa cells treated with 100 uM EPE for 4 hours (+) or mock treated (-). Antibody: Affinity purified rabbit Histone H2AX [p Ser139] antibody used at 0.1 ug/ml. Detection: Chemiluminescence with an exposure time of 3 minutes. Band appears at an observed molecular weight of ~17 kDa.

<b>Biological Strategies Validation. </b>Detection of human Histone H2AX [p Ser139] by western blot. Samples: Whole cell lysate (50 ug) from Jurkat cells treated with 100 uM EPE for 4 hours (+) or mock treated (-). Antibody: Affinity purified rabbit Histone H2AX [p Ser139] antibody NB100-384 used for WB at 0.1 ug/ml. Detection: Chemiluminescence with an exposure time of 3 seconds. Band appears at an observed molecular weight of ~18 kDa.

FFPE section of mouse CT26 colon carcinoma. Antibody: Affinity purified rabbi Histone H2AX [p Ser139] antibody used at a dilution of 1:1,000 (1 ug/ml). Detection: DAB.

Analysis of Histone H2AX [p Ser139] in EPE Treated Jurkat Cells. Cells were treated for 3 hrs in 5ug/ml etoposide, fixed in 1.5% PFA, and permeabilized in 90% Methanol. 1 million cells were stained with 0.5 ug anti-KLH or anti-H2AX NB100-384 and secondary FITC-conjugated goat anti-rabbit (in a 150ul reaction). Black- etosposide treated, anti-KLH; Red- untreated, anti-Histone H2AX [p Ser139]; Blue- etoposide treated , anti-Histone H2AX [p Ser139].

FFPE section of human ovarian carcinoma. Antibody: Affinity purified rabbit Histone H2AX [p Ser139] antibody used at a dilution of 1:5,000 (0.2 ug/ml). Detection: DAB.

Electropherogram image(s) of corresponding Simple Western lane view. Histone H2AX [p Ser139] antibody was used at 5 ug/ml dilution on Jurkat lysate(s).

Immunohistochemistry: Rabbit Polyclonal Histone H2AX [p Ser139] Antibody - Histone H2AX Antibody on mouse cancer tissue. H2AX (Gray) and H2BGFP(Green). Primary antibody dilution: 1:1000 in a 10um slice.

mTORC1/2 activity prevents Cisplatin-induced cell death in MCF-10A cells. (A) Western blot displaying effects on mTOR signaling during a dose escalation of PP242 treatment in MCF-10A cells; (B) Western blot displaying effects of mTOR signaling on a dose escalation of cisplatin treatment in MCF-10A cells; (C) Western blot displaying effects on mTOR signaling and cell death during non-treated, Cisplatin, PP242, and Cisplatin + PP242-treated MCF-10A cells.

ERM expression and localization in SKBR3 breast cancer cells(A) Western blot analysis of ERM levels in SKBR3, HeLa and PC3 cells. SKBR3 breast cancer cells do not express moesin. (B) Colocalization of ezrin/radixin and ErbB2 in SKBR3 cells. 3D-SIM of fixed cells, stained for endogenous ERM and ErbB2, shows a high degree of colocalization between the ezrin/radixin and ErbB2 at the plasma membrane (left panel: max. projection; middle: single plane section; right: single channels of insert). Scale bars: 10 μm. (C) Analysis of protein association in SKBR3 cells by proximity ligation assay (PLA). 2 h treatment with 3 μM GA leads to decreased association of ezrin/ErbB2 and radixin/ErbB2. Data is represented as mean +/− SEM (***P 1.0 mm, >2.0 mm) are shown. Data are expressed as the mean ± SD (n = 3, *p < 0.01 by t-test). Representative data from three independent experiments are shown. c, d hCB LT-HSCs were cultured for 10 days with control MTM protein or MTM-POT1. After 10 days of culture, LT-HSCs were re-isolated and number of TIF was examined. c Immunocytochemical staining of TRF1 (green), 53BP1 (red), and TOTO3 (blue). Scale bar, 2 μm (left). Frequencies of TIFs after 10 days of culture (right). Data are expressed as the mean ± SD (n = 100: control, n = 100: MTM-POT1, *p < 0.01 by t-test). Representative data from 2 independent experiments are shown. d Immunocytochemical staining of TRF1 (green), RPA32 (red), and TOTO3 (blue). Scale bar, 2 μm (left). Frequencies of TIFs after 10 days of culture (right). Data are expressed as the mean ± SD (n = 110–120: control, n = 110: MTM-POT1, *p < 0.01 by t-test). Representative data from two independent experiments are shown Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/28986560), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Cell numbers positively stained for NeuN, DCX, PCNA and caspase-3 in the subgranular region of the dentate gyrus in WT and RanBP9−/− (KO) mice.(A), DAPI-stained brain sections to show the highlighted subgranular zone within the dentate gyrus region of the hippocampus used for cell counts shown in B. (B), Representative brain sections stained with anti-NeuN, anti-DCX, anti-PCNA, anti-capsase-3 and counter stained with DAPI. Cell counting revealed significantly decreased numbers of NeuN positive cells in RanBP9−/− (KO) brains (22%) compared to WT controls. However DCX, PCNA and caspase positive cell numbers were not significantly altered. In each group, n = 3, data presented as mean± SEM. **, p<0.01 by Student’s t-test. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/23840553), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

