| Formulation | Catalog # | Availability | Price | |
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| BSA Free | BC100-494SS | |||
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| BSA Free | NB100-104SS | |||
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| Azide and BSA Free | NBP2-27409 | |||
| BSA Free | NB100-56704SS | |||
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| BSA Free | NBP1-77299SS | |||
| Formulation | Catalog # | Availability | Price | |
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| BSA Free | NB100-56509SS | |||
| Azide and BSA Free | NBP2-80788 | |||
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| BSA Free | NBP1-49678SS | |||
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| BSA Free | NB100-493SS | |||
| Formulation | Catalog # | Availability | Price | |
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| BSA Free | NB100-56705SS | |||
| Azide and BSA Free | NBP2-33243 | |||
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| BSA Free | NB100-402SS | |||
![Western Blot: PINK1 Antibody - BSA Free [BC100-494] - PPM1H does not dephosphorylate Ser111 of Rab8A or key phosphorylation sites of AMPK & Akt signaling pathways.(A) HEK293 cells were transiently transfected with constructs expressing the indicated components. 24 hr post-transfection, cells were treated ±10 µM CCCP (Carbonyl cyanide m-chlorophenyl hydrazine) for 3 hr to induce activation of the PINK1 kinase & trigger Rab8A phosphorylation at Ser111 (Lai et al., 2015). (B) As in (A) except cells were immunoblotted with the indicated antibodies that recognize key phosphorylation sites of AMPK & Akt signaling pathways. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31663853), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/bc100-494_rabbit-polyclonal-pink1-antibody-31020241534312.jpg)
![Western Blot: PINK1 Antibody - BSA Free [BC100-494] - PINK1 & Parkin are phosphorylated after a decrease in delta Ψm in mouse primary neurons. Neurons were infected with lentivirus encoding PINK1-Flag (A), wild-type HA-Parkin (B) or HA-Parkin with either the S65A or S65E mutation (C). Cells were treated with the mitochondrial uncoupler CCCP (30 μm) for 1–3 h & subjected to SDS-PAGE in the absence or presence of 50 μm phos-tag. Note that mobility does not reflect the molecular weight of proteins in phos-tag PAGE (Kinoshita et al. 15), & thus, molecular weight markers are not shown in the bottom gels. The red & black asterisks in (C) indicate phosphorylation of Parkin at Ser65 & an additional minor phosphorylation site, respectively. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/23751051), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/bc100-494_rabbit-polyclonal-pink1-antibody-310202415384188.jpg)
![Western Blot: PINK1 Antibody - BSA Free [BC100-494] - PINK1 translation is critical for the accumulation of PINK1 upon mitochondrial damage. aPINK1 mRNA levels were not altered by mitochondrial damage. HeLa cells were incubated with 10 μM CCCP or combination of 10 μM oligomycin & 4 μM antimycin for 2 h & then, PINK1 mRNA levels were measured by qRT-PCR. PINK1 mRNA level was normalized to the corresponding GAPDH levels & quantified as a percentage of control (n = 8, t-test). b, c Translation is involved in PINK1 accumulation upon CCCP treatment. HeLa cells were first pre-incubated with 100 μM cycloheximide (CHX) for 2 h & then washed. Cells were further incubated with 10 μM CCCP with or without CHX for 2 h (n = 4, two-way ANOVA). Values are mean ± SEM (n.s. = non-significant, ***p 1000 cells) & are shown as a percentage of control. Values are mean ± SEM (*p < 0.05, **p < 0.01, ***p < 0.001) Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/27456084), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/bc100-494_rabbit-polyclonal-pink1-antibody-310202415483619.jpg)
