| Formulation | Catalog # | Availability | Price | |
|---|---|---|---|---|
| Purified | NBP3-25349-0.025mg | |||
| Purified | NBP3-25349-0.05mg | |||
| BSA Free | NB100-142SS | |||
| Formulation | Catalog # | Availability | Price | |
|---|---|---|---|---|
| BSA Free | NB100-143SS | |||
| Formulation | Catalog # | Availability | Price | |
|---|---|---|---|---|
| BSA Free | NB500-170SS | |||
| Formulation | Catalog # | Availability | Price | |
|---|---|---|---|---|
| BSA Free | NB110-57130SS | |||
| Formulation | Catalog # | Availability | Price | |
|---|---|---|---|---|
| BSA Free | NBP3-38646SS | |||
| BSA Free | NBP3-38646 | |||
| BSA Free | NB100-690SS | |||
| Azide and BSA Free | NBP2-80570 | |||
| Formulation | Catalog # | Availability | Price | |
|---|---|---|---|---|
| BSA Free | NB110-89717SS | |||
| Formulation | Catalog # | Availability | Price | |
|---|---|---|---|---|
| BSA Free | NBP2-54791SS | |||
| Azide and BSA Free | NBP2-80822 | |||
| Formulation | Catalog # | Availability | Price | |
|---|---|---|---|---|
| BSA Free | NB100-104SS | |||
![Immunohistochemistry-Paraffin: Goat Polyclonal AIF-1/Iba1 Antibody [NB100-1028] - AIF-1/Iba1 immunoreactivity in an FFPE section of mouse spleen. NB100-1028 was diluted to 1ug per mL and was left on tissue sections for 30m at room temperature. Secondary was horse anti goat HRP polymer. Image from a verified customer review.](http://images.novusbio.com/fullsize/antibody/nb100-1028_goat-polyclonal-aif-1-iba1-antibody-immunohistochemistry-paraffin-752024135211..jpg)
![Immunohistochemistry-Paraffin: Goat Polyclonal AIF-1/Iba1 Antibody [NB100-1028] - AIF-1/Iba1 immunoreactivity in an FFPE section of human tonsil. NB100-1028 was diluted to 1ug per mL and was left on tissue sections for 30m at room temperature. Secondary was horse anti goat HRP polymer. Image from a verified customer review.](http://images.novusbio.com/fullsize/antibody/nb100-1028_goat-polyclonal-aif-1-iba1-antibody-immunohistochemistry-paraffin-7520241463..png)
![Immunohistochemistry-Paraffin: Goat Polyclonal AIF-1/Iba1 Antibody [NB100-1028] - AIF-1/Iba1 immunoreactivity in an FFPE section of equine spleen. NB100-1028 was diluted to 1ug per mL and was left on tissue sections for 30m at room temperature. Secondary was equine anti goat HRP polymer. Image from a verified customer review.](http://images.novusbio.com/fullsize/antibody/nb100-1028_goat-polyclonal-aif-1-iba1-antibody-immunohistochemistry-paraffin-2852024102248..png)
![Immunocytochemistry/ Immunofluorescence: AIF-1/Iba1 Antibody [NB100-1028] - Microglia proliferate in non‐APP mice upon peripheral immune challengeA, BIba‐1, Ki67, & DAPI staining in the cortex & hippocampus of wild‐type & Nlrp3−/− (5 & 15 months old). Microglia proliferate upon LPS injection (white arrows). Non‐microglia cells proliferation was observed as well (yellow arrows). Scale bar: 20 μm.CQuantification of microglial proliferation in cortex (left panel) & hippocampus (right panel) (mean of 5 ± SEM; two‐way ANOVA followed by Tukey's post hoc test, *P 1.5, FDR-corrected p1.5, FDR-corrected p<0.05) to identify GO terms, including inflammatory response (b). The volcano plot shows significant DEGs derived from the NanoString analysis of the brains of Plcg2 inactivation (PLCG2 inact, n=3) & WT (n=3) mice (1-month male) (c). Immunostaining of microglial markers with IBA1 (green) & P2RY12 (red) & quantification of percent area in brain sections of 1-month-old male WT & PLCG2 inact demonstrate unchanged microglial morphology & area coverage (d). GO gene ontology, BP biological process, DEGs differentially expressed genes, FDR false discovery rate Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/35180881), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-1028_goat-polyclonal-aif-1-iba1-antibody-310202415483623.jpg)
![Immunocytochemistry/ Immunofluorescence: AIF-1/Iba1 Antibody [NB100-1028] - Representative & quantitative immunohistochemistry of the peri-infarct cortex before the bregma (coordinate + 0.58) in normal WT, normal sEH KO, MCAO WT, MCAO sEH KO, MCAO with vehicle treatment & MCAO with AUDA treatment mice (n = 2 for normal groups, n = 5–6 for all groups subjected to MCAO). (A–F, S) The number of CD31-positive endothelial cells significantly increased in the sEH KO before & after MCAO & post-MCAO AUDA-treated mice, while (G–L) Note the increased phosphorylated TrkB (p-TrkB) immunoreactivity that partially co-localized with NeuN-positive neurons, particularly in the sEH KO & AUDA-treated mice (arrows) (T). The percentage of NeuN- & p-TrkB-positive double labeling in the neuronal population was significantly increased compared to that in the corresponding controls. (M–R, U–V) GFAP-positive astrogliosis & Iba1-positive microglial infiltration decreased in post-MCAO sEH KO & AUDA treatment groups relative to that in the corresponding controls. The scale bar represents 50 µm. *p < 0.05, **p < 0.01, ***p < 0.001. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/29311641), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-1028_goat-polyclonal-aif-1-iba1-antibody-310202415482273.jpg)
![Immunocytochemistry/ Immunofluorescence: AIF-1/Iba1 Antibody [NB100-1028] - Representative & quantitative immunohistochemistry of the peri-infarct cortex before the bregma (coordinate + 0.58) in normal WT, normal sEH KO, MCAO WT, MCAO sEH KO, MCAO with vehicle treatment & MCAO with AUDA treatment mice (n = 2 for normal groups, n = 5–6 for all groups subjected to MCAO). (A–F, S) The number of CD31-positive endothelial cells significantly increased in the sEH KO before & after MCAO & post-MCAO AUDA-treated mice, while (G–L) Note the increased phosphorylated TrkB (p-TrkB) immunoreactivity that partially co-localized with NeuN-positive neurons, particularly in the sEH KO & AUDA-treated mice (arrows) (T). The percentage of NeuN- & p-TrkB-positive double labeling in the neuronal population was significantly increased compared to that in the corresponding controls. (M–R, U–V) GFAP-positive astrogliosis & Iba1-positive microglial infiltration decreased in post-MCAO sEH KO & AUDA treatment groups relative to that in the corresponding controls. The scale bar represents 50 µm. *p < 0.05, **p < 0.01, ***p < 0.001. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/29311641), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-1028_goat-polyclonal-aif-1-iba1-antibody-310202415483641.jpg)
![Immunocytochemistry/ Immunofluorescence: AIF-1/Iba1 Antibody [NB100-1028] - Norgestrel reduces pro-inflammatory & promotes anti-inflammatory phenotypes in rd10 microglia.(A) RT-qPCR analysis detected similar levels of mRNAs encoding progesterone receptor membrane complexes 1 & 2 (PGRMC1, PGRMC2) & all three membrane progesterone receptor isoforms, alpha , beta & gamma (mPR alpha , mPR beta , mPR gamma ) in rd10 retinal microglial cells. Classical progesterone receptor (PR A/B) was not expressed. Actin, HPRT & GAPDH served as reference genes. (B) Immunolabeling confirmed the presence of these progesterone receptors in primary rd10 microglial cells. Hoechst (blue) staining reveals the cell nuclei. Scale bar represents 10μm. (C) Fluorescent microscopic images of primary rd10 microglia immunolabeled for (C) (i) markers of activation (CD68) & pro-inflammation (M1) (iNOS) & (C) (ii) anti-inflammatory activation (M2) (MRC1); after treatment with 20 μM Norgestrel over 24h. Norgestrel reduced pro-inflammatory & increased anti-inflammatory markers in rd10 microglia. Scale bar 10μm. (D) Quantification of fluorescence intensity of (D) (i) CD68 & iNOS & (D) (ii) MRC1 in primary rd10 microglial cultures following Norgestrel treatment over 24h. N = 8 mice, n = 4 technical replicates per group. (E) Nitrite concentration in the media of rd10 microglia in vitro treated with Norgestrel or vehicle over 24hr. Norgestrel significantly reduced nitrite release from rd10 microglia. N = 8 biological replicates, n = 2 technical replicates per sample. Results are presented as mean ± SEM (t-test, *p<0.05, ***p<0.005, ****p<0.001). Image collected & cropped by CiteAb from the following publication (//dx.plos.org/10.1371/journal.pone.0165197), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-1028_goat-polyclonal-aif-1-iba1-antibody-310202415482243.jpg)
![Immunohistochemistry: AIF-1/Iba1 Antibody [NB100-1028] - Temporal activation of caspase-8 in Iba1-positive myeloid cells. Frozen tissue sections from mice upon pMCAO (n = 9) were analyzed by immunohistochemistry for expression of active caspase-8 or for expression of the microglia/macrophage marker Iba1. The contralateral side to the ischemic area was used an internal control for each animal. A small increase in body size of Iba1 positive cells was detected in the peri-infarct area at 6 h, with larger increase in cell body & numbers of cells expressing Iba1 detected at 24 & 48 h post occlusion (a). Cleaved caspase-8 was detected at low levels at 6 h, but a significant increase in expression levels was observed at 24 & 48 h in the peri-infarct area, but not at the contralateral side (a). Double immunofluorescent staining revealed that increased active caspase-8 expression was localized in Iba1-positive cells (b). Scale bar represent 100 μm in IHC images (a) & 10 μm in IF images (b) Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/27566702), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-1028_goat-polyclonal-aif-1-iba1-antibody-31020241548514.jpg)
![Western Blot: AIF-1/Iba1 Antibody [NB100-1028] - GM1 effects on brain microglia in vivo, after peripheral administration of LPS. A Schematic representation of in vivo administration of GM1 after LPS-induced systemic inflammation in mice (N = 5 per treatment). B Representative images of Iba-1 stained microglia in the cortex of control animals infused with vehicle (CTRL) or GM1 (CTRL + GM1), & in animals treated with LPS & subsequently infused with vehicle artificial cerebrospinal fluid (LPS) or GM1 (LPS + GM1). C Immunoblot in whole brain lysates & densitometric analysis show LPS-dependent increase in Iba 1 expression. D Cortical & striatal microglia (Iba-1+ cells) cell body area quantified with MetaXpress software. GM1 administration significantly decreases cell body area in the cortex, but not in the striatum. E IL-6 protein levels in whole mouse brain homogenate. aCSF, artificial cerebrospinal fluid. Bars show mean values ± STDEV. Two-way ANOVA with Tukey’s multiple comparisons test; *p < 0.05, **p < 0.01, ***p < 0.001 Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/34991625), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-1028_goat-polyclonal-aif-1-iba1-antibody-310202415485114.jpg)
![Immunocytochemistry/ Immunofluorescence: AIF-1/Iba1 Antibody [NB100-1028] - ABIN1 knockdown increases proinflammatory cytokine production & microglial activation. (a-b) Levels of the ABIN1 mRNA & protein were detected 24 h after reperfusion using RT-qPCR & western blot, respectively, to confirm the efficiency of ABIN1 gene knockdown (n = 5 rats per group). (c) ELISA was used to detect the concentrations of TNF-alpha , IL-1 beta & MCP-1 in the peri-infarct cortex at 24 h after reperfusion (n = 5 rats per group). (d) Microglial morphology was observed using immunofluorescence staining for Iba-1 (green) in the peri-infarct cortex at 24 h after reperfusion (n = 3 rats per group). Scale bar = 50 μm. (e & f) Quantification of microglia process endpoints & cell & process lengths/cell (∗∗P < 0.01 compared to the sham group; ##P < 0.01 compared to the MCAO/R group). Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/33110436), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-1028_goat-polyclonal-aif-1-iba1-antibody-310202415485133.jpg)
![Immunocytochemistry/ Immunofluorescence: AIF-1/Iba1 Antibody [NB100-1028] - SCF+G-CSF treatment increases TREM2 expression in the Iba1+ microglia/macrophages surrounding the 6E10+ senile plaques. (A) Representative confocal images of TREM2 (red), 6E10 (purple) & Iba1 (green) triple immunofluorescence staining in the brains of aged APP/PS1 mice. Blue: Nuclear counterstaining by DAPI. (B) Representative orthographic view of z-stack images (12 z-stacks with 1μm intervals) illustrates the location & interaction of TREM2 + cells (red) & 6E10+ A beta plaques (white) in the brains of aged APP/PS1 mice. (C) Quantification data show the percentage of TREM2+ area surrounding the 6E10+ A beta plaques (within 10μm from the border of the A beta plaques) in the brains of aged APP/PS1 mice with or without SCF+G-CSF treatment. (D) Representative orthographic view of z-stack images (12 z-stacks with 1μm intervals) displays the location & interaction of TREM2+/Iba1+ co-expressing cells (yellow) & 6E10+ A beta plaques (white) in the brains of APP/PS1 mice. (E) Quantification data show the percentage of TREM2+/Iba1+ co-expression area in the total of Iba1+ area in the vicinity of 6E10+ A beta plaques in the brains of aged APP/PS1 mice with or without SCF+G-CSF treatment. N=4-5. Mean ± SEM. * p<0.05 by Student’s t-test. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/33269098), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-1028_goat-polyclonal-aif-1-iba1-antibody-310202415482219.jpg)
![Immunocytochemistry/ Immunofluorescence: AIF-1/Iba1 Antibody [NB100-1028] - SCF+G-CSF treatment increases the association of Iba1+ microglia/macrophages with senile plaques & enhances uptake of 4G8+ A beta by the Iba1+ microglia/macrophages in the brains of aged APP/PS1 mice. (A) Representative confocal images illustrate the association of Iba1+ cells (green) with 4G8+ A beta plaques (red) in the brains of aged APP/PS1 mice. Blue: Nuclear counterstaining by DAPI. (B) Quantification of the percentage of Iba1+ area in/surrounding the 4G8+ A beta plaques in the brains of aged APP/PS1 mice with or without SCF+G-CSF treatment. (C) Representative 3-dimensional projected images reveal the overlapped (yellow) Iba1+ cells (green) with 4G8+ A beta (red) in the brains of aged APP/PS1 mice. The white arrows indicate the co-expression (yellow) of 4G8+ A beta & Iba1+ cells in the brains of aged APP/PS1 mice. (D & E) Representative orthographic view of z-stack images (12 z-stacks with 1μm intervals) shows the co-expression (yellow) of 4G8+ A beta (red) & Iba1+ cells (green) in the brains of aged APP/PS1 mice. (F) Quantification data present the percentage of 4G8+ A beta volume within the Iba1+ cells in the brains of aged APP/PS1 mice treated with or without SCF+G-CSF. N=4-5. Mean ± SEM. *p<0.05 by Student’s t-test. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/33269098), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-1028_goat-polyclonal-aif-1-iba1-antibody-310202415485142.jpg)
![Immunocytochemistry/ Immunofluorescence: AIF-1/Iba1 Antibody [NB100-1028] - Representative & quantitative immunohistochemistry of the peri-infarct cortex before the bregma (coordinate + 0.58) in normal WT, normal sEH KO, MCAO WT, MCAO sEH KO, MCAO with vehicle treatment & MCAO with AUDA treatment mice (n = 2 for normal groups, n = 5–6 for all groups subjected to MCAO). (A–F, S) The number of CD31-positive endothelial cells significantly increased in the sEH KO before & after MCAO & post-MCAO AUDA-treated mice, while (G–L) Note the increased phosphorylated TrkB (p-TrkB) immunoreactivity that partially co-localized with NeuN-positive neurons, particularly in the sEH KO & AUDA-treated mice (arrows) (T). The percentage of NeuN- & p-TrkB-positive double labeling in the neuronal population was significantly increased compared to that in the corresponding controls. (M–R, U–V) GFAP-positive astrogliosis & Iba1-positive microglial infiltration decreased in post-MCAO sEH KO & AUDA treatment groups relative to that in the corresponding controls. The scale bar represents 50 µm. *p < 0.05, **p < 0.01, ***p < 0.001. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/29311641), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-1028_goat-polyclonal-aif-1-iba1-antibody-310202415485140.jpg)
![Immunocytochemistry/ Immunofluorescence: AIF-1/Iba1 Antibody [NB100-1028] - Antibody-mediated Nogo-A blockade decreases the number of cells expressing TNF alpha without affecting the number of Iba1-positive monocytes.Cells expressing TNF alpha , Iba1, & CD68 were labeled on cryosections by immunofluorescence in 4 mouse retinae, 24 h after control IgG or 11C7 injection. a Retinal sections showed many TNF alpha -containing cells located in the inner retina, between the outer plexiform layer & the ganglion cell layer 1 day after control IgG injection. A majority of cells was positive for Iba1 & exhibited vesicular staining of the lysosomal protein CD68, indicating their active state. b The injection of 11C7 strongly attenuated TNF alpha & CD68 expression & to a lower extent the intensity of Iba1 in macrophages/microglia. c Quantification of the number of cells expressing TNF alpha & Iba1 suggesting potent & specific effects of 11C7 on TNF alpha cytokine reduction. Six sections were examined for each retina. Statistics: one-way ANOVA, Dunnett’s post hoc test, **P < 0.01; ****P < 0.0001. Scale bars = 50 μm. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/32029703), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-1028_goat-polyclonal-aif-1-iba1-antibody-310202415485131.jpg)