SAN1 functions independently of the FA pathway and does not affect FA pathway activation. a, b CSAs of HeLa WT and SAN1−/− cells treated with scrambled ctrl siRNA or FANCD2 siRNA, in response to Cisplatin and MMC (N = 3). Statistical significance determined by two-way ANOVA. Error bars denote s.e.m. *p < 0.05, **p < 0.01, ***p < 0.001, ****p < 0.0001. c Immunoblot showing siRNA knockdown of FANCD2 in HeLa WT and SAN1−/− cells. d IF staining of FANCD2 foci in HeLa WT cells and SAN1−/− cells treated with 0.045 μM MMC. e Immunoblot of FANCD2 showing mono-ubiquitylation in HeLa WT and SAN1−/− cells treated with vehicle or 0.045 μM MMC. f, g CSAs of HeLa WT and SAN1−/− cells treated with ctrl or SNM1A siRNA and exposed to Cisplatin or MMC. Statistical significance was determined by two-way ANOVA test. h Immunoblot of SNM1A in HeLa WT and SAN1−/− cells treated with ctrl or SNM1A siRNA Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/29968717), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Reactivity:

Hu, Mu, Rt, Ca

Species Glossary

Reactivity: Hu, Mu, Rt, Ca

Applications:

, , , , , ,

Applications: , , , , , ,

Host:

Rabbit Polyclonal

Host: Rabbit Polyclonal

Conjugate:

Unconjugated

Available Conjugates:

Validated by:

Validated by:

Conjugate	Catalog #	Availability	Size	Price
Alexa Fluor 350	NB100-384AF350
Alexa Fluor 405	NB100-384AF405
Alexa Fluor 488	NB100-384AF488
Alexa Fluor 532	NB100-384AF532
Alexa Fluor 594	NB100-384AF594
Alexa Fluor 647	NB100-384AF647
Alexa Fluor 700	NB100-384AF700
Alexa Fluor 750	NB100-384AF750
Allophycocyanin	NB100-384APC
Biotin	NB100-384B
DyLight 350	NB100-384UV
DyLight 405	NB100-384V
DyLight 488	NB100-384G
DyLight 550	NB100-384R
DyLight 594	NB100-384DL594
DyLight 650	NB100-384C
DyLight 680	NB100-384FR
DyLight 755	NB100-384IR
FITC	NB100-384F
HRP	NB100-384H
Janelia Fluor 549	NB100-384JF549
Janelia Fluor 646	NB100-384JF646
PE	NB100-384PE
PerCP	NB100-384PCP
mFluor Violet 450 SE	NB100-384MFV450
mFluor Violet 500 SE	NB100-384MFV500
mFluor Violet 610 SE	NB100-384MFV610

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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

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NBP2-54753

53BP1 Antibody (1285C) - BSA Free

(2 Publications)

0.1 mg

NBP2-54753

Immunocytochemistry/Immunofluorescence: 53BP1 Antibody (1285C) [NBP2-54753] - Neuro2a cells were fixed for 10 minutes using 10% formalin and then permeabilized for 5 minutes using 1X TBS + 0.5% Triton-X100. The cells were incubated with 53BP1 Antibody at 5 ug/ml overnight at 4C and detected with an anti-rabbit Dylight 488 (Green) at a 1:500 dilution. Alpha tubulin (DM1A) (Catalog #NB100-690) was used as a co-stain at a 1:1000 dilution and detected with an anti-mouse Dylight 550 (Red) at a 1:500 dilution. Nuclei were counterstained with DAPI (Blue). Cells were imaged using a 40X objective.

Flow (Intracellular): 53BP1 Antibody (1285C) [NBP2-54753] - An intracellular stain was performed on HeLa Cells with 53BP1 (1285C) antibody (Catalog #NBP2-54753) (blue) and a matched isotype control MAB1050 (orange). Cells were fixed with 4% paraformaldehyde, following fixation, cells were permeabilized with 0.1% saponin. Cells were incubated in an antibody dilution of 1 ug/mL for 30 minutes at room temperature, followed by rabbit IgG APC-conjugated secondary antibody (F0111, R&D Systems).