![Western Blot: PINK1 Antibody - BSA Free [BC100-494] - Inhibition of endogenous miR-27a/b function increases human PINK1 expression. a Schematic diagram of sequence alignment of miR-27a/b & anti-miR-27a/b. Asterisks (*) indicate conserved nucleotides. b Inhibition of endogenous miR-27a/b function increased luciferase activities in HeLa cells. Cells were transfected with the reporter constructs containing the full-length 3′UTR of human PINK1 mRNA with wild-type (WT) or mutated (Mut) seed match sites downstream of Renilla luciferase gene. 48 h post-transfection, luciferase activities were measured (n = 4, t-test). c-f Inhibition of endogenous miR-27a/b increased PINK1 protein levels in HeLa (C-D) & M17 cells (E-F). Cells were transfected with 150 nM of anti-miR-27a/b or anti-control (anti-Ctl). 48 h post-transfection, cells were harvested for Western blot. PINK1 protein level was normalized to corresponding GAPDH level & quantified as a percentage of control (n = 4, t-test). Data are shown as a percentage of control. Values are mean ± SEM (n.s. = non-significant, **p < 0.01, ***p < 0.00) Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/27456084), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/bc100-494_rabbit-polyclonal-pink1-antibody-310202415482287.jpg)
![Western Blot: PINK1 Antibody - BSA Free [BC100-494] - Regulation of PINK1 by miRNA. a Schematic diagram of AGO-specific RNA immunoprecipitation assay. b, cPINK1 mRNAs are associated with miRNA/RISC complex. HeLa cells were transfected with 50 nM of AGO2 siRNA or negative control. 48 h post-transfection, AGO2-bound mRNAs were pulled down from cell lysates with 2A8 anti-AGO2 antibody or non-specific IgG antibody. PINK1 mRNA levels were then measured by qRT-PCR. siRNA against AGO2 served as a quality control for AGO-specific RNA immunoprecipitation assay. PINK1 mRNA levels were quantified as a percentage of group 1 (n = 6, two-way ANOVA). d, e Knock-down of DICER1 increased PINK1 protein levels. HeLa cells were transfected with 50 nM DICER1 siRNA (DICER1 KD) or negative control (Ctl). 48 h post-transfection, cells were harvested for Western blot. The arrowhead indicates a full-length PINK1 band & the asterisk indicates a non-specific band. Each protein level was normalized to corresponding GAPDH level & quantified as a percentage of control (n = 4, t-test). Values are mean ± SEM (n.s. = non-significant, **p < 0.01, ***p < 0.001) Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/27456084), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/bc100-494_rabbit-polyclonal-pink1-antibody-310202415482296.jpg)
![Western Blot: PINK1 Antibody - BSA Free [BC100-494] - The expression levels of microtubule protein light chain 3 (LC3B), PTEN inducing putative kinase 1 (PINK1), Parkin, mitofusin 1 (Mfn1), toll-like receptor (TLR) 9, cytochrome c oxidase 4 (COX4), myeloid differentiation factor 88 (MyD88), & nuclear factor (NF)-kappa B in lung tissues from animals with spontaneous breathing (CON) or mechanical ventilation at high tidal volume (HTV) with saline, antimycin A (AmA) or cyclosporine A (CsA). (A) Levels of PINK1, Parkin, & Mfn1 mRNA. (B) Levels of LC3B, PINK1, Parkin, & Mfn1 protein by Western blot. (C) Relative expression of LC3B-II/LC3B-I & PINK1 protein. (D) Relative expression of Parkin & Mfn1 protein. (E) Levels of TLR9 & COX4 mRNA. (F) Levels of MyD88 & nuclear factor-kappa B (NF-kappa B) mRNA. (G) Levels of TLR9, COX4, MyD88, & NF-kappa B protein by Western blot. (H) Relative expression of TLR9 & COX4 protein. (I) Relative expression of MyD88 & NF-kappa B protein. Fold expression for target genes was normalized to that measured for the beta -actin gene. Both of these experiments were in triplicate. aP < 0.05 vs. CON group;bP < 0.05 vs. HTV group; & cP < 0.05 vs. AmA group. Image collected & cropped by CiteAb from the following publication (//www.frontiersin.org/article/10.3389/fimmu.2018.01477/full), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/bc100-494_rabbit-polyclonal-pink1-antibody-310202415485118.jpg)