![Immunocytochemistry/ Immunofluorescence: AIF-1/Iba1 Antibody [NB100-1028] - SCF+G-CSF treatment increases TREM2 expression in the Iba1+ microglia/macrophages surrounding the 6E10+ senile plaques. (A) Representative confocal images of TREM2 (red), 6E10 (purple) & Iba1 (green) triple immunofluorescence staining in the brains of aged APP/PS1 mice. Blue: Nuclear counterstaining by DAPI. (B) Representative orthographic view of z-stack images (12 z-stacks with 1μm intervals) illustrates the location & interaction of TREM2 + cells (red) & 6E10+ A beta plaques (white) in the brains of aged APP/PS1 mice. (C) Quantification data show the percentage of TREM2+ area surrounding the 6E10+ A beta plaques (within 10μm from the border of the A beta plaques) in the brains of aged APP/PS1 mice with or without SCF+G-CSF treatment. (D) Representative orthographic view of z-stack images (12 z-stacks with 1μm intervals) displays the location & interaction of TREM2+/Iba1+ co-expressing cells (yellow) & 6E10+ A beta plaques (white) in the brains of APP/PS1 mice. (E) Quantification data show the percentage of TREM2+/Iba1+ co-expression area in the total of Iba1+ area in the vicinity of 6E10+ A beta plaques in the brains of aged APP/PS1 mice with or without SCF+G-CSF treatment. N=4-5. Mean ± SEM. * p<0.05 by Student’s t-test. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/33269098), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-1028_goat-polyclonal-aif-1-iba1-antibody-310202415482237.jpg)
![Immunocytochemistry/ Immunofluorescence: AIF-1/Iba1 Antibody [NB100-1028] - Representative & quantitative immunohistochemistry of the peri-infarct cortex before the bregma (coordinate + 0.58) in normal WT, normal sEH KO, MCAO WT, MCAO sEH KO, MCAO with vehicle treatment & MCAO with AUDA treatment mice (n = 2 for normal groups, n = 5–6 for all groups subjected to MCAO). (A–F, S) The number of CD31-positive endothelial cells significantly increased in the sEH KO before & after MCAO & post-MCAO AUDA-treated mice, while (G–L) Note the increased phosphorylated TrkB (p-TrkB) immunoreactivity that partially co-localized with NeuN-positive neurons, particularly in the sEH KO & AUDA-treated mice (arrows) (T). The percentage of NeuN- & p-TrkB-positive double labeling in the neuronal population was significantly increased compared to that in the corresponding controls. (M–R, U–V) GFAP-positive astrogliosis & Iba1-positive microglial infiltration decreased in post-MCAO sEH KO & AUDA treatment groups relative to that in the corresponding controls. The scale bar represents 50 µm. *p < 0.05, **p < 0.01, ***p < 0.001. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/29311641), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-1028_goat-polyclonal-aif-1-iba1-antibody-310202415482285.jpg)
![Immunocytochemistry/ Immunofluorescence: AIF-1/Iba1 Antibody [NB100-1028] - Representative & quantitative immunohistochemistry of the peri-infarct cortex before the bregma (coordinate + 0.58) in normal WT, normal sEH KO, MCAO WT, MCAO sEH KO, MCAO with vehicle treatment & MCAO with AUDA treatment mice (n = 2 for normal groups, n = 5–6 for all groups subjected to MCAO). (A–F, S) The number of CD31-positive endothelial cells significantly increased in the sEH KO before & after MCAO & post-MCAO AUDA-treated mice, while (G–L) Note the increased phosphorylated TrkB (p-TrkB) immunoreactivity that partially co-localized with NeuN-positive neurons, particularly in the sEH KO & AUDA-treated mice (arrows) (T). The percentage of NeuN- & p-TrkB-positive double labeling in the neuronal population was significantly increased compared to that in the corresponding controls. (M–R, U–V) GFAP-positive astrogliosis & Iba1-positive microglial infiltration decreased in post-MCAO sEH KO & AUDA treatment groups relative to that in the corresponding controls. The scale bar represents 50 µm. *p < 0.05, **p < 0.01, ***p < 0.001. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/29311641), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-1028_goat-polyclonal-aif-1-iba1-antibody-310202415482247.jpg)
![Immunocytochemistry/ Immunofluorescence: AIF-1/Iba1 Antibody [NB100-1028] - The presence or absence of TRPV1 influences microglial pathophysiological changes in recurrent febrile seizures mice. (A) Images of the cortex immunostained for the microglial marker Iba-1 (visualized in green FITC) & the lysosomal marker CD68/ED1 (visualized in red Alexa Fluor 594) & DAPI (visualized in blue) 5 days after rFS from wild type (WT) & TRPV1−/− mice (Scale bars: 50 μm). (B,C) Bar graph of quantification of Iba1+(B) & Iba1+ ED1+(C) in 5 days after rFS mice cortex. (D) Representative photomicrographs of different microglial morphological subtypes including resting/ramified (Ram), hypertrophic/intermediate (Inter) & round/ameboid (Amoeboid; Scale bars: 5 μm). (E) Quantification of relative percentage of microglia with different morphologies in the cortex of WT & TRPV1−/− mice (n = 6 per groups, **p < 0.01, ***p < 0.001, two-way ANOVA followed by Tukey’s multiple comparisons). (F–H) Representative Immunoblot bands (F) & densitometric analysis of Iba1 expression (G) & ED1 expression (H) were significantly increased in rFS from WT mice than in TRPV1−/− mice. Data were presented as means ± SEM, n = 6 per groups, *p < 0.05, **p < 0.01, ***p < 0.001, two-way ANOVA followed by Tukey’s multiple comparisons. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31680864), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-1028_goat-polyclonal-aif-1-iba1-antibody-310202415482254.jpg)
![Immunohistochemistry-Frozen: Goat Polyclonal AIF-1/Iba1 Antibody [NB100-1028] - AD Mouse Model. FxFr:10 µm thickness 1:200. Secondary antibody AF647. Image from a verified customer review.](http://images.novusbio.com/fullsize/antibody/nb100-1028_goat-polyclonal-aif-1-iba1-antibody-immunohistochemistry-frozen-4122024105512..jpg)
![Immunohistochemistry: Goat Polyclonal AIF-1/Iba1 Antibody [NB100-1028] - Pax5 and Iba1 immunoreactivity in a formalin fixed paraffin embedded classic Hodgkin's lymphoma biopsy. Formalin fixed paraffin embedded sections were deparaffinized and rehydrated. Sections then underwent heat induced epitope retrieval in a citrate-based solution for 20min in a food steamer. Sections were cooled, then blocked in phosphate buffered saline containing 0.2% Triton-X100 and 10% normal donkey serum for 1h at room temperature. Sections were then incubated with the primary antibody for 16h at room temperature. The following day slides were washed three times with PBS containing 0.05% Tween-20. Sections were then incubated with donkey anti-goat (647 conjugate) at 5ug per mL for 45min at room temperature. Slides were then washed as above and mounted with a coverslip. Image from a verified customer review.](http://images.novusbio.com/fullsize/antibody/nb100-1028_goat-polyclonal-aif-1-iba1-antibody-immunohistochemistry-332025111028..jpg)
![Simple Western: Mre11 Antibody [NB100-142] - Image shows a specific band for Mre11 in 0.5 mg/mL of HeLa lysate. A band appears at the theoretical molecular weight of 81 kDa for this product. This experiment was performed under reducing conditions using the 12-230 kDa separation system.](http://images.novusbio.com/fullsize/Mre11-Antibody-Simple-Western-NB100-142-img0010.jpg "Simple Western: Mre11 Antibody [NB100-142] - Image shows a specific band for Mre11 in 0.5 mg/mL of HeLa lysate. A band appears at the theoretical molecular weight of 81 kDa for this product. This experiment was performed under reducing conditions using the 12-230 kDa separation system.")
![Immunocytochemistry/Immunofluorescence: Mre11 Antibody [NB100-142] - IF analysis of Mre11 on HeLa. Image from verified customer review.](http://images.novusbio.com/fullsize/Mre11-Antibody-Immunocytochemistry-Immunofluorescence-NB100-142-img0009.jpg)
![<b>Genetic Strategies Validation. </b>Western Blot: 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.](http://images.novusbio.com/fullsize/Mre11-Antibody-Knockdown-Validated-NB100-142-img0012.jpg)
![Immunohistochemistry: Mre11 Antibody [NB100-142] - Immunohistochemical staining of MRE11 in a human epidermis cross section.](http://images.novusbio.com/fullsize/Mre11-Antibody-Immunohistochemistry-NB100-142-img0004.jpg)
![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.](http://images.novusbio.com/fullsize/Mre11-Antibody-Western-Blot-NB100-142-img0005.jpg)
![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.](http://images.novusbio.com/fullsize/Mre11-Antibody-Immunocytochemistry-Immunofluorescence-NB100-142-img0011.jpg)
![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.](http://images.novusbio.com/fullsize/Mre11 Antibody-Chromatin Immunoprecipitation-NB100-142-img0013.jpg)
![<b>Genetic Strategies Validation. </b>Western Blot: Mre11 Antibody [NB100-142] - TIG-1 human primary fibroblasts, whole cell lysate (30 ug). Image from verified customer review.](http://images.novusbio.com/fullsize/Mre11-Antibody-Knockdown-Validated-NB100-142-img0008.jpg)
![Western Blot: Mre11 Antibody [NB100-142] - MRE11 associates with the DS region of OriP.A) DNA affinity purification assays were performed with Raji nuclear extracts & DNA templates derived from DS wt, DS nm-, or delta DS. Input & template bound proteins were analyzed by Western blot with antibodies to TRF2, MRE11, EBNA1, PCNA, & PARP1, as indicated. B) Schematic of template DNA used for DNA affinity purification in A, & their respective protein binding sites. C) ChIP assays to monitor EBNA1, TRF2, & MRE11 binding at OriP wt or OriP nm- in transfected 293 cells. Immunoprecipitated DNA was quantified by real time PCR relative to total input DNA recovered for each transfected cell. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/18040525), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-142_rabbit-polyclonal-mre11-antibody-310202415384114.jpg)
![Western Blot: Mre11 Antibody [NB100-142] - Immunoblotting analysis of IR-induced AKT (Ser473) activation. (A) The levels of AKT activation were measured by AKT Ser473 phosphorylation in 293T, 293T/eIF3f & 293T/eIF3f-hMSH4 cells treated with 10 Gy IR in comparison to untreated controls. Levels of p53 Ser15 phosphorylation & the total protein levels of AKT, hMRE11 & p53 were also analyzed. alpha -tubulin was used as a loading control. (B) The levels of Chk2 activation (Chk2 Thr68 phosphorylation) in 293T, 293T/eIF3f & 293T/eIF3f-hMSH4 cells in response to 10 Gy IR. Cell lysates were prepared at 1 hr post IR treatment. Untreated cells were analyzed as controls, while alpha -tubulin was used as a loading control. Image collected & cropped by CiteAb from the following publication (//molecular-cancer.biomedcentral.com/articles/10.1186/1476-4598-12-51), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-142_rabbit-polyclonal-mre11-antibody-310202415293334.jpg)
![Western Blot: Mre11 Antibody [NB100-142] - The DNA damage response at telomeres uncapped through TRF2 depletion does not require BRCA1 or CtIPImmortalized Brca1F/− MEFs were infected with retroviruses expressing the indicated shRNAs and/or Cre recombinase, followed by selection with puromycin for 72 h. Cell extracts were prepared 48 h later & analysed by Western blotting as indicated. SMC1 & tubulin were used as loading controls. *non-specific band.Cells treated as in (A) were fixed 48 h after selection & stained with an anti-53BP1 antibody (green). Telomeres were visualized with a Cy3-conjugated (CCCTAA)3-PNA probe (red). Yellow arrowheads point to 53BP1 foci that co-localize with telomeres.Quantification of TIFs in cells treated as in (B). A minimum of 200 nuclei were scored for each sample. Error bars represent SD of two independent experiments. P-values were calculated using an unpaired two-tailed t-test. *P ≤ 0.05; NS, P > 0.05. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/25582120), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-142_rabbit-polyclonal-mre11-antibody-31020241554548.jpg)
![Western Blot: Mre11 Antibody [NB100-142] - MRE11 & NBS1 contribute to OriP replication & EBV episome stability.A) D98/HR1 cells were transfected with siRNA for MRE11 or NBS1, or Luciferase control & assayed by immuno-blot (IB) with antibodies specific for MRE11 (left pane) or NBS1 (right panel), or PCNA (lower panel) as a loading control. B) Transient DNA replication assays of OriP-containing plasmids were analyzed by Southern blot. D98/HR1 cells were transfected with OriP plasmid & siRNA for either MRE11, NBS1, or luciferase control (as indicated above each lane). Hirt extracted plasmid DNA was digested with DpnI plus BamHI (top panel) or BamHI only (lower panel) & probed with OriP specific probes. DNA was quantified by PhosphorImager analysis & the replication value was determined as the ratio of DpnI/BamHI to BamHI recovered products. Quantification shown below is a summary of at least four independent replication assays (data not shown). C)) EBV episomes from latently infected D98/HR1 cells were analyzed by pulse field electrophoresis & Southern blotting after transfection of siRNA for control (siLuc), MRE11, or NBS1. Raji cells were used as a control for EBV episome size & abundance. The percentage of EBV episomes relative to the EBV DNA retained in the well is calculated below. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/18040525), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-142_rabbit-polyclonal-mre11-antibody-310202416574.jpg)
![Western Blot: Mre11 Antibody [NB100-142] - Evidence that MRE11 & NBS1 are required for EBV episome maintenance.A) OriP plasmid maintenance assays were performed in MRE11 mutant (ATLD3) & reconstituted (ATLD3/wtMRE11) cell lines (left panel) or NBS1 mutant (GM7166) & reconstituted (GM7166/wtNBS1) cell lines (right panel). Plasmids containing OriP & EBNA1 were monitored by Southern blotting of Hirt lysates at 1 (lower panel) & 7 (upper panel) days post-transfection. Phosphorimager quantification of four independent experiments as shown in panal A where maintenance is measured as the ratio of day 7 to day 1 for OriP plasmid detection is shown below. B) EBV transformed B-lymphocytes were analyzed by PFG & Southern blotting for the presence of episomal forms of the EBV genome. Raji, Namalwa, NBS1 (GM15808), NBS1 (GM07078), LCL3472, & LCLAW7 DNA was loaded at equal concentrations & analyzed by ethidium staining of PFG (lower panel) or by Southern blot (upper panel) with EBV specific probe. C) Western blot of the same cell lines used for PFG analysis shown in panel B was probed with antibodies specific for NBS1 (antibody 143 & antibody 277), MRE11, or loading control Actin. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/18040525), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-142_rabbit-polyclonal-mre11-antibody-31020241612675.jpg)
![Western Blot: Mre11 Antibody [NB100-142] - Involvement of CBP & p300 in the transcription of the BRCA1 & RAD51 genes.(A) Down-regulation of BRCA1 & RAD51 proteins upon depletion of CBP and/or p300. H1299 cells were transfected for 48 hr with non-targeting (siNT), CBP (siCBP), p300 (sip300), or CBP+p300 (siC+p) siRNAs. The cells were harvested & whole cell extracts were subjected to immunoblotting. (B, C) Reduction of BRCA1 & RAD51 transcripts in CBP- & p300-depleted cells. H1299 cells were transfected for 48 hr with non-targeting (siNT), CBP (siCBP), p300 (sip300), or CBP+p300 (siC+p) siRNAs. Cells were harvested & subjected to quantitative real-time PCR for the detection of BRCA1 (B) & RAD51 (C) mRNAs. Expression levels were normalized against the levels of GAPDH mRNA. Data represent the mean ± SD. (D) H1299 cells were transfected for 48 hr with non-targeting (siNT), CBP (siCBP), p300 (sip300), or CBP+p300 (siC+p) siRNAs, & stained with propidium iodide (PI). The percentage of cells in each cell cycle phase was determined by FACS. Percentages of cells in G1, S, & G2/M are shown. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/23285190), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-142_rabbit-polyclonal-mre11-antibody-310202415525210.jpg)
![Western Blot: Nbs1 Antibody [NB100-143] - Lysates of HeLa human cervical epithelial carcinoma parental cell line and Nbs1 knockout (KO) HeLa cell line. PVDF membrane was probed with 1:1000 of Rabbit Anti-Human Polyclonal [NB100-143] followed by HRP-conjugated Anti-Rabbit IgG Secondary Antibody (HAF008). Specific band was detected for Nbs1 at approximately 95 kDa (as indicated) in the parental HeLa cell line, but is not detectable in the knockout HeLa cell line. This experiment was conducted under reducing conditions.](http://images.novusbio.com/fullsize/Nbs1-Antibody-Knockout-Validated-NB100-143-img0015.jpg "<b>Genetic Strategies Validation. </b>Western Blot: Nbs1 Antibody [NB100-143] - Lysates of HeLa human cervical epithelial carcinoma parental cell line and Nbs1 knockout (KO) HeLa cell line. PVDF membrane was probed with 1:1000 of Rabbit Anti-Human Polyclonal [NB100-143] followed by HRP-conjugated Anti-Rabbit IgG Secondary Antibody (HAF008). Specific band was detected for Nbs1 at approximately 95 kDa (as indicated) in the parental HeLa cell line, but is not detectable in the knockout HeLa cell line. This experiment was conducted under reducing conditions.")