Immunocytochemistry/Immunofluorescence: 53BP1 Antibody (1285C) [NBP2-54753] - 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 [1285C] NBP2-54753 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 (1285C) [NBP2-54753] - An intracellular stain was performed on Ntera2 cells with 53BP1 Antibody [1285C] NBP2-54753 (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 (1285C) [NBP2-54753] - HeLa cells were fixed for 10 minutes using 10% formalin and then permeabilized for 5 minutes using 1X TBS + 0.5% Triton-X100. The cells were incubated with 53BP1 Antibody at 5 ug/ml overnight at 4C and detected with an anti-rabbit Dylight 488 (Green) at a 1:500 dilution. Alpha tubulin (DM1A) (Catalog #NB100-690) was used as a co-stain at a 1:1000 dilution and detected with an anti-mouse Dylight 550 (Red) at a 1:500 dilution. Nuclei were counterstained with DAPI (Blue). Cells were imaged using a 40X objective.

Immunocytochemistry/Immunofluorescence: 53BP1 Antibody (1285C) [NBP2-54753] - NIH-3T3 cells were fixed for 10 minutes using 10% formalin and then permeabilized for 5 minutes using 1X TBS + 0.5% Triton-X100. The cells were incubated with 53BP1 Antibody at 5 ug/ml overnight at 4C and detected with an anti-rabbit Dylight 488 (Green) at a 1:500 dilution. Alpha tubulin (DM1A) (Catalog #NB100-690) was used as a co-stain at a 1:1000 dilution and detected with an anti-mouse Dylight 550 (Red) at a 1:500 dilution. Nuclei were counterstained with DAPI (Blue). Cells were imaged using a 40X objective.

Immunocytochemistry/Immunofluorescence: 53BP1 Antibody (1285C) [NBP2-54753] - 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 [1285C] NBP2-54753 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.

Reactivity:

Hu, Mu, Rt, Po, Bv, Ca, Eq, Fe, Pm

Species Glossary

Reactivity: Hu, Mu, Rt, Po, Bv, Ca, Eq, Fe, Pm

Applications:

, , ,

Applications: , , ,

Host:

Rabbit Monoclonal

Host: Rabbit Monoclonal

Sizes:

Sample Size Available

Sizes: Sample Size Available

Conjugate:

Unconjugated

Available Conjugates:

Conjugate	Catalog #	Availability	Size	Price
Alexa Fluor 350	NBP2-54753AF350
Alexa Fluor 405	NBP2-54753AF405
Alexa Fluor 488	NBP2-54753AF488
Alexa Fluor 532	NBP2-54753AF532
Alexa Fluor 594	NBP2-54753AF594
Alexa Fluor 647	NBP2-54753AF647
Alexa Fluor 700	NBP2-54753AF700
Alexa Fluor 750	NBP2-54753AF750
Allophycocyanin	NBP2-54753APC
Biotin	NBP2-54753B
DyLight 350	NBP2-54753UV
DyLight 405	NBP2-54753V
DyLight 488	NBP2-54753G
DyLight 550	NBP2-54753R
DyLight 594	NBP2-54753DL594
DyLight 650	NBP2-54753C
DyLight 680	NBP2-54753FR
DyLight 755	NBP2-54753IR
FITC	NBP2-54753F
HRP	NBP2-54753H
Janelia Fluor 549	NBP2-54753JF549
Janelia Fluor 646	NBP2-54753JF646
PE	NBP2-54753PE
PerCP	NBP2-54753PCP
mFluor Violet 450 SE	NBP2-54753MFV450
mFluor Violet 500 SE	NBP2-54753MFV500
mFluor Violet 610 SE	NBP2-54753MFV610

Available Formulations

Formulation	Catalog #	Availability	Price
BSA Free	NBP2-54753SS
Azide and BSA Free	NBP2-80550

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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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NB100-309

ATM Antibody (2C1)

(3 Reviews)

(130 Publications)

100 ul

NB100-309

Western Blot: ATM Antibody (2C1) [NB100-309] - Detection of human ATM protein using ATM antibody (2C1) [NB100-309] by western blot or immunoprecipitation. Theoretical molecular weight 351 kDa.

Immunohistochemistry-Paraffin: ATM Antibody (2C1) [NB100-309] - Human breast carcinoma. ATM stained by ATM antibody [2C1] diluted at 1:100.Antigen Retrieval: Citrate buffer, pH 6.0, 15 min.

Western Blot: ATM Antibody (2C1) [NB100-309] - Analysis of ATM in U2OS sarcoma cells using ATM antibody (2C1) [NB100-309]. Theoretical molecular weight 351 kDa. Western blot image submitted by a verifeid customer review.

Western Blot: ATM Antibody (2C1) [NB100-309] - Whole cell extract (30 ug) was separated by 5% SDS-PAGE, and the membrane was blotted with ATM antibody (2C1) [NB100-309] diluted at 1:1000. Theoretical molecular weight 351 kDa.