![Western Blot: PINK1 Antibody - BSA Free [BC100-494] - Mitophagy contributes to removal of excess mitochondrial fragments in preeclampsia.(a, left panel) Representative TEM image of a cytotrophoblast from PTC & PE placenta collected at 29 weeks. Mitochondrial proximity to ER (MAM) is indicated by white arrows, mitochondrial fission events are depicted by white stars (scale bar: 500 nm; n = 8 separate PE placentae). (a, right panel) percentage of mitochondrial tethering to the ER in in PE vs. PTC (PE placentae, n = 8; PTC placentae, n = 7; unpaired Student’s t-test *P < 0.05). b Representative western blots for MFN2 & calreticulin in ER isolated from PE & PTC placentae (PE & PTC, n = 3 separate samples). c WB & associated densitometry of ASAH2 (normalized to TOM20) in mitochondria from PTC & PE placentae. d Representative TEM depicting mitophagy (white arrow) in cytotrophoblast cell from PE placenta (scale bar: 500 nm, n = 8 separate PE placentae). e Western blot & associated densitometry of PINK1 & Parkin in PE vs. PTC mitochondrial isolates. Densitometry for PINK1 blot was used to calculate the ratio of full-length PINK63kDa to cleaved PINK153kDa (PE & PTC, n = 4 separate placentae, *P < 0.05) Image collected & cropped by CiteAb from the following publication (//www.nature.com/articles/s41419-018-0360-0), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/bc100-494_rabbit-polyclonal-pink1-antibody-310202415482279.jpg)
![Western Blot: PINK1 Antibody - BSA Free [BC100-494] - Deficiency or mutant PINK1 reduces phosphorylation of LETM1 at Thr192. a, b Proteins extracted from PINK1 WT or KO MEFs (a) or mouse brain (b) were subjected to IP with anti-LETM1, probed with pT192 & reprobed with anti-LETM1 by WB. c Proteins extracted from human fibroblast of control (Con) or a PINK1-Q456X patient (Q456X) were subjected to IP with anti-LETM1, probed with pT192 & reprobed with anti-LETM1 by WB. d HEK293 cells were transfected with Adtrack GFP control, AdPINK1-WT, & AdPINK1-Q456X mutant for 1 day. Endogenous LETM1 protein was isolated by IP with anti-LETM1, probed with pT192 & reprobed with anti-LETM1 by WB. e SH-SY5Y cells were treated with 25 µM rotenone for 8 or 16 h. Total cell lysates were either analyzed by WB with anti-PINK1, or subjected to IP with anti-LETM1, probed with pT192 & reprobed with anti-LETM1 antibodies by WB. All above experiments were replicated three times, respectively Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/29123128), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/bc100-494_rabbit-polyclonal-pink1-antibody-310202415482299.jpg)
![Western Blot: PINK1 Antibody - BSA Free [BC100-494] - Polyphyllin I suppressed, & PINK1 knockdown further suppressed, tumor growth in a MDA-MB-231 xenograft modelA. Tumor volumes were measured every week & differed at the end of the treatment period (*P < 0.01 compared to shCon cells treated with PPI, ##P< 0.01 compared to shPINK1 cells treated with PPI). B. Representative image of tumors from each group. C. Body weight changes in mice during the 6 weeks of PPI treatment. There were no differences in body weights between the PPI-treated shCon & vehicle-treated shCon groups or between the PPI-treated shPINK1 group & shCon groups. D. Representative tumor tissues were sectioned & subjected to H&E staining, TUNEL assay, & immunohistochemistry staining for C-CASP3. Scale bars: 50 μm. E. Representative tumor tissues from each group were prepared & subjected to western blot using anti-DRP1, -PARK2, -LC3B, -PINK1, & -C-CASP3 antibodies. Image collected & cropped by CiteAb from the following publication (//www.oncotarget.com/lookup/doi/10.18632/oncotarget.14413), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/bc100-494_rabbit-polyclonal-pink1-antibody-310202415483648.jpg)