![<b>Genetic Strategies Validation. </b>Western Blot: Nbs1 Antibody [NB100-143] - Western Blot with Nbs1 Antibody [NB100-143]. KSHV LANA recruits MRN (Mre11-Rad50-NBS1) complex. 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. Image collected and cropped by CiteAb from the following publication (//dx.plos.org/10.1371/journal.ppat.1006335), licensed under a CC-BY license.](http://images.novusbio.com/fullsize/Nbs1-Antibody-Western-Blot-NB100-143-img0016.jpg)
![Immunocytochemistry/Immunofluorescence: Nbs1 Antibody [NB100-143] - ICC/IF analysis of Nbs1 in HeLa cells with Nbs1 Antibody [NB100-143]. Image from verified customer review.](http://images.novusbio.com/fullsize/Nbs1-Antibody-Immunocytochemistry-Immunofluorescence-NB100-143-img0011.jpg)
![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.](http://images.novusbio.com/fullsize/Nbs1-Antibody-Immunohistochemistry-Paraffin-NB100-143-img0014.jpg)
![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.](http://images.novusbio.com/fullsize/Nbs1-Antibody-Western-Blot-NB100-143-img0010.jpg)
![<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.](http://images.novusbio.com/fullsize/Nbs1-Antibody-Western-Blot-NB100-143-img0012.jpg)
![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.](http://images.novusbio.com/fullsize/Nbs1-Antibody-Western-Blot-NB100-143-img0013.jpg)
![Immunocytochemistry/Immunofluorescence: Nbs1 Antibody [NB100-143] - Staining of HeLa cells using Nbs1 Antibody [NB100-143].](http://images.novusbio.com/fullsize/Nbs1-Antibody-Immunocytochemistry-Immunofluorescence-NB100-143-img0009.jpg)
![<b>Genetic Strategies Validation. </b>Immunocytochemistry/ Immunofluorescence: 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.](http://images.novusbio.com/fullsize/Nbs1 Antibody-Knockdown Validated-NB100-143-img0017.jpg)
![Immunocytochemistry/ Immunofluorescence: Nbs1 Antibody [NB100-143] - Replication centers of the integrated HPV recruit Mre11-Nbs1-Rad50 complex & Ku70/80 heterodimer.HeLa cells were transfected & analyzed as described previously. Co-immunostaining of HPV18 E1 (Alexa Fluor 568, second column) & the following proteins are presented: Mre11, Nbs1, Rad50, & Ku70/80 proteins (Alexa Fluor 488, first column). The localizations of the E1 & the respective DNA repair proteins are also shown in the third column as a merged image & DAPI stained nuclei are presented in the fourth column. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/19390600), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-143_rabbit-polyclonal-nbs1-antibody-310202415291962.jpg)
![Immunocytochemistry/ Immunofluorescence: Nbs1 Antibody [NB100-143] - Loss of MUS81 activates DNA damage responseA. MUS81 depleted U2OS cells accumulate NBS1 foci defining sites of DNA damage. B. Partial co-localization of NBS1 foci & RPA foci in MUS81-depleted cells. C. Co-localization of RPA foci to ssDNA regions. Cells were labelled with BrdU for 3 days concomitant with MUS81 depletion. BrdU was detected at ssDNA regions by immunofluorescence. D. NBS1 foci arise in cells that are both positive & negative for Cyclin A expression. Scale bars, 5 μm. E. NBS1 foci form largely at non-telomeric loci. F. Partial co-localization of NBS1 foci with PML nuclear bodies. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/26415217), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-143_rabbit-polyclonal-nbs1-antibody-310202415395910.jpg)
![Immunocytochemistry/ Immunofluorescence: Nbs1 Antibody [NB100-143] - Loss of MUS81 activates DNA damage responseA. MUS81 depleted U2OS cells accumulate NBS1 foci defining sites of DNA damage. B. Partial co-localization of NBS1 foci & RPA foci in MUS81-depleted cells. C. Co-localization of RPA foci to ssDNA regions. Cells were labelled with BrdU for 3 days concomitant with MUS81 depletion. BrdU was detected at ssDNA regions by immunofluorescence. D. NBS1 foci arise in cells that are both positive & negative for Cyclin A expression. Scale bars, 5 μm. E. NBS1 foci form largely at non-telomeric loci. F. Partial co-localization of NBS1 foci with PML nuclear bodies. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/26415217), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-143_rabbit-polyclonal-nbs1-antibody-310202415293317.jpg)
![Immunocytochemistry/ Immunofluorescence: Nbs1 Antibody [NB100-143] - Loss of MUS81 activates DNA damage responseA. MUS81 depleted U2OS cells accumulate NBS1 foci defining sites of DNA damage. B. Partial co-localization of NBS1 foci & RPA foci in MUS81-depleted cells. C. Co-localization of RPA foci to ssDNA regions. Cells were labelled with BrdU for 3 days concomitant with MUS81 depletion. BrdU was detected at ssDNA regions by immunofluorescence. D. NBS1 foci arise in cells that are both positive & negative for Cyclin A expression. Scale bars, 5 μm. E. NBS1 foci form largely at non-telomeric loci. F. Partial co-localization of NBS1 foci with PML nuclear bodies. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/26415217), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-143_rabbit-polyclonal-nbs1-antibody-31020241534354.jpg)
![Immunocytochemistry/ Immunofluorescence: Nbs1 Antibody [NB100-143] - Loss of MUS81 activates DNA damage responseA. MUS81 depleted U2OS cells accumulate NBS1 foci defining sites of DNA damage. B. Partial co-localization of NBS1 foci & RPA foci in MUS81-depleted cells. C. Co-localization of RPA foci to ssDNA regions. Cells were labelled with BrdU for 3 days concomitant with MUS81 depletion. BrdU was detected at ssDNA regions by immunofluorescence. D. NBS1 foci arise in cells that are both positive & negative for Cyclin A expression. Scale bars, 5 μm. E. NBS1 foci form largely at non-telomeric loci. F. Partial co-localization of NBS1 foci with PML nuclear bodies. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/26415217), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-143_rabbit-polyclonal-nbs1-antibody-31020241539451.jpg)
![Immunocytochemistry/ Immunofluorescence: Nbs1 Antibody [NB100-143] - HPV16 E2 partially colocalizes with the MRN complex proteins Mre11 & Nbs1. C33a cells were transfected with an HPV16 E2 expression plasmid, fixed in ice-cold methanol, & 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. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/28031358), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-143_rabbit-polyclonal-nbs1-antibody-310202415392545.jpg)
![Immunocytochemistry/ Immunofluorescence: Nbs1 Antibody [NB100-143] - Loss of MUS81 activates DNA damage responseA. MUS81 depleted U2OS cells accumulate NBS1 foci defining sites of DNA damage. B. Partial co-localization of NBS1 foci & RPA foci in MUS81-depleted cells. C. Co-localization of RPA foci to ssDNA regions. Cells were labelled with BrdU for 3 days concomitant with MUS81 depletion. BrdU was detected at ssDNA regions by immunofluorescence. D. NBS1 foci arise in cells that are both positive & negative for Cyclin A expression. Scale bars, 5 μm. E. NBS1 foci form largely at non-telomeric loci. F. Partial co-localization of NBS1 foci with PML nuclear bodies. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/26415217), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-143_rabbit-polyclonal-nbs1-antibody-310202415175283.jpg)
![Western Blot: Nbs1 Antibody [NB100-143] - UFL1 regulates the ATM signaling. a U2OS cells expressing UFL1 tet-on shRNA1 were irradiated with 2 Gy IR. Thirty minutes later, cells were lysed & blotted with indicated antibodies. b Representative picture of gamma H2AX, 53BP1, & BRCA1 foci in control (Dox-) & UFL1 knockdown (Dox+) U2OS cells 1 h after 0.5 Gy treatment. Scale bars, 10 µm. c–e Quantification of intensities of gamma H2AX, 53BP1, & BRCA1 foci in control (Dox-) & UFL1 knockdown (Dox+) U2OS cells. Data presented as mean ± SD of n = 50 cells. **p < 0.01 by Student’s t-test. Source data are provided as a Source Data file Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/30886146), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-143_rabbit-polyclonal-nbs1-antibody-31020241534365.jpg)
![Western Blot: Nbs1 Antibody [NB100-143] - Deletion of Exo1 leads to embryonic lethality in hypomorphic Nbs1 mice. (A) Graph of expected & observed live born pups from double heterozygous breedings based on normal Mendelian inheritance (n = 93). For brevity, the primary genotypes are abbreviated as follows: wild type = W, Nbs1 delta B/ delta B = N, Exo1−/− = E, Nbs1 delta B/ delta BExo−/− = NE. Statistical analysis was performed using an unpaired t-test. ***P < 0.0001 & n.s. = not significant. (B) Graph of expected & observed E14.5 embryos from double heterozygous breedings based on normal Mendelian inheritance (n = 89). (C) Representative images of E14.5 embryos of the indicated genotype. (D) Western blotting of NBS1 & EXO1 from embryonic fibroblast cultures derived from E14.5 embryos. Image collected & cropped by CiteAb from the following publication (//academic.oup.com/nar/article-lookup/doi/10.1093/nar/gkv691), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-143_rabbit-polyclonal-nbs1-antibody-310202415384186.jpg)
![Western Blot: Nbs1 Antibody [NB100-143] - EXO1 influences DNA repair & DNA replication in Nbs1 mutants. (A) Schematic illustration of the SA-GFP based SSA assay. (B) Western blotting of cells transfected with or without a vector expressing human NBS1. The genotypes are abbreviated throughout the figure as follows: wild type = W, Nbs1 delta B/ delta B = N, Exo1−/− = E, and Nbs1 delta B/ delta B Exo−/− = NE. (C) Quantification of SSA mediated repair plotted as the percentage of GFP positive cells. Values for NE are corrected for the reduced percentage of cells in S/G2 determined by BrdU & PI staining (mean 58% compared to a mean of 73% in the other genotypes). The fold rescue with NBS1 expression is the same in N & NE (2.2 fold). (D) Measurement of replication tract lengths following CldU or IdU pulse labeling. (E) Calculation of replication fork velocity in the indicated genotypes (as described in ‘Materials & Methods’ section). Examples of representative forks from W & NE cultures are shown for comparison. (F) Assessment of replication fork restart following 1 mM HU treatment using the indicated scheme. Relative tract ratio is calculated by dividing the length of the IdU tract by that of the CldU tract ( = 2 under unperturbed conditions). Thus, higher values indicate faster restart following HU removal. Image collected & cropped by CiteAb from the following publication (//academic.oup.com/nar/article-lookup/doi/10.1093/nar/gkv691), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-143_rabbit-polyclonal-nbs1-antibody-310202415535147.jpg)
![Western Blot: Nbs1 Antibody [NB100-143] - UFL1 protein accumulates at DSBs through the MRN complex. a U2OS cells stably expressing UFL1 Tet-on shRNA were treated with doxycycline (Dox) for 3–5 days, & then treated with or without 2 Gy IR. After 30 min, cells were harvested & lysed with NETN buffer. Cell lysates were incubated with UFL1 antibody + Benzonase. The immunoprecipitates were blotted with indicated antibodies. b Immunofluorescence of UFL1 & gamma H2AX in U2OS cells irradiated with IR (0.5 Gy). c Triamcinolone acetonide (TA) treatment induces the translocation of RFP-I-SceI-GR fusion protein from the cytoplasm to the nucleus & generates one double strand break at the cutting site. The protein localization was detected by indicated antibodies. d UFL1 foci formation at different time points following 0.5 Gy IR treatment. e, f UFL1 foci formation was analyzed in Mre11 knockdown cells or NBS1 deficient cells (NBST). g NBST cells were transfected with Vector (V) or Flag-NBS1 & treated with or without 2 Gy IR. After 30 min, the cells were lysed & immunoprecipitation with UFL1 antibody with Benzonase treatment was performed. The immunoprecipitates were blotted with indicated antibodies. h The schematic diagram of NBS1 protein domain. i U2OS cells were treated with or without 2 Gy IR, & the cell lysates were pulled down with GST, GST-NBS1 FHA+BRCT (1+2) proteins. After washes, the beads were boiled & analyzed with indicated antibodies. Scale bars, 10 µm. Source data are provided as a Source Data file Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/30886146), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-143_rabbit-polyclonal-nbs1-antibody-310202415535118.jpg)
![Western Blot: TDP-43/TARDBP Antibody (2E2-D3) [H00023435-M01] - TARDBP monoclonal antibody (M01), clone 2E2-D3 Analysis of TARDBP expression in A-431.](http://images.novusbio.com/fullsize/TDP-43-TARDBP-Antibody-2E2-D3-Western-Blot-H00023435-M01-img0025.jpg "Western Blot: TDP-43/TARDBP Antibody (2E2-D3) [H00023435-M01] - TARDBP monoclonal antibody (M01), clone 2E2-D3 Analysis of TARDBP expression in A-431.")
![Immunohistochemistry-Paraffin: TDP-43/TARDBP Antibody (2E2-D3) [H00023435-M01] - TARDBP in rat tissue samples. Image courtsey of product review by Daniel Pirici.](http://images.novusbio.com/fullsize/TDP-43-TARDBP-Antibody-2E2-D3-Immunohistochemistry-Paraffin-H00023435-M01-img0011.jpg)
![Western Blot: TDP-43/TARDBP Antibody (2E2-D3) [H00023435-M01] - PDI co-precipitates with TDP-43/TARDBP and is increased in mutant TDP-43 transgenic mouse spinal cords. Co-immunoprecipitation of wildtype and mutant Q331K TDP-43-mCherry from Neuro2a cell lysates using an anti-PDI antibody followed by TDP-43 immunoblot. Control immunoprecipitations were performed using untransfected (Untrans) or mCherry expressing cell lysates, buffer only with coprecipitating antibodies or TDP-43 Q331K cell lysates using an irrelevant, isotype-matched control antibody (IgG). Input control (2%) shows expression of mCherry-TDP43 in wildtype and Q331K cell lysates. Image collected and cropped by CiteAb from the following publication (//dx.plos.org/10.1371/journal.pone.0081170) licensed under a CC-BY license.](http://images.novusbio.com/fullsize/TDP-43-TARDBP-Antibody-2E2-D3-Western-Blot-H00023435-M01-img0028.jpg)
![Immunocytochemistry/Immunofluorescence: TDP-43/TARDBP Antibody (2E2-D3) [H00023435-M01] - Analysis of monoclonal antibody to TARDBP on HeLa cell. Antibody concentration 10 ug/ml.](http://images.novusbio.com/fullsize/TDP-43-TARDBP-Antibody-2E2-D3-Immunocytochemistry-Immunofluorescence-H00023435-M01-img0019.jpg)
![Immunohistochemistry-Paraffin: TDP-43/TARDBP Antibody (2E2-D3) [H00023435-M01] - TARDBP on formalin-fixed paraffin-embedded human leiomyosarcoma. [antibody concentration 3 ug/ml]](http://images.novusbio.com/fullsize/TDP-43-TARDBP-Antibody-2E2-D3-Immunohistochemistry-Paraffin-H00023435-M01-img0013.jpg)
![Western Blot: TDP-43/TARDBP Antibody (2E2-D3) [H00023435-M01] - Analysis of TARDBP expression in transfected 293T cell line by TARDBP monoclonal antibody (M01), clone 2E2-D3.Lane 1: TARDBP transfected lysate(44.7 KDa).Lane 2: Non-transfected lysate.](http://images.novusbio.com/fullsize/TDP-43-TARDBP-Antibody-2E2-D3-Western-Blot-H00023435-M01-img0026.jpg)
![Immunohistochemistry-Paraffin: TDP-43/TARDBP Antibody (2E2-D3) [H00023435-M01] - Analysis of monoclonal antibody to TARDBP on formalin-fixed paraffin-embedded human leiomyosarcoma tissue Antibody concentration 3 ug/ml.](http://images.novusbio.com/fullsize/TDP-43-TARDBP-Antibody-2E2-D3-Immunohistochemistry-Paraffin-H00023435-M01-img0021.jpg)
![<b>Genetic Strategies Validation. </b>Western Blot: TDP-43/TARDBP Antibody (2E2-D3) [H00023435-M01] - Analysis of TARDBP over-expressed 293 cell line, cotransfected with TARDBP Validated Chimera RNAi ( Cat # H00023435-R01V ) (Lane 2) or non-transfected control (Lane 1). Blot probed with TARDBP monoclonal antibody (M01), clone 2E2-D3 (Cat # H00023435-M01 ). GAPDH ( 36.1 kDa ) used as specificity and loading control.](http://images.novusbio.com/fullsize/TDP-43-TARDBP-Antibody-2E2-D3-Western-Blot-H00023435-M01-img0023.jpg)
![ELISA: TDP-43/TARDBP Antibody (2E2-D3) [H00023435-M01] - Detection limit for recombinant GST tagged TARDBP is 0.3 ng/ml as a capture antibody.](http://images.novusbio.com/fullsize/TDP-43-TARDBP-Antibody-2E2-D3-ELISA-H00023435-M01-img0027.jpg)
![Western Blot: TDP-43/TARDBP Antibody (2E2-D3) [H00023435-M01] - PDI co-precipitates with TDP-43 & is increased in mutant TDP-43 transgenic mouse spinal cords.(A) Co-immunoprecipitation of wildtype & mutant Q331K TDP-43-mCherry from Neuro2a cell lysates using an anti-PDI antibody followed by TDP-43 immunoblot. Control immunoprecipitations performed using untransfected (Untrans) or mCherry expressing cell lysates, buffer only with coprecipitating antibodies or TDP-43 Q331K cell lysates using an irrelevant, isotype-matched control antibody (IgG). Input control (2%) shows expression of mCherry-TDP43 in wildtype & Q331K cell lysates. Image collected & cropped by CiteAb from the following publication (//dx.plos.org/10.1371/journal.pone.0081170), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/h00023435-m01_mouse-monoclonal-tdp-43-tardbp-antibody-2e2-d3-310202415284521.jpg)
![Western Blot: TDP-43/TARDBP Antibody (2E2-D3) [H00023435-M01] - CLIP shows that TDP-43 directly interacts with translational target mRNAs. (A) Schematic diagram of the CLIP experiment. (B) Immunoblot showing specific IP of TDP-43 from MN1 cells under CLIP conditions. A TDP-43 band is specifically observed in the input & TDP-43 IP lanes from both untreated & UV-treated cells, but not in the IgG or anti-RBP X control lanes. RBP X is an IP of a different RNA-binding protein, which serves as an additional specificity control here. (C and D) Plots showing percentage of input mRNA in the TDP-43 IP for the mRNAs indicated in three separate CLIP assays from MN1 cells. Performing CLIP from UV-treated cells leads to significant recovery & enrichment relative to Gapdh for all mRNAs examined (C). In the absence of UV treatment, much less mRNA is recovered & no significant enrichment relative to Gapdh mRNA is observed. Note that the Y-axis scale in D is 1000× smaller than in C, indicating strong crosslinking dependence of mRNA co-immunoprecipitation (n = 3, s.e.m. error bars, P-values indicated in the plot, unpaired two-tailed t-test). Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/30357366), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/h00023435-m01_mouse-monoclonal-tdp-43-tardbp-antibody-2e2-d3-310202415483647.jpg)
![Western Blot: TDP-43/TARDBP Antibody (2E2-D3) [H00023435-M01] - SINE compounds partially rescue motor deficits in an animal model of ALS/FTD. (a) Schematic timeline for in vivo experiments. (b) Western blot demonstrating the expression of human TDP43 within the brains of AAV9-injected animals, which we have previously shown is largely restricted to neuronal cell types (Jackson et al.59). Full-length blots appear in Fig. S1. (c) The hang test measures the time it takes for animals to fall from grid-like scaffold when it is lifted & tilted. A single representative animal administered AAV9-TDP43 is shown; note the inability of the hind limbs to clasp the wire mesh. (d) TDP43 expression impaired motor performance on the hang test at 3 weeks, an effect that could be mitigated by 7.5 mg kg-1 KPT-350. (e) Rotarod testing at 4 weeks of age showed prominent deficits associated with TDP43 expression that were resistant to treatment with SINE compounds. n, number of animals per condition. ns, not significant, mean ± s.e.m. *p < 0.05, **p < 0.01, ***p < 0.001, one-way ANOVA with Bonferroni correction. Image collected & cropped by CiteAb from the following publication (//www.nature.com/articles/s41598-018-22858-w), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/h00023435-m01_mouse-monoclonal-tdp-43-tardbp-antibody-2e2-d3-310202415482260.jpg)
![Immunocytochemistry/Immunofluorescence: Ki67/MKI67 Antibody [NB500-170] - 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- NB500-170 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.](http://images.novusbio.com/fullsize/Ki67-MKI67-Antibody-Immunocytochemistry-Immunofluorescence-NB500-170-img0025.jpg "Immunocytochemistry/Immunofluorescence: Ki67/MKI67 Antibody [NB500-170] - 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- NB500-170 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.")