Immunohistochemistry-Paraffin: ATM Antibody (2C1) [NB100-309] - Human Kidney (formalin-fixed, paraffin-embedded) stained with ATM antibody (2C1) [NB100-309] at 5 ug/ml followed by biotinylated anti-mouse IgG secondary antibody, alkaline phosphatase-streptavidin and chromogen.

Knockdown Validated: ATM Antibody (2C1) [NB100-309] - Non-transfected (-) and transfected (+) HeLa whole cell extracts (60 ug) were separated by 5% SDS-PAGE, and the membrane was blotted with ATM antibody (2C1) [NB100-309] diluted at 1:500.

<b>Genetic Strategies Validation. </b>Knockdown Validated: ATM Antibody (2C1) [NB100-309] - Methylated EDSBs may be repaired by an ATM-dependent pathway. Immunoblots of ATM and DNA-PKcs in ATM shRNA-transfected HeLa cells, using ATM antibody (2C1) [NB100-309]. GAPDH is included as a loading control. Image collected and cropped by CiteAb from the following publication (//molecular-cancer.biomedcentral.com/articles/10.1186/1476-4598-9-70), licensed under a CC-BY license.

Immunoprecipitation: ATM Antibody (2C1) [NB100-309] - MDA-MB-231 whole cell lysates were immunoprecipitated with 2 ug ATM Antibody (NB100-309), followed by Western blot (primary antibody: NB100-309 at 1:1000, 4C overnight. Western blot image submitted by a verified customer review.

<b>Biological Strategies Validation. </b>Western Blot: ATM Antibody (2C1) [NB100-309] - MCELNs decreased the DNA damage of H9C2 cells after radiation. Western blot images of p-ATM (NB100-306) and ATM (NB100-309) in H9C2 cells after 48 h of culture with indicated treatment. IR (-/+): 0/16 Gy X-ray; MCELNs (-/+): 0/10 ug/mL. Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/35509278/) licensed under a CC-BY license.

Western blot analysis of the extent of knockdown MRE11 and ATM, and the lack of effect of Mirin activation of ATM. The extent of shRNA-mediated knockdown of MRE11 and ATM are shown for (A) clones GFP-7F1 and GFP-6D1 and (B) clones EDS-7F2 and EDS-6J8. The extent of knockdown was determined by analyzing the intensity of the ATM and MRE11 bands relative to the intensity of the loading control GAPDH bands (see Table 1). (C) The effect of Mirin on activation of ATM was determined by analysis of phosphorylation of ATM in response to ionizing radiation. Cultures treated with DMSO alone, 20 uM Mirin, or knockdown of ATM were analyzed by western blot 30 min after exposure to 10 Gy of ionizing radiation. Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/26209132), licensed under a CC-BY licence.

Methylated EDSBs may be repaired by an ATM-dependent pathway. (A) Immunoblots of ATM and DNA-PKcs in ATM shRNA-transfected HeLa cells. GAPDH is included as a loading control. Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/20356374), licensed under a CC-BY licence.

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

Reactivity:

Hu, Mu, Rt, Pm

Species Glossary

Reactivity: Hu, Mu, Rt, Pm

Applications:

, , , , , , , , ,

Applications: , , , , , , , , ,

Host:

Mouse Monoclonal

Host: Mouse Monoclonal

Conjugate:

Unconjugated

Validated by:

Validated by:

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NB100-104

ATM Antibody

(2 Reviews)

(99 Publications)

0.05 ml

NB100-104

<b>Biological Strategies Validation. </b>Immunocytochemistry/Immunofluorescence: ATM Antibody [NB100-104] - GM00637 cells with KU55933 pretreatment (a) were exposed to 50 uM spermidine or CCCP, followed by immunofluorescence analyses of total and p-ATM on Ser-1981. The scale bar is 10 um. Image collected and cropped by CiteAb from the following publication (//www.nature.com/articles/srep24700) licensed under a CC-BY license.

Flow Cytometry: ATM Antibody [NB100-104] - An intracellular stain was performed on HeLa cells with Dylight 550-conjugated ATM Antibody [NB100-104R] (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.

<b>Biological Strategies Validation. </b>Western Blot: ATM Antibody [NB100-104] - Analysis of double strand break repair in MCF-7 monolayer and mammosphere populations. Expression of proteins involved in the NHEJ pathway of DSB repair in response to increasing doses of ionizing radiation. Lysates were prepared from unirradiated cells and from cells harvested one hour after exposure to 1 or 10-Gy 60Co I3-radiation and analyzed by immunoblotting with antibodies against several DSB repair proteins. Phospho-ATM and phospho-DNA-PKcs refer to phosphorylation of these proteins at Ser1981 and Ser2056, respectively. Actin served as a loading control. Image collected and cropped by Citeab from the following publication (Senescence evasion by MCF-7 human breast tumor-initiating cells. Breast Cancer Res (2010)) licensed under a CC-BY license.

Western Blot: ATM Antibody [NB100-104] - Detection of ATM in Raji whole cell lysate using [NB100-104]. Observed molecular weight ~300 kDa. Theoretical molecular weight 351 kDa.

Immunocytochemistry/Immunofluorescence: ATM Antibody [NB100-104] - HeLa cells were fixed for 10 minutes using 10% formalin and then permeabilized for 5 minutes using 1X TBS + 0.05% Triton X-100. Then cells were incubated with [NB100-104] at a 1:100 dilution overnight at 4C and detected with an anti-rabbit DyLight 488 (Green) at a 1:500 dilution. Alpha tubulin was used as a co-stain at a 1:1000 dilution and detected with an anti-mouse DyLight 550 (Red) at a 1:500 dilution. Nuclei were counterstained with DAPI (Blue). Cells were imaged using a 40X objective.

Flow Cytometry: ATM Antibody [NB100-104] - Analysis of PE conjugate of ATM Antibody [NB100-104PE]. An intracellular stain was performed on HeLa cells with ATM antibody [NB100-104PE] (blue) and a matched isotype control [NBP2-24893PE] (orange). Cells were fixed with 4% PFA and then permeablized with 0.1% saponin.

Flow Cytometry: ATM Antibody [NB100-104] - An intracellular stain was performed on HepG2 cells with PE-conjugated ATM antibody [NB100-104PE] (blue) and a matched isotype control (orange). Cells were fixed with 4% PFA and then permeablized with 0.1% saponin. Cells were incubated in an antibody dilution of 5 ug/mL for 30 minutes at room temperature. Both antibodies were conjugated to Phycoerythrin.

Depletion of SMARCAL1 induces DNA damage and checkpoint activation in iSML1 iPSCs. (C) Immunoblot detection of the indicated DDR proteins in iSML1 iPSCs after 14 days of continuous treatment with DOX. Lamin B1 was used as the loading control. Data are mean+/-s.e.m. from three independent experiments. *P<=0.05, **P<=0.01, ***P<=0.001 (two-way ANOVA test). ns, not significant. Scale bars: 10 um. Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31515241), licensed under a CC-BY licence.

Osteopontin (OPN) is weakly expressed in NHF, HUVSMC and HUVEC and is not induced in hypoxia. A, Levels of OPN mRNA in AVF patients (n = 12) compared to control veins (Ctl). ****, P < .0001 (Test Mann‐Whitney). B, Representative immunofluorescence of OPN (red staining and arrow) and alpha‐smooth muscle actin ( alpha ‐SMA—green staining and arrows) of human control upper‐arm vein and venous limb of a mature AVF. Osteopontin quantification of group data (vein, n = 3; AVF, n = 2), unpaired t test, P < .01 (right). C, Quantitative immunoblotting to detect recombinant OPN protein. Serial dilutions from 50 to 0.2 ng were used. D, Bone marrow mesenchymal (MSC) and osteoblast (Osteo.) cell lysates analysed by immunoblotting for OPN as indicated. E, LNCap cells were transfected with control siRNA (siCtl), siHIF‐1 alpha (40 nmol/L), siOPN#1 (40 nmol/L) and siOPN#2 (40 nmol/L) and incubated in normoxia (Nx) or hypoxia 1% O2 (Hx) for 48 h. Cell lysates were analysed by immunoblotting for OPN or beta ‐tubulin as indicated. Quantification of the signal to OPN is shown using ImageJ (OPN/ beta ‐tubulin). F–H, NHF (F), HUVSMC (G) and HUVEC (H) cells were transfected with control siRNA (siCtl), siHIF‐1 alpha (40 nmol/L), siHIF‐2 alpha (40 nmol/L) and siHIF1/2 alpha (40 nmol/L + 40 nmol/L), incubated in hypoxia 1% O2 (Hx) for 48 h. AVF, Arteriovenous fistula; HUVEC, human umbilical vein endothelial cells; HUVSMC, Human umbilical vein smooth muscle cells; NHF, normal human fibroblasts Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/32032472), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