![<b>Genetic Strategies Validation. </b>Simple Western: Ki67/MKI67 Antibody [NB500-170] - Detection of Ki67/MKI67 by Simple WesternTM. Simple Western lane view shows lysates of HeLa parental cell line and Ki67 knockout (KO) HeLa cell line. A specific band was detected for Ki67/MKI67 at approximately 320 kDa (as indicated) in the parental cell line, but is not detectable in the knockout HeLa cell line using 20 ug/mL of Rabbit Anti-Ki67/MKI67 Polyclonal Antibody (Catalog # NB500-170). GAPDH is shown as a loading control. This experiment was conducted under reducing conditions and using the 12-230 kDa separation system.](http://images.novusbio.com/fullsize/Ki67-MKI67-Antibody-Knockout-Validated-NB500-170-img0023.jpg)
![Immunohistochemistry: Ki67/MKI67 Antibody [NB500-170] - Senescent MSPCs are characterized by loss of nestin expression. Double-immunofluorescence images of femoral metaphysis sections from 4-, 6-, 8-, and 12-week-old male Nestin-GFP mice using antibodies against GFP (green) and Ki67 (red). DAPI stains nuclei blue. GP growth plate. PS primary spongiosa. Quantification of the percentage of GFP+ cells that express Ki67. Image collected and cropped by CiteAb from the following publication (//www.nature.com/articles/s41467-017-01509-0) licensed under a CC-BY license.](http://images.novusbio.com/fullsize/Ki67-MKI67-Antibody-Immunocytochemistry-Immunofluorescence-NB500-170-img0022.jpg)
![Immunohistochemistry-Paraffin: Ki67/MKI67 Antibody [NB500-170] - Ki-67/MKI67 Antibody [NB500-170] - Tissue section of human tonsil using 1:50 dilution of rabbit anti-KI67 antibody. The staining was developed with HRP labeled anti-rabbit IgG secondary antibody and DAB reagent, and nuclei of cells were counter-stained with hematoxylin. This Ki67 antibody generated a specific nuclear staining in the cells in germinal centers of the tested tonsil tissue.](http://images.novusbio.com/fullsize/Ki-67-MKI67-Antibody-Immunohistochemistry-Paraffin-NB500-170-img0019.jpg)
![Immunohistochemistry-Paraffin: Ki67/MKI67 Antibody [NB500-170] - Ki-67/MKI67 Antibody [NB500-170] - Human tonsil using 1:200 dilution of rabbit anti-KI67 antibody. The staining was developed with HRP labeled anti-rabbit IgG secondary antibody and DAB reagent, and nuclei of cells were counter-stained with hematoxylin. This Ki67 antibody generated a specific nuclear staining in the cells in germinal centers of the tested tonsil tissue.](http://images.novusbio.com/fullsize/Ki-67-MKI67-Antibody-Immunohistochemistry-Paraffin-NB500-170-img0020.jpg)
![Western Blot: Ki67/MKI67 Antibody - BSA Free [NB500-170] - Whole cell lysates from SUM159, MDA-MB-231 and MCF-7 cells were loaded with 30 ug/lane. 10% SDS-PAGE. Ki67/MKI67 antibody (NB500-170) was used for primary antibody: 1:2000, 4C, overnight. Image from verified customer review.](http://images.novusbio.com/fullsize/Ki67-MKI67-Antibody---BSA-Free-Western-Blot-NB500-170-img0028.jpg)
![Immunocytochemistry/Immunofluorescence: Ki67/MKI67 Antibody [NB500-170] - 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-Ki67/MKI67 Antibody NB500-170 at 2 ug/ml overnight at 4C and detected with an anti-rabbit Dylight 488 (Green) at a 1:1000 dilution for 60 minutes. Nuclei were counterstained with DAPI (Blue). Cells were imaged using a 100X objective and digitally deconvolved.](http://images.novusbio.com/fullsize/Ki67-MKI67-Antibody-Immunocytochemistry-Immunofluorescence-NB500-170-img0026.jpg)
![Flow Cytometry: Ki67/MKI67 Antibody - BSA Free [NB500-170] - An intracellular stain was performed on U-251 MG cells with Ki67/MKI67 Antibody NB500-170AF594 (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 2.5 ug/mL for 30 minutes at room temperature. Both antibodies were conjugated to Alexa Fluor 594.](http://images.novusbio.com/fullsize/Ki67-MKI67-Antibody---BSA-Free-Flow-Cytometry-NB500-170-img0027.jpg)
![Western Blot: Ki67/MKI67 Antibody [NB500-170] - Ki-67/MKI67 Antibody [NB500-170] - Analysis of A431 (A) and Hek293 (B) cell lysate using Ki67 antibody (NB500-170) at 2 ug/ml.](http://images.novusbio.com/fullsize/Ki-67-MKI67-Antibody-Western-Blot-NB500-170-img0017.jpg)
![Immunocytochemistry/Immunofluorescence: Ki67/MKI67 Antibody [NB500-170] - Ki67 antibody was tested at 1:25 in HeLa cells with FITC (green). Nuclei and actin were counterstained with Dapi (blue) and Phalloidin (red).](http://images.novusbio.com/fullsize/Ki-67-MKI67-Antibody-Immunocytochemistry-Immunofluorescence-NB500-170-img0014.jpg)
![Immunocytochemistry/Immunofluorescence: Ki67/MKI67 Antibody [NB500-170] - Confocal immunofluorescent analysis of MCF7 cells using Ki67 antibody (NB500-170, 1:5). An Alexa Fluor 488-conjugated Goat to rabbit IgG was used as secondary antibody (green). Actin filaments were labeled with Alexa Fluor 568 phalloidin (red). DAPI was used to stain the cell nuclei (blue).](http://images.novusbio.com/fullsize/Ki-67-MKI67-Antibody-Immunocytochemistry-Immunofluorescence-NB500-170-img0016.jpg)
![Immunocytochemistry/Immunofluorescence: Ki67/MKI67 Antibody [NB500-170] - A431 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- NB500-170 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.](http://images.novusbio.com/fullsize/Ki67-MKI67-Antibody-Immunocytochemistry-Immunofluorescence-NB500-170-img0024.jpg)
![Immunohistochemistry-Paraffin: Ki67/MKI67 Antibody [NB500-170] - Ki-67/MKI67 Antibody [NB500-170] - Human tonsil.](http://images.novusbio.com/fullsize/Ki-67-MKI67-Antibody-Immunohistochemistry-Paraffin-NB500-170-img0015.jpg)
![Immunohistochemistry: Ki67/MKI67 Antibody - BSA Free [NB500-170] - PKD2 enzymatic deficiency had no effect on the proliferation or apoptosis of intestinal epithelial cells in mice exposed to DSS.(a) Representative 200× immunohistochemical images (left) & quantification of Ki-67+ proliferating intestinal epithelial cells (right) in wild-type & PKD2SSAA/SSAA mice. Bar represents 5 μm. (b) Representative 200× immunohistochemical images (left) & quantification of cleaved Caspase-3+ apoptotic intestinal epithelial cells (right) in wild-type & PKD2SSAA/SSAA mice. Bar represents 5 μm. Results are representative of three separate experiments with three mice per group. All p > 0.05 as measured by one way-ANOVA among four groups. Image collected & cropped by CiteAb from the following publication (//www.nature.com/articles/srep34079), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb500-170_rabbit-polyclonal-ki67-mki67-antibody-3102024153437.jpg)
![Immunohistochemistry: Ki67/MKI67 Antibody - BSA Free [NB500-170] - Deletion of Vangl2, but not Vangl1, in the mammary gland results in narrow ducts & low cell turnover. (A) RT-qPCR analysis of Vangl1 & Vangl2 mRNA levels in the mammary glands of MMTV-Cre, MMTV-Cre;Vangl2flox/+ & MMTV-Cre;Vangl2flox/flox at 10 weeks of age. (B) Representative images of 10 week old, carmine stained mammary glands & quantification of total branch number from MMTV-Cre, MMTV-Cre;Vangl2flox/+ & MMTV-Cre;Vangl2flox/flox mice (n = 3 mice per genotype). (C) Histological analysis by H&E staining show normal duct formation in 10 week old MMTV-Cre & MMTV-Cre;Vangl2flox/+ glands, whereas ducts from MMTV-Cre;Vangl2flox/flox glands are narrow & have significantly diminished lumens (n = 3 mice/genotype). (D) Immunostaining in mammary ducts show normal distribution of luminal (Cytokeratin 8 (K8), green), & basal (K5), red; SMA magenta) cell populations. (E) Immunofluorescence of adhesion junctional protein E-Cadherin (CDH1, green) & apical membrane marker pERM (red). (F,G) Immunostaining in 10 week old MMTV-Cre;Vangl2+/+ & MMTV-Cre;Vangl2flox/flox glands & quantitation of (F) Ki67 & (G) Cleaved Caspase 3 (n = 3–5 mice per genotype). Lu indicates lumen. * indicates non-magnified duct. Data are represented as mean +/− SEM. Scale bar represents 100 μm (C,F,G) 50 μm (D) & 10 μm (E). Student’s t-test *p < 0.05 & ****p < 0.0001. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31068622), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb500-170_rabbit-polyclonal-ki67-mki67-antibody-310202416171470.jpg)
![Immunocytochemistry/ Immunofluorescence: Ki67/MKI67 Antibody - BSA Free [NB500-170] - Senescent MSPCs are characterized by loss of nestin expression. a, b Representative images of GFP immunofluorescence staining (green) & quantitative analysis of GFP+ cells in femoral primary spongiosa from 4, 6, 8, & 12-week-old male Nestin-GFP mice. Images in upper panels in a are lower power w/ boxes outlining area of higher power in lower panels. Numbers of GFP+ cells per mm2 tissue area in primary spongiosa (N. GFP+ cells/PS.Ar) b. 4W, 6W, 8W, & 12W represent 4-, 6-, 8-, & 12-week-old mice, respectively. DAPI stains nuclei blue. c, d Representative images of flow cytometry analysis (c) & % of CD45−GFP+ cells (d) in femoral metaphysis from 4-, 6-, 8-, & 12-week-old male Nestin-GFP mice. e, f Double-immunofluorescence images of femoral metaphysis sections from 4-, 6-, 8-, & 12-week-old male Nestin-GFP mice using antibodies against GFP (green) & Ki67 (red) e. DAPI stains nuclei blue. GP growth plate. PS primary spongiosa. Quantification of % of GFP+ cells that express Ki67 f. Five mice per group. Data are represented as mean ± s.e.m. *P < 0.05 as determined by ANOVA. g Diagram showing isolation of Nestin-GFP+ (red) & Nestin-GFP− (purple) mesenchymal stem/progenitor cells (MSPCs) by fluorescence-activated cell sorting. Detailed information on isolation of MSPCs from femoral metaphysis from Nestin-GFP mice are described in Supplementary Fig. 3 & Methods section. h–j The sorted cells cultured, & SA-beta Gal staining (h), BrdU incorporation (i), & p16INK4a immunostaining (j) performed, & representative images shown. k–m Quantification of % of cells that express SA-beta Gal (k), BrdU (l), & p16INK4a (m). n = 5. Data are represented as mean ± s.e.m. *P < 0.01 as determined by Student’s t-tests Image collected & cropped by CiteAb from following publication (//pubmed.ncbi.nlm.nih.gov/29101351), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb500-170_rabbit-polyclonal-ki67-mki67-antibody-310202416175292.jpg)
![Immunocytochemistry/ Immunofluorescence: Ki67/MKI67 Antibody - BSA Free [NB500-170] - Cellular senescence occurs in primary spongiosa of long bone during late puberty. a–e Representative senescence-associated beta -galactosidase (SA-beta Gal) staining (blue) & quantitative analysis of SA-beta Gal+ cells in femoral metaphysis (a–c) & diaphysis (d, e) sections from increasing ages of male mice. 4, 6, 8, & 12W represent 4-, 6-, 8-, & 12-week-old mice, respectively. Images in a are lower power with boxes outlining the area of higher power in b. Numbers of SA-beta Gal+ cells per mm2 tissue area in primary spongiosa (N. SA-beta Gal+ cells/PS.Ar) (c) & diaphysis (N. SA-beta Gal+ cells/DP.Ar) (e). Counterstained with eosin (pink). f, g Representative images of immunofluorescence staining (f) & quantitative analysis of ki67+ (g) cells (red) in femoral primary spongiosa from 4, 6, 8, & 12-week-old male mice. DAPI stains nuclei blue. Images in upper panels in f are lower power with boxes outlining the area of higher power in lower panels. Five mice per group. Data are represented as mean ± s.e.m. Ar tissue area, DP diaphysis, GP growth plate, N number, PS primary spongiosa. *P < 0.01 as determined by ANOVA Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/29101351), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb500-170_rabbit-polyclonal-ki67-mki67-antibody-310202416175289.jpg)
![Immunocytochemistry/Immunofluorescence: TRF-2 Antibody [NB110-57130] - 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 antibody at a 1:200 dilution overnight at 4 degrees Celsius and detected with DyLight 488 (Green) at a 1:500 dilution. Alpha tubulin was used as a co-stain at a 1:1000 dilution and detected with Dylight 550 (Red). Nuclei were detected with DAPI (Blue) at 2.0 ug/ml in 1X PBS. Cells were imaged using a 40X objective.](http://images.novusbio.com/fullsize/TRF-2-Antibody-Immunocytochemistry-Immunofluorescence-NB110-57130-img0011.jpg "Immunocytochemistry/Immunofluorescence: TRF-2 Antibody [NB110-57130] - 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 antibody at a 1:200 dilution overnight at 4 degrees Celsius and detected with DyLight 488 (Green) at a 1:500 dilution. Alpha tubulin was used as a co-stain at a 1:1000 dilution and detected with Dylight 550 (Red). Nuclei were detected with DAPI (Blue) at 2.0 ug/ml in 1X PBS. Cells were imaged using a 40X objective.")
![Simple Western: TRF-2 Antibody [NB110-57130] - Lane view shows a specific band for TRF2 in 1.0 mg/mL of HeLa lysate. This experiment was performed under reducing conditions using the 12-230 kDa separation system.](http://images.novusbio.com/fullsize/TRF-2-Antibody-Simple-Western-NB110-57130-img0010.jpg)
![Western Blot: TRF-2 Antibody [NB110-57130] - Analysis of HeLa whole cell lysate (A), HeLa nuclear cell lysate (B), k562 cell lysate (C), HepG2 cell lysate (D), NIH/3T3 cell lysate (E), CHO cell lysate (F), PC12 cell lysate (G), and Cos7 cell lysate (H) using antibody at a concentration of 2 ug/mL.](http://images.novusbio.com/fullsize/TRF-2-Antibody-Western-Blot-NB110-57130-img0008.jpg)
![Immunohistochemistry-Paraffin: TRF-2 Antibody [NB110-57130] - Analysis in xenografted human breast cancer tissue using DAB with hematoxylin counterstain.](http://images.novusbio.com/fullsize/TRF-2-Antibody-Immunohistochemistry-Paraffin-NB110-57130-img0007.jpg)
![Immunohistochemistry-Paraffin: TRF-2 Antibody [NB110-57130] - Analysis of FFPE human breast cancer tissue with rabbit polyclonal TRF2 antibody at a dilution of 1:200. The staining was developed with HRP-DAB detection method and the counterstaining was performed using hematoxylin. This TRF2 antibody generated an expected nuclear signal in all the cancer cells and the stromal cells. In the tested section, only a subset of myoepithelial cells showed positivity for this protein.](http://images.novusbio.com/fullsize/TRF-2-Antibody-Immunohistochemistry-Paraffin-NB110-57130-img0013.jpg)
![Immunocytochemistry/Immunofluorescence: TRF-2 Antibody [NB110-57130] - 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-TRF-2 Antibody NB110-57130 at 2 ug/ml overnight at 4C and detected with an anti-rabbit Dylight 488 (Green) at a 1:1000 dilution for 60 minutes. Nuclei were counterstained with DAPI (Blue). Cells were imaged using a 100X objective and digitally deconvolved.](http://images.novusbio.com/fullsize/TRF-2-Antibody-Immunocytochemistry-Immunofluorescence-NB110-57130-img0016.jpg)
![Flow Cytometry: TRF-2 Antibody [NB110-57130] - An intracellular stain was performed on HeLa cells with TRF-2 Antibody NB110-57130 (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).](http://images.novusbio.com/fullsize/TRF-2-Antibody-Flow-Cytometry-NB110-57130-img0017.jpg)
![Chromatin Immunoprecipitation: TRF-2 Antibody [NB110-57130] - Analysis in mouse. Titrated TRF2 antibody to determine concentration required for ChIP experiment. ChIP image submitted by a verified customer review.](http://images.novusbio.com/fullsize/TRF-2-Antibody-Chromatin-Immunoprecipitation-NB110-57130-img0009.jpg)
![<b>Genetic Strategies Validation. </b>Immunocytochemistry/Immunofluorescence: TRF-2 Antibody [NB110-57130] - RNAi-mediated depletion of human separase (ESPL1) induces TIFs. Control scrambled siRNA- (control) and ESPL1 siRNA-treated fibroblasts stained with anti-p53-binding protein 1 (53BP1; green) and anti-TRF2 (red). It is noteworthy that in ESPL1 siRNA-treated cells, 53BP1 signals frequently overlap with TRF2 signals marking the TIFs. Scale bar, 5 um. Image collected and cropped by CiteAb from the following publication (//www.nature.com/doifinder/10.1038/ncomms10405), licensed under a CC-BY license.](http://images.novusbio.com/fullsize/TRF-2-Antibody-Immunocytochemistry-Immunofluorescence-NB110-57130-img0015.jpg)
![Immunohistochemistry-Paraffin: TRF-2 Antibody [NB110-57130] - Analysis of FFPE human breast cancer tissue with rabbit polyclonal TRF2 antibody at 1:200 dilution. The staining was developed with HRP-DAB detection method and the counterstaining was performed using hematoxylin. This TRF2 antibody generated an expected nuclear signal in all the cancer cells and the stromal cells. In the tested section, only a subset of myoepithelial cells showed positivity for this protein.](http://images.novusbio.com/fullsize/TRF-2-Antibody-Immunohistochemistry-Paraffin-NB110-57130-img0012.jpg)
![Flow Cytometry: TRF-2 Antibody [NB110-57130] - An intracellular stain was performed on HeLa cells with TRF-2 Antibody NB110-57130AF488 (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.](http://images.novusbio.com/fullsize/TRF-2-Antibody-Flow-Cytometry-NB110-57130-img0014.jpg)
![Western Blot: TRF-2 Antibody - BSA Free [NB110-57130] - Repressive chromatin induced on p21 promoter in TRF2 dependent way. (A–C) Loss of chromatin activation marks H3K4Me, H3K4Me2 in stable TRF2 expressed HT1080 cells (A); increase in LSD1 occupancy in TRF2 over-expressing HT1080 cells. (B) (Full images are shown in Supplementary Figures S6 & S7); Co-immunoprecipitation of TRF2 with LSD1 (immunoprecipitation with anti-TRF2 antibody followed by immunoblotting with anti-LSD1 or anti-TRF2 antibody) (C); (D) Reverse Co-immunoprecipitation of LSD1 with TRF2 (immunoprecipitation with anti-LSD1 antibody followed by immunoblotting with anti-TRF2 antibody); (E) & reduced occupancy of the repressor complex REST, Co-REST & LSD1 on silencing TRF2 on p21 promoter. Image collected & cropped by CiteAb from the following publication (//www.nature.com/articles/s41598-017-11177-1), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb110-57130_rabbit-polyclonal-trf-2-antibody-31020241528452.jpg)
![Chromatin Immunoprecipitation: TRF-2 Antibody - BSA Free [NB110-57130] - TRF2 occupancy on G4-motif sites on gene promoters within cells.A, telomeric enrichment was tested for TRF2 ChIP samples performed in HT1080 cells. Telomeric signal was normalized to signal from ALU probe. B, TRF2 occupancy at gene promoter sites in HT1080 cells (endogenous TRF2 & TRF2-overexpressed) quantified using ChIP-qRT PCR. TRF2 ChIP/IgG (mock) enrichment was normalized to 1% input; CTCF promoter (which does not harbor a TRF2 peak) was used as negative control; error bars correspond to S.D., & statistical significance was calculated by paired t test (*, p < 0.05; **, p < 0.01). For the TRF2-overexpressed condition (in red), all p values were <0.01. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31575660), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb110-57130_rabbit-polyclonal-trf-2-antibody-310202415293320.jpg)