TRF1HP1 alpha results in reduced TIFs induced by mutant hTR expression. Cells stably expressing TRF1HP1 alpha (WT or mutant variants of HP1 alpha ) were infected with lentivirus containing WT hTR, or mutant hTR (47A or TSQ1) on day 0, selected for stable expression after 48 h, and analyzed on day 5. a Fluorescence microscopy images of representative cells expressing mutant hTR 47A stained with telomeric (Tel-Cy3) peptide nucleic acid (PNA) probes (magenta in merged image) via fluorescent in situ hybridization (FISH), antibody against DNA-damage repair protein marker 53BP1 (green in merged image), and counterstained with DAPI. Zoom-in images (the last row) correspond to yellow-squared regions of the row above. b % TIF per telomere of each nucleus is quantified; n = 94–159 nuclei combining data of three independent experiments. ****p < 0.0001; n.s. (no significance). a, b Scale bar: 10 µm. c Upon TSQ1 expression, TRF1HP1 alpha results in fewer TIFs compared to Vonly, TRF1 or HP1 alpha controls. TRFHP1 alpha ~11.4% shows decreased TIFs compared to Vonly: ~19.7% ***p = 0.0008; TRF1: ~20.4% ***p = 0.0005; HP1 alpha : ~17.9% *p = 0.0137 (n = 30–38 nuclei). b, c Significance is assessed by one-way ANOVA and Dunnett’s multiple comparison test with 95% confidence level. d Fluorescence images of control cells overexpressing WT hTR (n = 27–36 nuclei). Same color scheme as a. TIFs quantification in the presence of e WT hTR or f Vonly (n = 28–36 nuclei) show minimal baseline DNA damage at telomeres. b, c; e, f Error bars represent s.e.m. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/30181605), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Reactivity:

Hu, Mu, Rt, Ca, Ma

Species Glossary

Reactivity: Hu, Mu, Rt, Ca, Ma

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 405	NB100-104AF405
Alexa Fluor 488	NB100-104AF488
Alexa Fluor 647	NB100-104AF647
Alexa Fluor 700	NB100-104AF700
Biotin	NB100-104B
DyLight 405	NB100-104V
DyLight 488	NB100-104G
DyLight 550	NB100-104R
DyLight 594	NB100-104DL594
DyLight 650	NB100-104C
FITC	NB100-104F
HRP	NB100-104H
PE	NB100-104PE

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NB200-103

p53 Antibody (PAb 240) - BSA Free

(3 Reviews)

(39 Publications)

0.1 ml

NB200-103

Flow Cytometry: p53 Antibody (PAb 240) [NB200-103] - An intracellular stain was performed on HeLa cells with p53 Antibody [PAb 240] NB200-103 (blue) and a matched isotype control (orange). Cells were fixed with 4% PFA and then permeabilized with 0.1% saponin. Cells were incubated in an antibody dilution of 1.0 ug/mL for 30 minutes at room temperature, followed by Mouse IgG (H+L) Cross-Adsorbed Secondary Antibody, Dylight 550 (35503, Thermo Fisher).

Immunocytochemistry/Immunofluorescence: p53 Antibody (PAb 240) [NB200-103] - HeLa cells were fixed for 10 minutes using 10% formalin and then permeabilized for 5 minutes using 1X TBS + 0.5% Triton X-100. The cells were incubated with anti-p53 (PAb 240) [NB200-103] at a 1:200 dilution overnight at 4C and detected with an anti-mouse DyLight 488 (Green) at a 1:500 dilution. Actin was detected with Phalloidin 568 (Red) at a 1:200 dilution. Nuclei were counterstained with DAPI (Blue). Cells were imaged using a 40X objective.

Immunocytochemistry/Immunofluorescence: p53 Antibody (PAb 240) [NB200-103] - 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 anti-p53 Antibody (PAb 240) NB200-103 at 2 ug/ml overnight at 4C and detected with an anti-mouse 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.

Immunocytochemistry/Immunofluorescence: p53 Antibody (PAb 240) [NB200-103] - Neuro2a 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-p53 Antibody (PAb 240) NB200-103 at 2 ug/ml overnight at 4C and detected with an anti-mouse 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.

Flow (Intracellular): p53 Antibody (PAb 240) [NB200-103] - An intracellular stain was performed on HeLa cells with p53 (PAb240) NB200-103 (blue) and a matched isotype control NBP2-27287 (orange). Cells were fixed with 4% PFA and then permeablized with 0.1% saponin. Cells were incubated in an antibody dilution of 2.5 ug/mL for 30 minutes at room temperature, followed by APC-conjugated anti-mouse IgG secondary antibody F0101B.

Flow Cytometry: p53 Antibody (PAb 240) [NB200-103] - An intracellular stain was performed on HeLa cells with p53 (PAb240) NB200-103AF647 (blue) and a matched isotype control (orange). Cells were fixed with 4% PFA and then permeablized with 0.1% saponin. Cells were incubated in an antibody dilution of 2.5 ug/mL for 30 minutes at room temperature. Both antibodies were conjugated to Alexa Fluor 647.

Flow Cytometry: p53 Antibody (PAb 240) [NB200-103] - An intracellular stain was performed on A549 cells with p53 (PAb240) NB200-103AF488 (blue) and a matched isotype control (orange). Cells were fixed with 4% PFA and then permeablized with 0.1% saponin. Cells were incubated in an antibody dilution of 10 ug/mL for 30 minutes at room temperature. Both antibodies were conjugated to Alexa Fluor 488.