![Western Blot: TRF-2 Antibody - BSA Free [NB110-57130] - Repressive chromatin induced on p21 promoter in TRF2 dependent way. (A–C) Loss of chromatin activation marks H3K4Me, H3K4Me2 in stable TRF2 expressed HT1080 cells (A); increase in LSD1 occupancy in TRF2 over-expressing HT1080 cells. (B) (Full images are shown in Supplementary Figures S6 & S7); Co-immunoprecipitation of TRF2 with LSD1 (immunoprecipitation with anti-TRF2 antibody followed by immunoblotting with anti-LSD1 or anti-TRF2 antibody) (C); (D) Reverse Co-immunoprecipitation of LSD1 with TRF2 (immunoprecipitation with anti-LSD1 antibody followed by immunoblotting with anti-TRF2 antibody); (E) & reduced occupancy of the repressor complex REST, Co-REST & LSD1 on silencing TRF2 on p21 promoter. Image collected & cropped by CiteAb from the following publication (//www.nature.com/articles/s41598-017-11177-1), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb110-57130_rabbit-polyclonal-trf-2-antibody-310202415363710.jpg)
![Chromatin Immunoprecipitation: TRF-2 Antibody - BSA Free [NB110-57130] - Thousands of extra-telomeric TRF2 binding sites found across the genome.A, extra-telomeric TRF2 peaks found in HT1080 cells following TRF2 ChIP-Seq: 20304 TRF2 peaks were common between two independent experiments. B, distribution of common TRF2 peaks around TSSs. Distance from the TSS is shown in kb. C, replicate consistency plot generated using irreproducible discovery rate analysis; 1956 peaks found at ≤0.01 are marked. D, distribution of 1956 TRF2 peaks with IDR 0.01 (TRF2HC peaks) around the TSS. Distance from the TSS is shown in kb. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31575660), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb110-57130_rabbit-polyclonal-trf-2-antibody-310202415371955.jpg)
![Western Blot: TRF-2 Antibody - BSA Free [NB110-57130] - TRF1HP1 alpha allele-specific protection effects upon si-TRF2-induced telomeric damage. 72 h after transfection, a TRF2 knockdown efficiency with antibody against TRF2 (anti-TRF2) & GAPDH (anti-GAPDH) as loading control. (−) si-non-targeting; (+) si-TRF2. Quantification of TIFs in b si-non-targeting (n = 32–47 nuclei per group) or c si-TRF2. Left *p = 0.0188, right *p = 0.0192, **p = 0.0042, ****p < 0.0001 (n = 31–48 nuclei per group). b, c Significance is assessed by one-way ANOVA & Dunnett’s multiple comparison test with 95% confidence level. Error bars represent s.e.m. Note the similar pattern among TRF1HP1 alpha alleles in c compared to the corresponding allele pattern in Fig. 4b Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/30181605), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb110-57130_rabbit-polyclonal-trf-2-antibody-310202415284520.jpg)
![Chromatin Immunoprecipitation: TRF-2 Antibody - BSA Free [NB110-57130] - TRF2 peaks harbor G-quadruplex motifs genome-wide.A, schematic representation of a G4 motif; sequence pattern with loop/stem & PG4 motif formed by a tetrad of guanine trimers interspersed with loops that can vary in length. B & C, PG4 motifs & TRF2 peaks significantly overlap. High-confidence TRF2-binding sites (TRF2HC peaks) determined by ChIP-Seq in HT1080 cells were significantly enriched in PG4-motif sequences (B), & conversely, PG4-motif sequences were enriched within TRF2HC peaks (C). Nonoverlapping PG4 motifs were considered for analysis; for control analysis, 100 regions of identical length for each TRF2 peak were taken. *, p < 0.05; **, p < 0.01 (Fisher's exact test). Error bars, S.D. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31575660), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb110-57130_rabbit-polyclonal-trf-2-antibody-31020241538415.jpg)
![Western Blot: TRF-2 Antibody - BSA Free [NB110-57130] - Repressive chromatin induced on p21 promoter in TRF2 dependent way. (A–C) Loss of chromatin activation marks H3K4Me, H3K4Me2 in stable TRF2 expressed HT1080 cells (A); increase in LSD1 occupancy in TRF2 over-expressing HT1080 cells. (B) (Full images are shown in Supplementary Figures S6 & S7); Co-immunoprecipitation of TRF2 with LSD1 (immunoprecipitation with anti-TRF2 antibody followed by immunoblotting with anti-LSD1 or anti-TRF2 antibody) (C); (D) Reverse Co-immunoprecipitation of LSD1 with TRF2 (immunoprecipitation with anti-LSD1 antibody followed by immunoblotting with anti-TRF2 antibody); (E) & reduced occupancy of the repressor complex REST, Co-REST & LSD1 on silencing TRF2 on p21 promoter. Image collected & cropped by CiteAb from the following publication (//www.nature.com/articles/s41598-017-11177-1), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb110-57130_rabbit-polyclonal-trf-2-antibody-310202415392522.jpg)
![Western Blot: TRF-2 Antibody - BSA Free [NB110-57130] - TRF2 transcriptionally regulates p21 expression through promoter occupancy. (A) Quantitative ChIP using TRF2 antibody gives enriched binding of TRF2 on p21 promoter in HT1080 & MDA-MB-231 cells, IgG was used as isotypic antibody control; normalized with 10% input (data represented as mean ± SEM, for three replicates). (B,C) TRF2 represses p21 promoter activity. In luciferase assay, si-RNA-mediated silencing or TRF2 over expression resulted in increased (B, *p value < 0.05, Student’s t-test; data represented as mean ± SEM of three replicates) or reduction (C, *p value < 0.05, Student’s t-test; data represented as mean ± SEM of three replicates) in p21 promoter activity in HT1080 & MDA-MB-231 cells, respectively; over expression of TRF2 devoid of DNA binding [deletion of basic (delB), myb (delM) & both basic/myb (delB-delM) domains] resulted in partial or complete rescue of p21 promoter activity in HT1080 & MDA-MB-231 cells (data represented as mean ± SEM, for three replicates) (C). (D,E) HT1080 cells over expressing TRF2 show reduced p21 protein expression, bar graph shows the densitometry analysis of three different immunoblot replicates (*p value < 0.05, Student’s t-test; data represented as mean ± SEM of three replicates). (E) (Full images are shown in Supplementary Figure S5); TRF2 silencing results in increase in p21 protein, bar graph shows the densitometry analysis of three different immunoblots (*p value < 0.05, Student’s t-test; data represented as mean ± SEM of three replicates) (F); & mRNA expression in HT1080 cells (*p value < 0.05, Student’s t-test; data represented as mean ± SEM of three replicates, GAPDH used as internal control for real-time PCR). Image collected & cropped by CiteAb from the following publication (//www.nature.com/articles/s41598-017-11177-1), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb110-57130_rabbit-polyclonal-trf-2-antibody-31020241624926.jpg)
![Chromatin Immunoprecipitation: TRF-2 Antibody - BSA Free [NB110-57130] - TRF2 occupancy at gene promoters is sensitive to intracellular G-quadruplex–binding ligand 360A.A, TRF2 occupancy at gene promoter sites was checked by ChIP qRT-PCR in HT1080 cells following overexpression of TRF2 in the presence or absence of 360A. Error bars, S.D. from three independent experiments; CTCF promoter was used as a negative control. B, TRF2 level was checked by Western blotting in the presence of the ligand 360A in both untransfected & TRF2 transient overexpression conditions. Overexpression was also confirmed by probing for DDK tag. GAPDH was used as loading control. C, expression of target genes was analyzed by qRT-PCR in HT1080 cells following overexpression of TRF2 in the presence or absence of 360A. GAPDH expression was used for normalization; error bars, S.D. from three independent experiments. Statistical significance was calculated by paired t test (*, p < 0.05; **, p < 0.01). Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31575660), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb110-57130_rabbit-polyclonal-trf-2-antibody-3102024162491.jpg)
![Western Blot: TRF-2 Antibody - BSA Free [NB110-57130] - A. Co-IP analysis of the interaction between DSP & TRF2 in HEK293 cells & MCF-7 cells. B. Co-IP analysis of the interaction between DSP & TRF2 in DSP-EGFP transfected HEK293 cells or DSP△NLS-EGFP transfected HEK293 cells. C. DSP pull down by telomere targeting CASID with the condition of TRF2 knockdown in HEK293 cells. Histone H3 is the loading control. D.TRF1 & TRF2 pull-down assay by telomere targeting CASID with the condition of DSP knockdown in HEK293 cells. E. Left, Dot blot of telomere DNA repeats in chromatin pull down by DSP with the condition of TRF1 or TRF2 knockdown. The dot-blot was performed at least three times & the represented one is shown. Right, the histogram shows the quantitated results of the dot blots. The triple asterisks (***) indicates a p-value less than 0.01. ns. indicates the insignificance difference. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31595153), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb110-57130_rabbit-polyclonal-trf-2-antibody-310202416235527.jpg)
![Immunocytochemistry/ Immunofluorescence: TRF-2 Antibody - BSA Free [NB110-57130] - TERRA & telomere transcription in ALT cells.(a) TERRA northern blot hybridizations of RNA from the indicated cell lines (VA13: WI-38 VA13; 1.2.11: HeLa 1.2.11) pre-treated with RNaseA or left untreated. Ethidium bromide stained 18S ribosomal RNA (rRNA) is shown to control for loading. Long TERRA molecules comprised between the wells of the gels (w) & 28S rRNA are indicated. (b) TERRA CpG-island promoter methylation analysis of the indicated cell lines. Genomic DNA was digested with the methylation sensitive restriction enzyme MspI or its methylation insensitive isoschizomer HpaII. DNA was hybridized using a radioactively labelled probe detecting TERRA promoter CpG-island repeats. Nomet: fragments corresponding to unmethylated restriction products. (c) Dot blot hybridization of DNA immunoprecipitated with antibodies against phosphorylated Serines S2 & S5 of RNA polymerase II C-terminal domain. Hybridizations were performed with a telomeric probe. Quantifications are shown at the bottom. (d) Bars & error bars are averages & s.d. from three independent experiments. (e) Examples of TERRA FISH in the indicated cells. TERRA is shown in red, DAPI-stained DNA in blue. Scale bar, 9 μm. (f) IF/FISH experiments in the indicated cell lines. TERRA is in red, TRF2 in green & PML in blue. In the merge panels, arrowheads point to nuclear foci where the three factors co-localize. Scale bar, 9 μm. (g) Information surface at 0.01 μm detail level of three TERRA-containing APBs. TERRA is in red, TRF2 in green & PML in cyan. Images were generated with Three-Dimensional Structured Illumination Microscopy (3D-SIM). Scale bars, 0.4 μm. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/25330849), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb110-57130_rabbit-polyclonal-trf-2-antibody-310202416235545.jpg)
![Western Blot: TRF-2 Antibody - BSA Free [NB110-57130] - TRF2 occupancy at gene promoters is sensitive to intracellular G-quadruplex–binding ligand 360A.A, TRF2 occupancy at gene promoter sites was checked by ChIP qRT-PCR in HT1080 cells following overexpression of TRF2 in the presence or absence of 360A. Error bars, S.D. from three independent experiments; CTCF promoter was used as a negative control. B, TRF2 level was checked by Western blotting in the presence of the ligand 360A in both untransfected & TRF2 transient overexpression conditions. Overexpression was also confirmed by probing for DDK tag. GAPDH was used as loading control. C, expression of target genes was analyzed by qRT-PCR in HT1080 cells following overexpression of TRF2 in the presence or absence of 360A. GAPDH expression was used for normalization; error bars, S.D. from three independent experiments. Statistical significance was calculated by paired t test (*, p < 0.05; **, p < 0.01). Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31575660), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb110-57130_rabbit-polyclonal-trf-2-antibody-31020241624924.jpg)
![Western Blot: TRF-2 Antibody - BSA Free [NB110-57130] - A. Gene ontology analysis of proteins identified by CASID targeting telomeres. B. Western blot detection of TRF1, POT1, & DSP in the proteins pulled down by CASID with the presence of telo-sgRNA in HEK293 cells. Input represents the initial nuclear extract before the pull-down mediated by CASID. C. left, ChIP assay of telomere binding of TRF2 or DSP in MCF-7 cells & HEK293 cells. The chromatin DNA precipitated by anti-DSP & anti-TRF2 antibodies were analyzed by dot blot using the probes recognizing telomere (Telo-p) or Alu DNA repeats (Alu-p). The detection of Alu DNA repeats serves as negative control. The dot-blot was performed at least three times & the represented one is shown. Right, the histogram shows the quantitated results of the dot blots. The triple asterisks (***) indicates a p-value less than 0.01. D. Fluorescence imaging of DSP-EGFP in MCF-7 cells & U2OS cells. The EGFP signal indicates the localization of DSP-EGFP (green) & the Telo-FISH signal indicates the localization of telomeres (red). The overlapping between DSP-EGFP & Telo-FISH is in yellow as revealed in the enlarged nuclear area. The dCAS9-EGFP construct without telo-sgRNA was used for U2OS transfection & the imaging of EGFP serves as negative control. E. DSP localization in interphase & pro-metaphase nucleus. DSP-EGFP indicates the DSP locations & DAPI indicates the nucleus. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31595153), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb110-57130_rabbit-polyclonal-trf-2-antibody-31020241624912.jpg)
![Western Blot: TRF-2 Antibody - BSA Free [NB110-57130] - TRF2 interacts with lamin A/C.(a) Pull down of endogenous TRF2 in IMR90s. The top panel shows a blot probed for endogenous lamin A/C, & the bottom panel shows a blot with the same samples probed for TRF2. (b) Pull down of endogenously expressed lamin A/C in IMR90s. The top panel shows a blot probed for endogenous TRF2, & the bottom panel shows a blot with the same samples probed for endogenous lamin A/C. (c) Pull down of endogenous lamin A/C in IMR90s exogenously expressing GFP, GFP-TRF2, GFP-TRF delta B delta M or GFP-TRF1. The top panel shows a blot probed for GFP, & the bottom panel shows the same blot probed for lamin A/C. (d) Pull down of endogenous TRF2 in IMR90s exogenously expressing GFP, GFP-LMNA or progerin (GFP-LMNA delta 50). The top panel shows a blot probed for GFP, & the bottom panel shows the same blot probed for TRF2. Asterisks denote IgG bands. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/25399868), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb110-57130_rabbit-polyclonal-trf-2-antibody-310202416235540.jpg)
![Western Blot: TRF-2 Antibody - BSA Free [NB110-57130] - Widespread dysregulation of shelterin protein expression in bortezomib-treated HEL & BGC-823 cellsA. & B. mRNA levels of shelterin factors TRF1, TRF2, TPP1, POT1, RAP1 & TIN2 in bortezomib-treated cells. Cells were treated with bortezomib for 24 hours & qPCR was used for quantitative assays. The levels of each target mRNA in bortezomib-treated cells were expressed as percentages of those in untreated cells. (A) HEL cells & (B) BGC-823 cells. C. & D. Immunoblotting assessment of TRF1, TRF2 & POT1 protein expression in bortezomib-treated cells. Same sets of cells above were analyzed for TRF1, TRF2 & POT1 protein levels & shown was representative of three independent experiments. (C) HEL cells & (D) BGC-823 cells. * & **: P < 0.05 & 0.01, respectively. BTZ, bortezomib. Image collected & cropped by CiteAb from the following publication (//www.oncotarget.com/lookup/doi/10.18632/oncotarget.5752), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb110-57130_rabbit-polyclonal-trf-2-antibody-31020241623553.jpg)
![Western Blot: TRF-2 Antibody - BSA Free [NB110-57130] - A. Co-IP analysis of the interaction between DSP & TRF2 in HEK293 cells & MCF-7 cells. B. Co-IP analysis of the interaction between DSP & TRF2 in DSP-EGFP transfected HEK293 cells or DSP△NLS-EGFP transfected HEK293 cells. C. DSP pull down by telomere targeting CASID with the condition of TRF2 knockdown in HEK293 cells. Histone H3 is the loading control. D.TRF1 & TRF2 pull-down assay by telomere targeting CASID with the condition of DSP knockdown in HEK293 cells. E. Left, Dot blot of telomere DNA repeats in chromatin pull down by DSP with the condition of TRF1 or TRF2 knockdown. The dot-blot was performed at least three times & the represented one is shown. Right, the histogram shows the quantitated results of the dot blots. The triple asterisks (***) indicates a p-value less than 0.01. ns. indicates the insignificance difference. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31595153), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb110-57130_rabbit-polyclonal-trf-2-antibody-31020241624919.jpg)
![Western Blot: TRF-2 Antibody - BSA Free [NB110-57130] - Telomere deprotection contributes to replication stress lethality. a Western blots of whole cell extracts from HT1080 6TG cells stably transduced with control, TRF2 shRNA (TRF sh-F) or TRF2 over expression (TRF2OE) vectors. b Representative images of cyto-centrifuged chromosome spreads stained with DAPI (blue), gamma -H2AX IF (red) & telomere PNA (green) from control, TRF sh-F or TRF2OE HT1080 6TG cells treated with DMSO or APH. Scale bar represents 10 µm. c, d Quantitation of mitotic telomere DDR foci from Control sh & TRF2 sh-F cells (c) or vector & TRF2OE cells (d) ± DMSO or APH (three biological replicates scoring n = 50 mitotic spreads per replicate compiled in a Tukey box plot, Mann–Whitney test). e Difference in the mean number of mitotic telomeric gamma -H2AX foci between HT1080 6TG TRF2 sh-F or TRF2OE cells & their appropriate vector control. These are a different representation of the same data shown in (c, d) (mean ± s.e.m., n = 3 three biological replications, Student’s t-test). f Mitotic duration to cell death in APH treated control, TRF2 sh-F & or TRF2OE cells (three biological replicates scoring ≥267 mitotic death events per condition are shown in a dot plot, mean ± s.e.m., Mann–Whitney test). g Mitotic outcome of control, TRF2 sh-F & TRF2OE cells treated with APH or DMSO (mean ± s.e.m., n = 3 biological replicates of at least 267 mitoses per condition, Fisher’s Exact Test). For all panels, *p < 0.05, **p < 0.01. Source data are provided as a Source Data file Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31530811), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb110-57130_rabbit-polyclonal-trf-2-antibody-310202416235510.jpg)