Flow Cytometry: p53 Antibody (PAb 240) [NB200-103] - An intracellular stain was performed on MCF7 cells with p53 [PAb 240] Antibody NB200-103AF647 (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: p53 Antibody (PAb 240) [NB200-103] - An intracellular stain was performed on Neuro2a cells with p53 Antibody [PAb 240] NB200-103 (blue) and a matched isotype control (orange). Cells were fixed with 4% PFA and then permeabilized with 0.1% saponin. Cells were incubated in an antibody dilution of 1.0 ug/mL for 30 minutes at room temperature, followed by Mouse IgG (H+L) Cross-Adsorbed Secondary Antibody, Dylight 550 (35503, Thermo Fisher).

Reactivity:

Hu, Mu, Rt, Ye, Xp(-)

Species Glossary

Reactivity: Hu, Mu, Rt, Ye, Xp(-)

Applications:

, , , , , ,

Applications: , , , , , ,

Host:

Mouse Monoclonal

Host: Mouse Monoclonal

Sizes:

Sample Size Available

Sizes: Sample Size Available

Conjugate:

Unconjugated

Available Conjugates:

Conjugate	Catalog #	Availability	Size	Price
Alexa Fluor 350	NB200-103AF350
Alexa Fluor 405	NB200-103AF405
Alexa Fluor 488	NB200-103AF488
Alexa Fluor 532	NB200-103AF532
Alexa Fluor 594	NB200-103AF594
Alexa Fluor 647	NB200-103AF647
Alexa Fluor 700	NB200-103AF700
Alexa Fluor 750	NB200-103AF750
Allophycocyanin	NB200-103APC
Biotin	NB200-103B
DyLight 350	NB200-103UV
DyLight 405	NB200-103V
DyLight 488	NB200-103G
DyLight 550	NB200-103R
DyLight 594	NB200-103DL594
DyLight 650	NB200-103C
DyLight 680	NB200-103FR
DyLight 755	NB200-103IR
FITC	NB200-103F
HRP	NB200-103H
Janelia Fluor 549	NB200-103JF549
Janelia Fluor 646	NB200-103JF646
PE	NB200-103PE
PerCP	NB200-103PCP
mFluor Violet 450 SE	NB200-103MFV450
mFluor Violet 500 SE	NB200-103MFV500
mFluor Violet 610 SE	NB200-103MFV610

Available Formulations

Formulation	Catalog #	Availability	Price
BSA Free	NB200-103SS
Azide and BSA Free	NBP2-80898

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NB100-2280

Histone H2AX [p Ser139] Antibody

(1 Review)

(42 Publications)

0.1 ml

NB100-2280

Immunohistochemistry: Histone H2AX [p Ser139] Antibody [NB100-2280] - Telomere dysfunctional induced foci (TIF) in HBV-related multistep hepatocarcinogenesis and the correlations thereof with stathmin and elongation factor 1alpha (EF1alpha) expression. A. Representative features of colocalization of Histone H2AX [p Ser139] and telomeric DNA in defined lesions of human multistep hepatocarcinogenesis. TIF are indicated by colored arrowheads: blue, DAPI; green, gamma H2AX; red, telomeres; yellow, TIF. Image collected and cropped by CiteAb from the following publication (//translational-medicine.biomedcentral.com/articles/10.1186/1479-5876-12-154) licensed under a CC-BY license.

Immunohistochemistry-Paraffin: Histone H2AX [p Ser139] Antibody [NB100-2280] - Detection of human Histone H2AX [p Ser139] antibody by immunohistochemistry. Sample: FFPE section of human seminoma. Antibodies: Affinity purified rabbit Histone H2AX [p Ser139] antibody used at a dilution of 1:500. Detection: DAB.

Immunohistochemistry: Histone H2AX [p Ser139] Antibody [NB100-2280] - Detection of Mouse Histone H2AX [p Ser139] by Immunohistochemistry. Sample: FFPE section of mouse colon carcinoma CT26. Antibodies: Affinity purified rabbit Histone H2AX [p Ser139] antibody. Detection: DAB.

Simple Western: Histone H2AX [p Ser139] Antibody [NB100-2280] - Electropherogram image(s) of corresponding Simple Western lane view. Histone H2AX [p Ser139] antibody was used at 1:20 dilution on Jurkat lysate(s).

Telomere dysfunctional induced foci (TIF) in HBV-related multistep hepatocarcinogenesis and the correlations thereof with stathmin and elongation factor 1alpha (EF1alpha) expression. A. Representative features of colocalization of gamma-H2AX and telomeric DNA in defined lesions of human multistep hepatocarcinogenesis. TIF are indicated by colored arrowheads: blue, DAPI; green, gamma-H2AX; red, telomeres; yellow, TIF. Image collected and cropped by CiteAb from the following publication (//translational-medicine.biomedcentral.com/articles/10.1186/1479-5876-12-154), licensed under a CC-BY licence.

Hepatic activation of FOXO3 induces oxidative damage and Akt activation. c) Representative IHC staining for phospho-gammaH2AX (bar = 100 um) and quantification of phospho-gammaH2AX-positive cells as a percentage of total hepatocyte cells in livers of patients in area of small cells and large cells. Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31488102), licensed under a CC-BY licence.

Biological and molecular analysis of cutaneous wound healing in p73+/+ and p73-/- mice. (G) Representative micrographs of immunohistochemistry (IHC) staining for gammaH2AX in skin specimens from p73+/+ and p73-/- mice 10 days after wounding. All scale bars represent 50 um. In In (C), (E), and (G), regions of the skin are labeled as: IFE, HF, epidermal wound edge (WE), and newly-formed epidermis of the wound (W); and the dotted line indicates the border between the WE and W. *p-value < 0.05, **p-value < 0.01, ***p-value < 0.001. See also S3 and S4 Figs. Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31216312), licensed under a CC-BY licence.

IDO1 inhibitor enhances the efficacy of radiotherapy in vivo. 1 x 105 of SiHa tumorsphere cells were subcutaneously injected to nude mice for tumor growth. After the tumor volume reached 50 mm3, the mice were divided into four groups of non-treated (Ctrl), INCB-024360 treated (INCB), radiotherapy (Rx), or INCB-024360 plus radiotherapy (INCB + Rx). For the INCB or INCB + Rx group, mice were injected once with 50 mg/kg INCB-024360 intraperitoneally before radiotherapy. For the Rx or INCB + Rx group, mice received 2 Gy radiation per day for total 10 Gy. Mice were sacrificed at day 30 after the last radiation treatment and the xenografted tumors were taken out for picturing (A) and weighting (B). The expression of Ki-67 or p-gammaH2AXser139 was determined by paraffin section followed by immunohistochemical staining (C). The inserted bars indicated 50 uM. The quantification results were performed by TissueFAX software (D). * p < 0.05; ** p < 0.01. The experiments were repeated two times and data from one experiment were presented. Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/32545442), licensed under a CC-BY licence.

Involvement of CBP in BNIP3 expression regulated by HIF-1 alpha and FOXO3 under hypoxia. (A) UCB-hMSCs were incubated with hypoxia condition for 24 h. Co-immunoprecipitation of HIF-1 alpha and FOXO3 with IgG and CBP were shown in left panel. IgG was used as a negative control. The total protein expressions of HIF-1 alpha , FOXO3, CBP and beta -actin in lysate were shown in right panel. n = 3. (B) CBP (20 μM) was pretreated to UCB-hMSCs, and cells were incubated with hypoxia for 24 h. The BNIP3 mRNA expression level was analyzed by qPCR. n = 6. (C) BNIP3 and beta -actin protein expressions were analyzed by western blot. Data represent mean ± S.E. n = 4. (D, E) Sample DNA was immuno-precipitated with RNA polymerase, IgG, HIF-1 alpha and FOXO3 specific antibodies. CHIP (top panel) and lysate (bottom panel) samples were amplified with the primers of GAPDH and BNIP3 promoters. Quantitative CHIP data was analyzed by qPCR, and shown in the right panel. n = 4. Western blot data were normalized by beta -actin, and qPCR data were normalized by ACTB mRNA expression level. Quantitative data are presented as a mean ± S.E.M. All blot images are representative. *p < 0.05 versus control, #p < 0.05 versus hypoxia. Image collected and cropped by CiteAb from the following open publication (//linkinghub.elsevier.com/retrieve/pii/S2213231717303804), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Nox4 overexpression accelerated senescence of NP cells. (a, b) RT-qPCR analysis (N = 4) and representative immunoblot analysis of p53, p16, p21, and Rb in NP cells overexpressing Nox4. (c) The percentage of SA-beta -gal-positive NP cells overexpressing Nox4 (N = 8). (d, e) Immunofluorescence staining of BrdU and percentage of BrdU-positive cells in NP cells overexpressing Nox4 (N = 8). (f, g) RT-qPCR analysis of matrix degradation enzymes and proinflammatory cytokines in NP cells overexpressing Nox4 (N = 4). NP cells were transfected with Nox4 vectors for Nox4 overexpression. ∗, P value < 0.05, error bars represent standard error. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/29147462), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Reactivity:

Hu, Mu, Ca, Po, Bt, Bv, ChHa, Gp, Pm, Rb

Species Glossary

Reactivity: Hu, Mu, Ca, Po, Bt, Bv, ChHa, Gp, Pm, Rb

Applications:

, , ,

Applications: , , ,

Host:

Rabbit Polyclonal

Host: Rabbit Polyclonal

Conjugate:

Unconjugated

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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

Kit Type

Lysate Type

Preservative

Protein Or Peptide

Research Areas

Has Sample Size

Promotional Item

Species Glossary

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Histone H2AX [p Ser139] Antibody

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Histone H2AX [p Ser139] Antibody