![Western Blot: TRF-2 Antibody - BSA Free [NB110-57130] - A. Co-IP analysis of the interaction between DSP & TRF2 in HEK293 cells & MCF-7 cells. B. Co-IP analysis of the interaction between DSP & TRF2 in DSP-EGFP transfected HEK293 cells or DSP△NLS-EGFP transfected HEK293 cells. C. DSP pull down by telomere targeting CASID with the condition of TRF2 knockdown in HEK293 cells. Histone H3 is the loading control. D.TRF1 & TRF2 pull-down assay by telomere targeting CASID with the condition of DSP knockdown in HEK293 cells. E. Left, Dot blot of telomere DNA repeats in chromatin pull down by DSP with the condition of TRF1 or TRF2 knockdown. The dot-blot was performed at least three times & the represented one is shown. Right, the histogram shows the quantitated results of the dot blots. The triple asterisks (***) indicates a p-value less than 0.01. ns. indicates the insignificance difference. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31595153), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb110-57130_rabbit-polyclonal-trf-2-antibody-31020241624913.jpg)
![Western Blot: TRF-2 Antibody - BSA Free [NB110-57130] - A. TRF2 or DSP1 pull down by telomere targeting CASID with the condition of MST-312 treatment (left) or hTERT knockdown (right) in MDA-MB-231cells. B. Southern blot of telomere DNA from MDA-MB-231cells treated with MST-312 or with hTERT knockdown. C. Top, Dot blot of telomere DNA repeats from the chromatin pull down by DSP from the cells treated by MST-312 (left) or hTERT knockdown (right). Alu DNA repeats serve as negative control. Bottom, the histogram shows the quantitated results of the dot blots. The triple asterisks (***) indicates a p-value less than 0.01. D. Fluorescence image of DSP-EGFP transfected MDA-MB-231 cells with the conditions of MST-312 treatment or hTERT knockdown. E. Pull down assay of DSP by CASID targeting telomere in WI38 cells with or without ectopically expression of hTERT gene. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31595153), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb110-57130_rabbit-polyclonal-trf-2-antibody-31020241624911.jpg)
![Western Blot: TRF-2 Antibody - BSA Free [NB110-57130] - Attenuation of bortezomib-induced shelterin protein dysregulation by hTERT over-expressionA. & B. Cells expressing ectopic hTERT were treated with bortezomib for 24 hours & mRNA levels of shelterin proteins then analyzed using qPCR. The levels of each target mRNA in bortezomib-treated cells were expressed as percentages of those in untreated cells. (A) HEL-hTERT cells & (B) BGC-823-hTERT cells. C. & D. Immunoblotting assessment of TRF1, TRF2 & POT1 protein expression in bortezomib-treated cells. Same sets of cells above were analyzed for TRF1, TRF2 & POT1 protein levels & shown was representative of three independent experiments. (C) HEL-hTERT cells & (D) BGC-823-hTERT cells.* & **: P < 0.05 & 0.01, respectively. BTZ, bortezomib. Image collected & cropped by CiteAb from the following publication (//www.oncotarget.com/lookup/doi/10.18632/oncotarget.5752), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb110-57130_rabbit-polyclonal-trf-2-antibody-310202416235549.jpg)
![Immunocytochemistry/ Immunofluorescence: TRF-2 Antibody - BSA Free [NB110-57130] - RNaseH1 depletion leads to RPA activation at ALT telomeres.(a) HeLa & U2OS cells were transfected with the indicated siRNAs & 48 & 72 h later protein extracts were prepared. Western blot analysis was performed using antibodies against RNaseH1, RPA32 phosphorylated at Serine 33 (pSer33), total RPA32 & KAP1 (loading control). The asterisk indicates a cross-reacting band. Cells treated for 6 h with 5 mM hydroxyurea (HU) were used as controls for pSer33 activation. (b) SiRNA transfected cells were subjected to indirect immunofluorescence using antibodies against TRF2 (to visualize telomeres; red) & pSer33 (green). DNA was counterstained with DAPI (blue). Arrows point to examples of pSer33 foci co-localizing with TRF2 (TIFs). Scale bar, 9 μm. Cells treated for 6 h with 5 mM HU were used as controls for pSer33 activation. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/25330849), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb110-57130_rabbit-polyclonal-trf-2-antibody-310202416235532.jpg)
![Western Blot: TRF-2 Antibody - BSA Free [NB110-57130] - TRF2 interacts with lamin A/C.(a) Pull down of endogenous TRF2 in IMR90s. The top panel shows a blot probed for endogenous lamin A/C, & the bottom panel shows a blot with the same samples probed for TRF2. (b) Pull down of endogenously expressed lamin A/C in IMR90s. The top panel shows a blot probed for endogenous TRF2, & the bottom panel shows a blot with the same samples probed for endogenous lamin A/C. (c) Pull down of endogenous lamin A/C in IMR90s exogenously expressing GFP, GFP-TRF2, GFP-TRF delta B delta M or GFP-TRF1. The top panel shows a blot probed for GFP, & the bottom panel shows the same blot probed for lamin A/C. (d) Pull down of endogenous TRF2 in IMR90s exogenously expressing GFP, GFP-LMNA or progerin (GFP-LMNA delta 50). The top panel shows a blot probed for GFP, & the bottom panel shows the same blot probed for TRF2. Asterisks denote IgG bands. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/25399868), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb110-57130_rabbit-polyclonal-trf-2-antibody-31020241624921.jpg)
![Western Blot: TRF-2 Antibody - BSA Free [NB110-57130] - Widespread dysregulation of shelterin protein expression in bortezomib-treated HEL & BGC-823 cellsA. & B. mRNA levels of shelterin factors TRF1, TRF2, TPP1, POT1, RAP1 & TIN2 in bortezomib-treated cells. Cells were treated with bortezomib for 24 hours & qPCR was used for quantitative assays. The levels of each target mRNA in bortezomib-treated cells were expressed as percentages of those in untreated cells. (A) HEL cells & (B) BGC-823 cells. C. & D. Immunoblotting assessment of TRF1, TRF2 & POT1 protein expression in bortezomib-treated cells. Same sets of cells above were analyzed for TRF1, TRF2 & POT1 protein levels & shown was representative of three independent experiments. (C) HEL cells & (D) BGC-823 cells. * & **: P < 0.05 & 0.01, respectively. BTZ, bortezomib. Image collected & cropped by CiteAb from the following publication (//www.oncotarget.com/lookup/doi/10.18632/oncotarget.5752), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb110-57130_rabbit-polyclonal-trf-2-antibody-310202416235531.jpg)
![Western Blot: TRF-2 Antibody - BSA Free [NB110-57130] - TRF2 interacts with lamin A/C.(a) Pull down of endogenous TRF2 in IMR90s. The top panel shows a blot probed for endogenous lamin A/C, & the bottom panel shows a blot with the same samples probed for TRF2. (b) Pull down of endogenously expressed lamin A/C in IMR90s. The top panel shows a blot probed for endogenous TRF2, & the bottom panel shows a blot with the same samples probed for endogenous lamin A/C. (c) Pull down of endogenous lamin A/C in IMR90s exogenously expressing GFP, GFP-TRF2, GFP-TRF delta B delta M or GFP-TRF1. The top panel shows a blot probed for GFP, & the bottom panel shows the same blot probed for lamin A/C. (d) Pull down of endogenous TRF2 in IMR90s exogenously expressing GFP, GFP-LMNA or progerin (GFP-LMNA delta 50). The top panel shows a blot probed for GFP, & the bottom panel shows the same blot probed for TRF2. Asterisks denote IgG bands. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/25399868), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb110-57130_rabbit-polyclonal-trf-2-antibody-3102024162490.jpg)
![Western Blot: TRF-2 Antibody - BSA Free [NB110-57130] - TRF2 transcriptionally regulates p21 expression through promoter occupancy. (A) Quantitative ChIP using TRF2 antibody gives enriched binding of TRF2 on p21 promoter in HT1080 & MDA-MB-231 cells, IgG was used as isotypic antibody control; normalized with 10% input (data represented as mean ± SEM, for three replicates). (B,C) TRF2 represses p21 promoter activity. In luciferase assay, si-RNA-mediated silencing or TRF2 over expression resulted in increased (B, *p value < 0.05, Student’s t-test; data represented as mean ± SEM of three replicates) or reduction (C, *p value < 0.05, Student’s t-test; data represented as mean ± SEM of three replicates) in p21 promoter activity in HT1080 & MDA-MB-231 cells, respectively; over expression of TRF2 devoid of DNA binding [deletion of basic (delB), myb (delM) & both basic/myb (delB-delM) domains] resulted in partial or complete rescue of p21 promoter activity in HT1080 & MDA-MB-231 cells (data represented as mean ± SEM, for three replicates) (C). (D,E) HT1080 cells over expressing TRF2 show reduced p21 protein expression, bar graph shows the densitometry analysis of three different immunoblot replicates (*p value < 0.05, Student’s t-test; data represented as mean ± SEM of three replicates). (E) (Full images are shown in Supplementary Figure S5); TRF2 silencing results in increase in p21 protein, bar graph shows the densitometry analysis of three different immunoblots (*p value < 0.05, Student’s t-test; data represented as mean ± SEM of three replicates) (F); & mRNA expression in HT1080 cells (*p value < 0.05, Student’s t-test; data represented as mean ± SEM of three replicates, GAPDH used as internal control for real-time PCR). Image collected & cropped by CiteAb from the following publication (//www.nature.com/articles/s41598-017-11177-1), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb110-57130_rabbit-polyclonal-trf-2-antibody-310202416235546.jpg)
![Western Blot: TRF-2 Antibody - BSA Free [NB110-57130] - TRF2 transcriptionally regulates p21 expression through promoter occupancy. (A) Quantitative ChIP using TRF2 antibody gives enriched binding of TRF2 on p21 promoter in HT1080 & MDA-MB-231 cells, IgG was used as isotypic antibody control; normalized with 10% input (data represented as mean ± SEM, for three replicates). (B,C) TRF2 represses p21 promoter activity. In luciferase assay, si-RNA-mediated silencing or TRF2 over expression resulted in increased (B, *p value < 0.05, Student’s t-test; data represented as mean ± SEM of three replicates) or reduction (C, *p value < 0.05, Student’s t-test; data represented as mean ± SEM of three replicates) in p21 promoter activity in HT1080 & MDA-MB-231 cells, respectively; over expression of TRF2 devoid of DNA binding [deletion of basic (delB), myb (delM) & both basic/myb (delB-delM) domains] resulted in partial or complete rescue of p21 promoter activity in HT1080 & MDA-MB-231 cells (data represented as mean ± SEM, for three replicates) (C). (D,E) HT1080 cells over expressing TRF2 show reduced p21 protein expression, bar graph shows the densitometry analysis of three different immunoblot replicates (*p value < 0.05, Student’s t-test; data represented as mean ± SEM of three replicates). (E) (Full images are shown in Supplementary Figure S5); TRF2 silencing results in increase in p21 protein, bar graph shows the densitometry analysis of three different immunoblots (*p value < 0.05, Student’s t-test; data represented as mean ± SEM of three replicates) (F); & mRNA expression in HT1080 cells (*p value < 0.05, Student’s t-test; data represented as mean ± SEM of three replicates, GAPDH used as internal control for real-time PCR). Image collected & cropped by CiteAb from the following publication (//www.nature.com/articles/s41598-017-11177-1), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb110-57130_rabbit-polyclonal-trf-2-antibody-31020241624927.jpg)
![Western Blot: TRF-2 Antibody - BSA Free [NB110-57130] - Attenuation of bortezomib-induced shelterin protein dysregulation by hTERT over-expressionA. & B. Cells expressing ectopic hTERT were treated with bortezomib for 24 hours & mRNA levels of shelterin proteins then analyzed using qPCR. The levels of each target mRNA in bortezomib-treated cells were expressed as percentages of those in untreated cells. (A) HEL-hTERT cells & (B) BGC-823-hTERT cells. C. & D. Immunoblotting assessment of TRF1, TRF2 & POT1 protein expression in bortezomib-treated cells. Same sets of cells above were analyzed for TRF1, TRF2 & POT1 protein levels & shown was representative of three independent experiments. (C) HEL-hTERT cells & (D) BGC-823-hTERT cells.* & **: P < 0.05 & 0.01, respectively. BTZ, bortezomib. Image collected & cropped by CiteAb from the following publication (//www.oncotarget.com/lookup/doi/10.18632/oncotarget.5752), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb110-57130_rabbit-polyclonal-trf-2-antibody-310202416235529.jpg)
![Simple Western: alpha Tubulin Antibody (DM1A) [NB100-690] - Simple Western lane view shows a specific band for alpha Tubulin in 1.0 mg/ml of HeLa lysate. This experiment was performed under reducing conditions using the 12-230 kDa separation system. Alpha tubulin molecular weight: 50 kDa.](http://images.novusbio.com/fullsize/alpha-Tubulin-Antibody-DM1A-Simple-Western-NB100-690-img0023.jpg "Simple Western: alpha Tubulin Antibody (DM1A) [NB100-690] - Simple Western lane view shows a specific band for alpha Tubulin in 1.0 mg/ml of HeLa lysate. This experiment was performed under reducing conditions using the 12-230 kDa separation system. Alpha tubulin molecular weight: 50 kDa.")
![Immunohistochemistry: alpha Tubulin Antibody (DM1A) [NB100-690] - Analysis of formalin fixed colon sections. Heat mediated antigen retrieval was performed using sodium citrate buffer for 20 min before incubating with primary antibody at a 0.5ug/ml dilution for 15 min at RT.](http://images.novusbio.com/fullsize/alpha-Tubulin-Antibody-DM1A-Immunohistochemistry-NB100-690-img0028.jpg)
![Immunohistochemistry: alpha Tubulin Antibody (DM1A) [NB100-690] - Analysis of colon tissue. Sections were formalin fixed and embedded with paraffin. Sodium citrate heat mediated antigen retrieval for 20 min. Incubated with primary antibody for 15 min at a 5 ug/ml concentration. Corner image is staining with secondary only.](http://images.novusbio.com/fullsize/alpha-Tubulin-Antibody-DM1A-Immunohistochemistry-NB100-690-img0029.jpg)
![Immunohistochemistry: alpha Tubulin Antibody (DM1A) [NB100-690] - Analysis of formalin fixed paraffin embedded heart sections. Used at a dilution of 1:500.](http://images.novusbio.com/fullsize/alpha-Tubulin-Antibody-DM1A-Immunohistochemistry-NB100-690-img0031.jpg)
![Western Blot: alpha Tubulin Antibody (DM1A) [NB100-690] - Analsis of alpha tubulin in 9 cell lysates. Lane 1. HeLa; Lane 2. JURKAT; Lane 3. COS7; Lane 4. NIH-3T3; Lane 5. PC-12; Lane 6. RAT2; Lane 7. CHO; Lane 8. MDBK; Lane 9. MDCK](http://images.novusbio.com/fullsize/alpha-Tubulin-Antibody-DM1A-Western-Blot-NB100-690-img0032.jpg)
![Flow Cytometry: alpha Tubulin Antibody (DM1A) [NB100-690] - Intracellular flow cytometric staining of 1 x 10^6 CHO (A) and HEK-293 (B) cells using alpha Tubulin antibody (dark blue). Isotype control shown in orange. An antibody concentration of 1 ug/1x10^6 cells was used.](http://images.novusbio.com/fullsize/alpha-Tubulin-Antibody-DM1A-Flow-Cytometry-NB100-690-img0016.jpg)
![Immunomicroscopy: alpha Tubulin Antibody (DM1A) [NB100-690] - Analysis of HeLa cells, green staining is alpha tubulin whereas red is DNA stained with propidium iodide.](http://images.novusbio.com/fullsize/alpha-Tubulin-Antibody-DM1A-Immunomicroscopy-NB100-690-img0037.jpg)
![Western Blot: alpha Tubulin Antibody (DM1A) [NB100-690] - GS treatment increases markers of beiging in 3T3-L1 adipocytes. GS treatment upregulates markers of beiging, including beta-3AR (C) proteins. Data presented as mean +/- SEM from n = 4 replicates per group. * p 0 for sensitive & <0 resistant. (D) Apoptotic H1299 (null p53), A549 (wild type p53), Bm7-shGFP (mutant p53), & Bm7-shTP53 (knock-down p53) cells treated with simvastatin were detected using flow cytometry, *P < 0.05 & **P < 0.01. (E) Apoptotic HCC827-shGFP (mutant p53) & HCC827-shTP53 (knock-down p53) cells treated with simvastatin & cisplatin were detected using flow cytometry, *P < 0.05 & **P < 0.01. (F) Western blots of indicated proteins involved in apoptosis & autophagy in both Bm7 & HCC827 cells with control (shGFP) & p53 knockdown (shTP53) treated with simvastatin is shown. MDM2, murine double minute 2; AKT, serine–threonine kinase; PARP, poly (ADP-ribose) polymerase; mTOR, mammalian target of rapamycin; WT, wild type. Full-length blots/gels are presented in Supplementary Fig. 1. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31892709), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-690_mouse-monoclonal-alpha-tubulin-antibody-dm1a-img-80196-310202415541925.jpg)
![Western Blot: alpha Tubulin Antibody (DM1A) - BSA Free [NB100-690] - Pre-treatment with 0.5 mM sodium arsenite (SA) enhances permissivity in a cell-type-specific manner across reovirus strains. (A) CV-1, HeLa, L929, or HPDE cells were left untreated (no SA) or were treated with 0.5 mM SA for 30 min prior to infection (Pre-SA). Following this, cells were infected with T3D such that ~20% to 50% of cells were infected & at 18 h p.i. cells were fixed & immunostained for μNS & DAPI to visualize viral factories (VFs). The percent of cells containing VFs was quantified ((# of cells containing VFs/total # of cells) × 100) from three independent experiments. The expression level of μNS (B) & μ1 (C) was determined in CV-1, L929, or HeLa cells either left untreated (no SA) or treated with 0.5 mM SA for 30 min (Pre-SA) before infection with T3D at MOI = 1. At 18 h p.i., cells were harvested & the expression level of the indicated proteins was determined by immunoblot. M = mock. Densitometry analysis of the band intensity for μNS & μ1 was adjusted to the matched alpha -tubulin loading control for two independent experiments. Columns represent mean ± SEM. (D) CV-1; (E) L929; or (F) HeLa cells were left untreated (no SA) or were treated with 0.5 mM SA prior to infection (Pre-SA). Cells were then infected with the reovirus strains, T3D, T1L, or T3A, as described in (A). At 18 h p.i., cells were fixed & immunostained for μNS & DAPI to detect VFs. The percent of cells containing VFs was quantified ((# of cells containing VFs/total # of cells) × 100) from at least two independent experiments. * p < 0.05; ** p < 0.01; two-tailed unpaired t test. The error bars indicate S.D. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31216693), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-690_mouse-monoclonal-alpha-tubulin-antibody-dm1a-img-80196-31020241553208.jpg)
![Western Blot: ERK1 Antibody (1E5) [NBP2-22203] - Western blot analysis of whole cell lysates from (1) MCF7 (2) NIH3T3 cell lines using ERK1 antibody (clone 1E5) at 1:1000 dilution. The signal was developed using HRP labeled goat-anti Mouse secondary antibody with ECL based detection.](http://images.novusbio.com/fullsize/ERK1-Antibody-1E5-Western-Blot-NBP2-22203-img0008.jpg "Western Blot: ERK1 Antibody (1E5) [NBP2-22203] - Western blot analysis of whole cell lysates from (1) MCF7 (2) NIH3T3 cell lines using ERK1 antibody (clone 1E5) at 1:1000 dilution. The signal was developed using HRP labeled goat-anti Mouse secondary antibody with ECL based detection.")
![Immunocytochemistry/Immunofluorescence: ERK1 Antibody (1E5) [NBP2-22203] - Analysis of NIH/3T3 cells using ERK1 mouse mAb (green). Blue: DRAQ5 fluorescent DNA dye. Red: Actin filaments have been labeled with Alexa Fluor-555 phalloidin.](http://images.novusbio.com/fullsize/ERK1-Antibody-1E5-Immunocytochemistry-Immunofluorescence-NBP2-22203-img0002.jpg)
![Immunohistochemistry-Paraffin: ERK1 Antibody (1E5) [NBP2-22203] - Immunohistochemical analysis of paraffin-embedded breast cancer tissues using ERK1 mouse mAb with DAB staining.](http://images.novusbio.com/fullsize/ERK1-Antibody-1E5-Immunohistochemistry-Paraffin-NBP2-22203-img0004.jpg)
![Flow Cytometry: ERK1 Antibody (1E5) [NBP2-22203] - Flow cytometric analysis of Hela cells using ERK1 mouse mAb (blue) and negative control (red).](http://images.novusbio.com/fullsize/ERK1-Antibody-1E5-Flow-Cytometry-NBP2-22203-img0001.jpg)
![Western Blot: ERK1 Antibody (1E5) [NBP2-22203] - Analysis using MAPK3 mAb against human ERK1 (AA: 9-143) recombinant protein. (Expected MW is 40.8 kDa)](http://images.novusbio.com/fullsize/ERK1-Antibody-1E5-Western-Blot-NBP2-22203-img0006.jpg)
![Western Blot: ERK1 Antibody (1E5) [NBP2-22203] - Western blot analysis using ERK1 mouse mAb against Hela (1), Jurkat (2), RAW264.7 (3), HEK293 (4), K562 (5), NIH/3T3 (6), Cos7 (7) and PC-12 (8) cell lysate.](http://images.novusbio.com/fullsize/ERK1-Antibody-1E5-Western-Blot-NBP2-22203-img0007.jpg)
![Immunohistochemistry-Paraffin: ERK1 Antibody (1E5) [NBP2-22203] - Analysis of paraffin-embedded bladder cancer tissues using ERK1 mouse mAb with DAB staining.](http://images.novusbio.com/fullsize/ERK1-Antibody-1E5-Immunohistochemistry-Paraffin-NBP2-22203-img0003.jpg)
![ELISA: ERK1 Antibody (1E5) [NBP2-22203] - Red: Control Antigen (100ng); Purple: Antigen (10ng); Green: Antigen (50ng); Blue: Antigen (100ng)](http://images.novusbio.com/fullsize/ERK1-Antibody-1E5-ELISA-NBP2-22203-img0005.jpg)
![Immunocytochemistry/Immunofluorescence: Ki67/MKI67 Antibody - BSA Free [NB110-89717] - 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- NB110-89717 at 2 ug/ml overnight at 4C and detected with an anti-rabbit Dylight 488 (Green) at a 1:1000 dilution for 60 minutes. Nuclei were counterstained with DAPI (Blue). Cells were imaged using a 100X objective and digitally deconvolved.](http://images.novusbio.com/fullsize/Ki67-MKI67-Antibody---BSA-Free-Immunocytochemistry-Immunofluorescence-NB110-89717-img0023.jpg "Immunocytochemistry/Immunofluorescence: Ki67/MKI67 Antibody - BSA Free [NB110-89717] - 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- NB110-89717 at 2 ug/ml overnight at 4C and detected with an anti-rabbit Dylight 488 (Green) at a 1:1000 dilution for 60 minutes. Nuclei were counterstained with DAPI (Blue). Cells were imaged using a 100X objective and digitally deconvolved.")
![Immunohistochemistry: Ki67/MKI67 Antibody - BSA Free [NB110-89717] - KLF4 ablation leads to abnormal proliferation and differentiation in small intestinal epithelium. Higher magnification IHC staining of highlighted frames. Small intestine from Klf4-/- mice induced by tamoxifen for different time endurances were stained by H&E and PAS, and also immunohistochemistry staining was performed with anti-Ki67, anti-Lysozyme, anti-DCAMKL-1, and anti-PCNA antibodies respectively. Bottom panel: IHC staining with ZO-1 antibody in one-month knockout intestine tissue. Image collected and cropped by CiteAb from the following publication (//dx.plos.org/10.1371/journal.pone.0032492) licensed under a CC-BY license.](http://images.novusbio.com/fullsize/Ki67-MKI67-Antibody---BSA-Free-Immunohistochemistry-NB110-89717-img0020.jpg)
![Flow Cytometry: Ki67/MKI67 Antibody - BSA Free [NB110-89717] - An intracellular stain was performed on HeLa cells with Ki-67/MKI67 antibody NB110-89717PE (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 Phycoerythrin.](http://images.novusbio.com/fullsize/Ki67-MKI67-Antibody---BSA-Free-Flow-Cytometry-NB110-89717-img0017.jpg)
![Immunocytochemistry/Immunofluorescence: Ki67/MKI67 Antibody - BSA Free [NB110-89717] - Immunofluorescences against MyHC (red) and Ki67/MKI67 (green) revealing differences in proliferation and differentiation in relation to different PrP concentration. alpha-MEM supplemented with: Ctrl (20% FBS), Low (5 x 10^5 platelets/ml), Medium (1 x 10^6 platelets/ml), and High (1.5 x 10^6 platelets/ml); nuclei were counterstained in blue by DAPI. Scale bars: MyHC = 200 um; Ki67 = 100 um. Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/33041857/) licensed under a CC-BY license.](http://images.novusbio.com/fullsize/Ki67-MKI67 Antibody - BSA Free-Immunocytochemistry-Immunofluorescence-NB110-89717-img0024.jpg)
![Immunocytochemistry/Immunofluorescence: Ki67/MKI67 Antibody - BSA Free [NB110-89717] - 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 anti-Ki-67/MKI67 at 2 ug/ml overnight at 4C and detected with an anti-rabbit DyLight 488 (green) at a 1:500 dilution. Nuclei were counterstained with DAPI (blue). Cells were imaged using a 40X objective.](http://images.novusbio.com/fullsize/Ki67-MKI67-Antibody---BSA-Free-Immunocytochemistry-Immunofluorescence-NB110-89717-img0015.jpg)
![Immunocytochemistry/Immunofluorescence: Ki67/MKI67 Antibody - BSA Free [NB110-89717] - A431 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-Ki67/MKI67 Antibody NB110-89717 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.](http://images.novusbio.com/fullsize/Ki67-MKI67-Antibody---BSA-Free-Immunocytochemistry-Immunofluorescence-NB110-89717-img0022.jpg)
![Immunohistochemistry-Paraffin: Ki67/MKI67 Antibody - BSA Free [NB110-89717] - Analysis of Ki-67 in paraffin embedded mouse prostate tissue using anti-Ki-67 antibody. Image from verified customer review.](http://images.novusbio.com/fullsize/Ki67-MKI67-Antibody---BSA-Free-Immunohistochemistry-Paraffin-NB110-89717-img0009.jpg)
![Immunohistochemistry: Ki67/MKI67 Antibody - BSA Free [NB110-89717] - Ki-67/MKI67 Antibody [NB110-89717] - Analysis of a mouse intestine cross section. The antibody was used at a dilution of 1:250. Detection: DAB staining. Epitope Retrieval Buffer-High pH was substituted for Epitope Retrieval Buffer-Reduced pH.](http://images.novusbio.com/fullsize/Ki67-MKI67-Antibody---BSA-Free-Immunohistochemistry-NB110-89717-img0010.jpg)
![Immunohistochemistry-Paraffin: Ki67/MKI67 Antibody - BSA Free [NB110-89717] - Staining of a cross section of mouse spleen. Detection: DAB staining using Immunohistochemistry Accessory Kit. Epitope Retrieval Buffer-High pH was substituted for Epitope Retrieval Buffer-Reduced pH.](http://images.novusbio.com/fullsize/Ki67-MKI67-Antibody---BSA-Free-Immunohistochemistry-Paraffin-NB110-89717-img0012.jpg)
![Immunohistochemistry: Ki67/MKI67 Antibody - BSA Free [NB110-89717] - Ki67 Antibody [NB110-89717] - FFPE section of mouse Peyer's patch. Antibody: Affinity purified rabbit anti-mouse Ki-67 used at a dilution of 1:250. Detection: DAB staining using Immunohistochemistry Accessory Kit. Epitope Retrieval Buffer-High pH was substituted for Epitope Retrieval Buffer-Reduced pH.](http://images.novusbio.com/fullsize/Ki67-MKI67-Antibody---BSA-Free-Immunohistochemistry-NB110-89717-img0014.jpg)
![Immunohistochemistry: Ki67/MKI67 Antibody - BSA Free [NB110-89717] - Ki-67/MKI67 Antibody [NB110-89717] - Detection of Ki67 in FFPE mouse intestine using NB110-89717.](http://images.novusbio.com/fullsize/Ki67-MKI67-Antibody---BSA-Free-Immunohistochemistry-NB110-89717-img0006.jpg)
![Immunohistochemistry-Paraffin: Ki67/MKI67 Antibody - BSA Free [NB110-89717] - Analysis of Ki-67 in human prostate xenograft control (left) and treated (right) using anti-Ki-67 antibody. Image from verified customer review.](http://images.novusbio.com/fullsize/Ki67-MKI67-Antibody---BSA-Free-Immunohistochemistry-Paraffin-NB110-89717-img0019.jpg)
![Flow Cytometry: Ki67/MKI67 Antibody - BSA Free [NB110-89717] - An intracellular stain was performed on U-937 cells with NB110-89717PE (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 Phycoerythrin.](http://images.novusbio.com/fullsize/Ki67-MKI67-Antibody---BSA-Free-Flow-Cytometry-NB110-89717-img0016.jpg)
![Flow Cytometry: Ki67/MKI67 Antibody - BSA Free [NB110-89717] - Ki-67/MKI67 Antibody [NB110-89717] - Staining of mouse bone marrow cells using NB110-89717 at a dilution of 1:100. Photo courtesy of product review by verified customer.](http://images.novusbio.com/fullsize/Ki67-MKI67-Antibody---BSA-Free-Flow-Cytometry-NB110-89717-img0004.jpg)
![<b>Genetic Strategies Validation. </b>Simple Western: Ki67/MKI67 Antibody - BSA Free [NB110-89717] - Detection of Ki67/MKI67 by Simple WesternTM. Simple Western lane view shows lysates of HeLa parental cell line and Ki67 knockout (KO) HeLa cell line. A specific band was detected for Ki67/MKI67 at approximately 312 kDa (as indicated) in the parental cell line, but is not detectable in the knockout HeLa cell line using 20 ug/mL of Rabbit Anti-Ki67/MKI67 Polyclonal Antibody (Catalog # NB110-89717). GAPDH is shown as a loading control. This experiment was conducted under reducing conditions and using the 12-230 kDa separation system.](http://images.novusbio.com/fullsize/Ki67-MKI67-Antibody---BSA-Free-Knockout-Validated-NB110-89717-img0021.jpg)
![Immunocytochemistry/ Immunofluorescence: Ki67/MKI67 Antibody - BSA Free [NB110-89717] - Long term Sonidegib treatment in mouse reduces taste buds (TB) & SHH ligand in circumvallate papilla (CV) whereas proliferation & innervation are retained. Immunofluorescent antibody detection of SHH ligand (red) & K8 (green) for TB cells; K8 (red) for TB cells & Ki67 (green) for cell proliferation; & K8 (red) with NF (green) for GL innervation or P2X3 (green) for GL taste fibers, after Vehicle or 48d Sonidegib treatment. For SHH/K8, large dotted lines indicate the basal lamina. Small dotted lines outline the surface epithelium. Inset (K8/P2X3) shows an image of nerves extending into CV epithelial basal lamina (arrow). Scale bar: 50 μm, applies to all images. Inset at 2×. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/30385780), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb110-89717_rabbit-polyclonal-ki67-mki67-antibody-310202415175296.jpg)
![Immunohistochemistry: Ki67/MKI67 Antibody - BSA Free [NB110-89717] - KLF4 ablation leads to abnormal proliferation & differentiation in small intestinal epithelium.(A) Small intestine from Klf4−/− mice induced by tamoxifen for different time endurances were stained by H&E & PAS, & also immunohistochemistry staining was performed with anti-Ki67, anti-Lysozyme, anti-DCAMKL-1, & anti-PCNA antibodies respectively. (B) Statistic analysis of IHC staining results from (A). (*, P<0.05) (C) IHC staining from (A) in higher magnification of highlighted frames. Bottom panel: IHC staining with ZO-1 antibody in one-month knockout intestine tissue. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/22384261), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb110-89717_rabbit-polyclonal-ki67-mki67-antibody-310202415394542.jpg)
![Immunohistochemistry: Ki67/MKI67 Antibody - BSA Free [NB110-89717] - KLF4 ablation leads to abnormal proliferation & differentiation in small intestinal epithelium.(A) Small intestine from Klf4−/− mice induced by tamoxifen for different time endurances were stained by H&E & PAS, & also immunohistochemistry staining was performed with anti-Ki67, anti-Lysozyme, anti-DCAMKL-1, & anti-PCNA antibodies respectively. (B) Statistic analysis of IHC staining results from (A). (*, P<0.05) (C) IHC staining from (A) in higher magnification of highlighted frames. Bottom panel: IHC staining with ZO-1 antibody in one-month knockout intestine tissue. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/22384261), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb110-89717_rabbit-polyclonal-ki67-mki67-antibody-310202415175256.jpg)
![Immunocytochemistry/ Immunofluorescence: Ki67/MKI67 Antibody - BSA Free [NB110-89717] - Culture conditions influence cell behavior. Immunofluorescences against MyHC (red) & Ki67 (green) reveal the remarkable differences in terms of differentiation & proliferation employing Cyto-Grow commercial medium compared with alpha -MEM (nuclei labeled in blue by DAPI). The respective quantifications are reported as fusion index & rate of proliferating nuclei (Ki67 positive). Statistical analysis: one-way ANOVA & Tukey’s test. **p < 0.01, ***p < 0.001 (n = 3). Scale bars: MyHC = 200 μm; Ki67 = 100 μm. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/33041857), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb110-89717_rabbit-polyclonal-ki67-mki67-antibody-310202415284548.jpg)
![Immunocytochemistry/ Immunofluorescence: Ki67/MKI67 Antibody - BSA Free [NB110-89717] - Paclitaxel in combination with MWE retarded tumor growth in a human bladder carcinoma TSGH 8301 xenograft model.(a) TSGH 8301 cells (1 × 107 cells/mouse) were injected into the right inguinal region of a nude mouse to form tumor xenografts. When the tumor size reached approximately 250 to 300 mm3, the mice were randomly divided into 4 groups & received the following treatments: paclitaxel combined with MWE, MWE alone, paclitaxel alone & sterile deionized water (control group). Tumor size was monitored every week, & the results are expressed as the percentage of the size at week 0 (the day treatment started) for each group. (b) The levels of total (t-PTEN) & phospho-PTEN (p-PTEN) & Caspase 3 in the tumor specimens were determined by Western blotting & then quantified using beta -actin as the protein loading control; the results are expressed as a percentage of the control. (c) Immunohistochemical examination of p-PTEN in the tumor sections obtained from the indicated treatment. (d) & (e) Fluorescent immunohistochemical detection of Ki67 & TUNEL examination in the xenografts obtained from the indicated treatment. (f ) Western blotting analysis of the levels of Cyclin B1, Cdc2 & Aurora A in xenograft tumors. Arrow indicates the Ki67 or TUNEL positive cells. One-way ANOVA with post-hoc Dunnett’s test was used to calculate the p value for each treatment compared to paclitaxel alone, (+p < 0.05;++p < 0.01) at each time point (**indicates p < 0.01 & *indicates p < 0.05). Image collected & cropped by CiteAb from the following publication (//www.nature.com/articles/srep20417), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb110-89717_rabbit-polyclonal-ki67-mki67-antibody-31020241621846.jpg)
![Immunocytochemistry/ Immunofluorescence: Ki67/MKI67 Antibody - BSA Free [NB110-89717] - Sonidegib treatment reduces taste buds (TB), SHH ligand & proliferation in rat fungiform papilla (FP) while innervation is retained. (a) Immunofluorescent antibody detection of SHH ligand (red) & K19 (green) for TB cells; K18 (red) for TB cells & Ki67 (green) for cell proliferation, after Vehicle, 16d or 28d Sonidegib treatments. SHH is reduced in association with TB, K19+ cell loss. Asterisks (*) indicate nonspecific SHH immunoproduct in cornified surface cells in 16d Sonidegib image. The Vehicle, K18/Ki67 image shows 3 regions positive for Ki67+ cells (Apical, Basal & Perigemmal). Proliferating cells are lost in Apical FP region after 16–28d Sonidegib. (b) Number of Ki67+ cells in Apical & Basal regions of FP in Vehicle- & Sonidegib-treated mice. Numbers of tongues analyzed are in parentheses. For each tongue 8–10 FP were analyzed. Sonidegib treatment reduces apical epithelial cell proliferation in FP compared to Vehicle. Statistical analysis was one-way ANOVA with Tukey HSD posthoc comparisons (*p ≤ 0.05, compared to Vehicle, APICAL). (c) Immunofluorescent antibody detection of K19 or K18 (red) for TB cells & NF (green) for lingual & CT innervation or P2X3 (green) for CT nerve fibers. Innervation was retained after Sonidegib exposure. Asterisks (*) indicate nonspecific P2X3 immunoproduct in surface layer in Vehicle image. (d) Enlarged images from 28d Sonidegib papillae. Arrows point to NF+ or P2X3+ fibers in the FP epithelium. Throughout, white dotted lines indicate the basal lamina. Yellow dotted lines indicate surface of epithelium. (a,c) Scale bar: 50 μm, applies to all images. (d) Scale bar: 25 μm, applies to both images. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/30385780), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb110-89717_rabbit-polyclonal-ki67-mki67-antibody-310202416205161.jpg)
![Immunocytochemistry/ Immunofluorescence: Ki67/MKI67 Antibody - BSA Free [NB110-89717] - SPIN1 controls proliferation & apoptosis of liposarcoma cell-derived tumors in BALB/c nude mice(A) Analysis of tumors from BALB/c nude mice (n = 15) 10 days after subcutaneous injection of T778 cells expressing control miRNA (miCtrl) or miRNA against SPIN1 [miSPIN1(1)]. Scale bar = 5 mm. (B) Average tumor weight of mice shown in (A) (C) Quantitative RT-PCR analysis of SPIN1, GDNF, & RET expression in T778 cell-derived tumors treated with the indicated miRNA. (D) Western blot analysis of SPIN1, RET, & RETph levels in T778 cell-derived tumors treated with the indicated miRNA. alpha -Tubulin & GFP were used as loading controls. (E) Detection of Ki67 by immunofluorescence in T778 cell-derived tumors treated with the indicated miRNA. Scale bar = 100 μm. (F) Quantification of Ki67 staining shown in (E). (G) TUNEL assay for detection of apoptotic cells in T778 cell-derived tumors treated with the indicated miRNA. Scale bar = 100 μm. (H) Quantification of TUNEL staining shown in (G) (B, C, F, H) Error bars represent +/– SEM, *p < 0.05, **p < 0.01. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/25749382), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb110-89717_rabbit-polyclonal-ki67-mki67-antibody-31020241620513.jpg)
![Immunocytochemistry/ Immunofluorescence: Ki67/MKI67 Antibody - BSA Free [NB110-89717] - Sonidegib treatment in rat reduces taste buds (TB) & SHH ligand in circumvallate papilla (CV) whereas cell proliferation & GL innervation are retained. Immunofluorescent antibody detection of SHH ligand (red) & K19 (green) for TB cells; K18 (red) for TB cells & Ki67 (green) for cell proliferation; K19 (red) for TB cells & NF (green) for innervation; and, K18 (red) for TB cells & P2X3 (green) for taste nerve fibers, after Vehicle or 36d Sonidegib treatment. White dotted lines outline the epithelium. Asterisk in SHH/K19, 36d Sonidegib indicates nonspecific K19 immunostaining. Arrow points to the P2X3+ nerves extending into CV epithelium after Sonidegib treatment. SHH is reduced in association with TB cells. Cell proliferation is maintained & nerves fibers are retained after Sonidegib treatment. Scale bar: 50μm, applies to all images, except K19/NF. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/30385780), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb110-89717_rabbit-polyclonal-ki67-mki67-antibody-31020241621233.jpg)
![Immunocytochemistry/ Immunofluorescence: Ki67/MKI67 Antibody - BSA Free [NB110-89717] - Overexpression of Chibby expression inhibits cell proliferation & invasion of HCC cells. (A) Adenovirus-mediated ectopic expression of Chibby & enhanced the expression of Chibby in Huh7 cells. After 48 h of infection with adenoviral vectors (Ad-GFP or Ad-Chibby) at different multiplicity of infection, the protein lysates from the Huh7 cells were harvested to determine the ectopic gene expression using Western blot analysis. Ad-GFP was designed as the control vector. (B) Representative immunofluorescent images of Ki67 in Huh7-normal control, Huh7-Ad-GFP, & Huh7-Ad-Chibby cells. (C,D) The enhancement of Chibby in Huh7 cells transfected with Ad-Chibby suppressed cell proliferation & invasiveness by colon-formation assay & the Boyden chamber system, respectively. Data represent mean ± SE from three independent analyses. Scale bar, 100 μm, * p < 0.05 & ** p < 0.01 vs. Ad-GFP group. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/32192213), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb110-89717_rabbit-polyclonal-ki67-mki67-antibody-310202416212380.jpg)
![Immunocytochemistry/ Immunofluorescence: Ki67/MKI67 Antibody - BSA Free [NB110-89717] - High doses of metformin inhibit the proliferation of C2C12 cells without inducing apoptosis.(a) C2C12 cells were treated with different doses of metformin in growth medium (GM) & the total number of cells was counted after 1, 2, 3 & 4 days of treatment by immunofluorescence microsopy. The initial number of plated cells was the same in each growth condition. Statistical significance was evaluated by the Student’s t-test (*p<0.05) (b) TUNEL assay. C2C12 cells were treated with 100μM, 2mM & 10mM metformin for 48h. As positive control for the TUNEL assay C2C12 myoblasts were incubated with DNΑse I before staining and, as negative control, cells were stained with the label solution without the addition of the reaction enzyme terminal deoxynucleotidyl transferase (TdT). (c) Total protein extracts of C2C12 myoblasts treated with 100μM, 2mM & 10mM were analyzed by SDS-PAGE for the expression of the apoptotic markers cl-caspase 3 & cl-caspase 7. For the induction of apoptosis in the positive control was used staurosporine 1μM for 4 hours. GAPDH is used as loading control (d) Proliferating C2C12 myoblasts, were plated at the same initial number (4*104 in GM in 9,5 cm2 area wells), incubated with 100μM, 2mM & 10mM metformin for 48h. The percentage of cells expressing Ki67 was measured by Cell Profiler cell image analysis software. Statistical significance was evaluated by the Student’s t-test (*p<0.05). Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/28859084), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb110-89717_rabbit-polyclonal-ki67-mki67-antibody-310202416212356.jpg)
![Immunocytochemistry/Immunofluorescence: Ki67/MKI67 Antibody (1297A) [NBP2-54791] - A431 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-Ki67/MKI67 Antibody (1297A) NBP2-54791 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.](http://images.novusbio.com/fullsize/Ki67-MKI67-Antibody-1297A-Immunocytochemistry-Immunofluorescence-NBP2-54791-img0007.jpg "Immunocytochemistry/Immunofluorescence: Ki67/MKI67 Antibody (1297A) [NBP2-54791] - A431 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-Ki67/MKI67 Antibody (1297A) NBP2-54791 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.")
![<b>Genetic Strategies Validation. </b>Knockout Validated: Ki67/MKI67 Antibody (1297A) [NBP2-54791] - Ki67/MKI67 was detected in immersion fixed HeLa human cervical epithelial carcinoma cell line but is not detected in Ki67/MKI67 knockout (KO) HeLa cell line using Rabbit Anti-Human Ki67/MKI67 Monoclonal Antibody (Catalog # NBP2-54791) at 1 ug/mL for 3 hours at room temperature. Cells were stained using the NorthernLights(TM) 557-conjugated Anti-Rabbit IgG Secondary Antibody (red; Catalog # NL004) and counterstained with DAPI (blue). Specific staining was localized to nuclei.](http://images.novusbio.com/fullsize/Ki67-MKI67-Antibody-1297A-Knockout-Validated-NBP2-54791-img0006.jpg)
![Immunocytochemistry/Immunofluorescence: Ki67/MKI67 Antibody (1297A) [NBP2-54791] - 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- NBP2-54791 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.](http://images.novusbio.com/fullsize/Ki67-MKI67-Antibody-1297A-Immunocytochemistry-Immunofluorescence-NBP2-54791-img0009.jpg)
![Immunocytochemistry/Immunofluorescence: Ki67/MKI67 Antibody (1297A) [NBP2-54791] - 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 Ki67/MKI67 Antibody [1297A] conjugated to Alexa Fluor 647 (NBP2-54791AF647) at 2 ug/ml for 1 hour at room temperature. Nuclei were counterstained with DAPI (Blue). Cells were imaged using a 40X objective.](http://images.novusbio.com/fullsize/Ki67-MKI67-Antibody-1297A-Immunocytochemistry-Immunofluorescence-NBP2-54791-img0010.jpg)
![Immunohistochemistry-Paraffin: Ki67/MKI67 Antibody (1297A) [NBP2-54791] - Ki-67/MKI67 was detected in immersion fixed paraffin-embedded sections of human liver cancer tissue using Rabbit Anti-Human Ki-67/MKI67 Monoclonal Antibody at 3 µg/mL for 1 hour at room temperature followed by incubation with the Anti-Rabbit IgG VisUCyte™ HRP Polymer Antibody. Tissue was stained using DAB (brown) and counterstained with hematoxylin (blue). Specific staining was localized to nuclei. Staining with VisUCyte HRP Polymer Detection Reagents.](http://images.novusbio.com/fullsize/Ki67-MKI67-Antibody-1297A-Immunohistochemistry-Paraffin-NBP2-54791-img0002.jpg)
![Flow (Intracellular): Ki67/MKI67 Antibody (1297A) [NBP2-54791] - Ki-67/MKI67 Antibody (1297A) [NBP2-54791] - An intracellular stain was performed on Jurkat Cells with Ki-67/MKI67 (1297A) antibody NBP2-54791 (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).](http://images.novusbio.com/fullsize/Ki67-MKI67-Antibody-1297A-Flow-Intracellular-NBP2-54791-img0004.jpg)
![Immunocytochemistry/Immunofluorescence: Ki67/MKI67 Antibody (1297A) [NBP2-54791] - 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-Ki67/MKI67 (1297A) at 2.0 ug/mL overnight at 4C and detected with an anti-rabbit Dylight 488 (Green) at a 1:500 dilution. Alpha tubulin (DM1A) NB100-690 was used as a co-stain at a 1:1000 dilution and detected with an anti-mouse Dylight 550 (Red) at a 1:500 dilution. Nuclei were counterstained with DAPI (Blue). Cells were imaged using a 40X objective.](http://images.novusbio.com/fullsize/Ki67-MKI67-Antibody-1297A-Immunocytochemistry-Immunofluorescence-NBP2-54791-img0003.jpg)
![Flow Cytometry: Ki67/MKI67 Antibody (1297A) [NBP2-54791] - An intracellular stain was performed on HeLa cells with Ki67/MKI67 Antibody [1297A] NBP2-54791APC (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 Allophycocyanin.](http://images.novusbio.com/fullsize/Ki67-MKI67-Antibody-1297A-Flow-Cytometry-NBP2-54791-img0005.jpg)
![Immunohistochemistry-Paraffin: Ki67/MKI67 Antibody (1297A) [NBP2-54791] - Ki67/MKI67 immunoreactivity in mouse small intestine. NBP2-54791 was diluted to 0.5ug/mL in Antibody Diluent and was left on sections for 1h at room temperature. Secondary was Horse Anti-Rabbit HRP. Image from verified customer review.](http://images.novusbio.com/fullsize/nbp2-54791_rabbit-monoclonal-ki67-mki67-antibody-1297a-1552023121119.jpg)
![Immunohistochemistry-Paraffin: Rabbit Monoclonal Ki67/MKI67 Antibody (1297A) [NBP2-54791] - Ki67 immunoreactivity in FFPE sections of human tonsil. NBP2-54791 was used at 500ng per mL and was left on tissue sections for 1hr at room temperature. Image from a verified customer review.](http://images.novusbio.com/fullsize/nbp2-54791_rabbit-monoclonal-ki67-mki67-antibody-1297a-immunohistochemistry-paraffin-15202512223..jpg)
![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.](http://images.novusbio.com/fullsize/ATM-Antibody-2C1-Western-Blot-NB100-309-img0018.jpg "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.](http://images.novusbio.com/fullsize/ATM-Antibody-2C1-Immunohistochemistry-Paraffin-NB100-309-img0021.jpg)
![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.](http://images.novusbio.com/fullsize/ATM-Antibody-2C1-Western-Blot-NB100-309-img0010.jpg)
![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.](http://images.novusbio.com/fullsize/ATM-Antibody-2C1-Immunohistochemistry-Paraffin-NB100-309-img0012.jpg)
![<b>Genetic Strategies Validation. </b>Western Blot: 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.](http://images.novusbio.com/fullsize/ATM-Antibody-2C1-Knockdown-Validated-NB100-309-img0017.jpg)
![<b>Genetic Strategies Validation. </b>Western Blot: 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.](http://images.novusbio.com/fullsize/ATM-Antibody-2C1-Western-Blot-NB100-309-img0019.jpg)
![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.](http://images.novusbio.com/fullsize/ATM-Antibody-2C1-Western-Blot-NB100-309-img0020.jpg)
![<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.](http://images.novusbio.com/fullsize/nb100-309_mouse-monoclonal-atm-antibody-2c1-25520231514910.jpg)
![Western Blot: ATM Antibody (2C1) [NB100-309] - Western blot analysis of the extent of knockdown MRE11 & ATM, & the lack of effect of Mirin activation of ATM. The extent of shRNA-mediated knockdown of MRE11 & ATM are shown for (A) clones GFP-7F1 & GFP-6D1 & (B) clones EDS-7F2 & EDS-6J8. The extent of knockdown was determined by analyzing the intensity of the ATM & 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 μM Mirin, or knockdown of ATM were analyzed by western blot 30 min after exposure to 10 Gy of ionizing radiation. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/26209132), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-309_mouse-monoclonal-atm-antibody-2c1-310202415371910.jpg)
![Western Blot: ATM Antibody (2C1) [NB100-309] - Rac1 inhibition abolishes IR-induced activation of both ATM & ATR signaling. (A) MCF-7 cells were treated with/without 20-Gy IR in the presence or absence of 100 μM NSC23766 & incubated for 1 hour at 37°C before analysis. To assess the ATM kinase activity, ATM was immunoprecipitated from cell lysate by using anti-ATM antibody (2C1) & assayed for ATM activity by using p53 recombinant protein as substrate. To measure the Chk2 activity, Chk2 was immunoprecipitated from cell lysate by using B-4 anti-Chk2 antibody & assayed for Chk2 activity by using Cdc25C recombinant protein as substrate. As controls, ATM & Chk2 protein levels in the immunoprecipitates (IP-WB) as well as in cell lysates (WB) were assessed with immunoblotting. (B) ATR & Chk1 were immunoprecipitated from cell lysates by using N-19 anti-ATR & G-4 anti-Chk1 antibody, respectively. ATR activity was assayed by using p53 recombinant protein substrate, & Chk1 activity assayed by using Cdc25C recombinant protein substrate. As controls, ATR & Chk1 protein levels in the immunoprecipitates (IP-WB), as well as in cell lysates (WB) were assessed with immunoblotting. (C) MCF-7 cells were exposed to IR at the indicated doses in the presence or absence of NSC23766, incubated for 1 hour, & assessed for Chk1 & Chk2 activities. *Kinase assay does not contain Cdc25C substrate. (D) T47D & ZR-75-1 cells were exposed to 10-Gy IR in the presence or absence of 100 μM NSC23766, incubated for 1 hour, & analyzed for Chk1 & Chk2 activities. Image collected & cropped by CiteAb from the following publication (//breast-cancer-research.biomedcentral.com/articles/10.1186/bcr3164), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-309_mouse-monoclonal-atm-antibody-2c1-310202415535119.jpg)
![Western Blot: ATM Antibody (2C1) [NB100-309] - Inhibition of Rac1 by N17Rac1 mutant or Rac1 siRNA diminishes IR-induced G2/M checkpoint activation. (A) MCF-7 cells were infected with Ad.N17Rac1 or Ad.Control for 24 hours & exposed to 15-Gy IR. Left panel: the cells were analyzed for DNA content 24 hours after IR. The result depicts the percentage of cells with 4N-DNA content & is shown as mean ± SD of quadruplicate samples. *P < 0.001 (n = 4), significant difference from the irradiated Ad.Control-infected cells. Right panel: Inset: at 15 minutes after IR, the infected cells were analyzed for Rac1 activities (Rac1-GTP) & protein levels (total Rac1). Bar graph: mitotic cells in the cell samples were analyzed 2 hours after IR. The result depicts the percentage of mitotic cells & is shown as mean ± SD of triplicate samples. **P = 0.002 (n = 3), significant difference from the irradiated Ad.Control-infected cells. (B) Upper panel: MCF-7 cells transfected with Rac1 siRNA (Rac1) or control siRNA (Control) were incubated for the indicated times & analyzed for protein levels of Rac1 & Actin. Lower panel: After 2-day incubation, the siRNA-transfected cells were exposed to IR, incubated for 24 hours, & assessed for DNA content. Results depict the percentage of cells with 4N-DNA content & represent the mean ± SD of three separate experiments in duplicate samples. *P < 0.001 (n = 6), significant difference from the irradiated Control-siRNA transfected cells. (C) After 2-day incubation, siRNA-transfected cells were treated with/without 20-Gy IR, incubated for 1 hour, & analyzed for ATM, ATR, Chk1, & Chk2 activities. Image collected & cropped by CiteAb from the following publication (//breast-cancer-research.biomedcentral.com/articles/10.1186/bcr3164), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-309_mouse-monoclonal-atm-antibody-2c1-310202415525285.jpg)
![Western Blot: ATM Antibody (2C1) [NB100-309] - HeLa whole cell extract and nuclear extracts (30 ug) were separated by 5% SDS-PAGE, and the membrane was blotted with ATM antibody [2C1] (NB100-309) diluted at 1:500. The HRP-conjugated anti-mouse IgG antibody was used to detect the primary antibody.](http://images.novusbio.com/fullsize/nb100-309_mouse-monoclonal-atm-antibody-2c1-91020242041241.jpg)
![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.](http://images.novusbio.com/fullsize/nb100-309_mouse-monoclonal-atm-antibody-2c1-91020242063311.jpg)
![Western Blot: ATM Antibody [NB100-104] - Detection of ATM in HeLa nuclear extract using ATM antibody [NB100-104]. Theoretical molecular weight 351 kDa.](http://images.novusbio.com/fullsize/ATM-Antibody-Western-Blot-NB100-104-img0009.jpg "Western Blot: ATM Antibody [NB100-104] - Detection of ATM in HeLa nuclear extract using ATM antibody [NB100-104]. Theoretical molecular weight 351 kDa.")
![Immunohistochemistry-Paraffin: ATM Antibody [NB100-104] - Staining of human tonsil, germinal center and mantle zone with ATM Antibody [NB100-104].](http://images.novusbio.com/fullsize/ATM-Antibody-Immunohistochemistry-Paraffin-NB100-104-img0014.jpg)
![<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.](http://images.novusbio.com/fullsize/ATM-Antibody-Immunocytochemistry-Immunofluorescence-NB100-104-img0018.jpg)
![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.](http://images.novusbio.com/fullsize/ATM-Antibody-Flow-Cytometry-NB100-104-img0016.jpg)
![<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.](http://images.novusbio.com/fullsize/ATM-Antibody-Western-Blot-NB100-104-img0017.jpg)
![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.](http://images.novusbio.com/fullsize/ATM-Antibody-Western-Blot-NB100-104-img0001.jpg)
![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.](http://images.novusbio.com/fullsize/ATM-Antibody-Immunocytochemistry-Immunofluorescence-NB100-104-img0011.jpg)
![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.](http://images.novusbio.com/fullsize/ATM-Antibody-Flow-Cytometry-NB100-104-img0012.jpg)
![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.](http://images.novusbio.com/fullsize/ATM-Antibody-Flow-Cytometry-NB100-104-img0015.jpg)
![Immunocytochemistry/ Immunofluorescence: ATM Antibody [NB100-104] - ATM is activated by spermidine in GM00637 cells.GM00637 cells with or without KU55933 pretreatment (a,b), & GM05849 cells (c) were exposed to 50 μM spermidine or CCCP, followed by immunofluorescence analyses of total & p-ATM on Ser-1981. The scale bar is 10 μm. Ratios of cells expressing p-ATM Ser-1981 to cells expressing total ATM were presented (d). 20–45 cells/condition from three experiments were collected. Values are mean ± SD, *p < 0.05 vs. control. Image collected & cropped by CiteAb from the following publication (//www.nature.com/articles/srep24700), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-104_rabbit-polyclonal-atm-antibody-31020241535641.jpg)
![Immunocytochemistry/ Immunofluorescence: ATM Antibody [NB100-104] - ATM is activated by spermidine in GM00637 cells.GM00637 cells with or without KU55933 pretreatment (a,b), & GM05849 cells (c) were exposed to 50 μM spermidine or CCCP, followed by immunofluorescence analyses of total & p-ATM on Ser-1981. The scale bar is 10 μm. Ratios of cells expressing p-ATM Ser-1981 to cells expressing total ATM were presented (d). 20–45 cells/condition from three experiments were collected. Values are mean ± SD, *p < 0.05 vs. control. Image collected & cropped by CiteAb from the following publication (//www.nature.com/articles/srep24700), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-104_rabbit-polyclonal-atm-antibody-310202415304298.jpg)
![Western Blot: ATM Antibody [NB100-104] - Depletion of SMARCAL1 induces DNA damage & checkpoint activation in iSML1 iPSCs. (A,B) The iSML1 iPSCs were cultured for 7 & 14 days in the presence of doxycycline (DOX) to induce SMARCAL1 downregulation & then immunostained. The graphs (top) show quantification of the number of gamma -H2AX-positive cells (A) or ATM-pSer1981-positive cells (B). Representative images from triplicate experiments are shown (bottom). (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 µm. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31515241), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-104_rabbit-polyclonal-atm-antibody-310202415371997.jpg)
![Western Blot: ATM Antibody [NB100-104] - Analysis of double strand break repair in MCF-7 monolayer & mammosphere populations. (a) Cells were exposed to 4 Gy 60Co gamma -radiation & the relative degree of double-strand breakage (DSB) was determined by the comet assay under neutral conditions immediately after exposure & at the times indicated after exposure. (b) The 'comets' (n of about 100) were categorized according to the NIH LISTSERV (Comet Assay Interest Group web site) in which type 1 comets display the least DNA damage & type 5 the most. The error bars represent the mean ± standard error of the mean in both panels. The comets of the unirradiated cells are labeled Cont. (c) 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 & from cells harvested one hour after exposure to 1 or 10-Gy 60Co gamma -radiation & analyzed by immunoblotting with antibodies against several DSB repair proteins. Phospho-ATM & phospho-DNA-PKcs refer to phosphorylation of these proteins at Ser1981 & Ser2056, respectively. Actin served as a loading control. Image collected & cropped by CiteAb from the following publication (//breast-cancer-research.biomedcentral.com/articles/10.1186/bcr2583), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-104_rabbit-polyclonal-atm-antibody-310202415535196.jpg)