![Western Blot: PINK1 Antibody - BSA Free [BC100-494] - Corticosterone affects NIX-dependent mitophagy through decreasing PGC1 alpha in vivo.a–f Mice exposed to vehicle, corticosterone (10 mg/kg), corticosterone w/ phorbol 12-myristate 13-acetate (PMA pretreatment, 200 μg/kg), or PMA alone for 7 days. a Slide samples for IHC immunostained w/ LAMP1 (green), TOMM20 (red), & DAPI (blue). Scale bars, 100 μm (magnification, ×200). n = 5. b The expressions of NIX, PTEN-induced kinase 1 (PINK1), & BCL2 interacting protein 3 (BNIP3) detected w/ WB where beta -actin used as a loading control. n = 5. c Slide samples for IHC immunostained w/ synpatophysin (green), PSD95 (red), & DAPI (blue). Scale bars, 100 μm (magnification, ×200). n = 5. d Synaptophysin & PSD95 detected by WB. Loading control is beta -actin. n = 5. e The mice subjected to Y-maze test to evaluate spatial memory function. n = 6. f The mice subjected to forced swim test to evaluate depression-like behavior. n = 5. g Vehicle or RU 486 (5 mg/kg) injected mice presented w//w/out corticosterone (10 mg/kg) for 3 days. The expressions of peroxisome proliferator-activated receptor gamma coactivator 1-alpha (PGC1 alpha ) & NIX visualized via WB. Loading control is beta -actin. n = 5. h The schematic model for mechanisms of inhibition in NIX-dependent mitophagy by glucocorticoid shown. All blots & IF images representative. n = 5 or 6 from each animal w/ two technical replicates each in results of IHC & WB. Quantitative data presented as a mean ± S.E.M. The representative images acquired by SRRF imaging system. Two-sided two-way ANOVA conducted except Fig. 8b, data of which analyzed by two-sided unpaired student’s t test. ** indicates p < 0.01 versus control & ## indicates p < 0.01 versus corticosterone, respectively. Data provided as a Source data file. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/33473105), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/bc100-494_rabbit-polyclonal-pink1-antibody-310202415482218.jpg)
![Western Blot: PINK1 Antibody - BSA Free [BC100-494] - G-TPP activity is conserved in primary fibroblasts(A, C) Fibroblasts were treated with 15 µM G-TPP for the indicated time points. Cells were harvested & western blots were probed with antibodies against (A) PINK1, pS65-Ub & total Ub or (C) autophagy adapter proteins. GAPDH & Vinculin served as loading control. G-TPP treatment led to PINK1 stabilization & pS65-Ub induction in primary skin fibroblasts. p62 levels were induced upon G-TPP treatment, while other adapters seemed decreased. (B, D) Human fibroblasts were treated with 15 µM G-TPP for 16 h & fixed & stained with antibodies against (B) pS65-Ub (green) or (D) the autophagy adapters NBR1, NDP52, p62, OPTN & TAX1BP1 (green). Mitochondria were stained with antibodies against TOM20 (red), nuclei were visualized with Hoechst (blue). Scale bars indicate 10 µM. A magnified image of the boxed region, the fluorescence profile along the arrow & the Pearson’s correlation coefficient of adapter protein & mitochondrial stainingare shown to the right. Shown is the mean ± SEM of at least five randomly selected images (unpaired, two-sided t-test, ***p < 0.0005). Image collected & cropped by CiteAb from the following publication (//www.oncotarget.com/lookup/doi/10.18632/oncotarget.22287), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/bc100-494_rabbit-polyclonal-pink1-antibody-310202415482286.jpg)
![Western Blot: PINK1 Antibody - BSA Free [BC100-494] - Polyphyllin I triggers PINK1/PARK2-dependent mitophagyA. MDA-MB-231 cells were treated with 8 μM PPI for different periods of time as indicated, & PARK2, P62, & ubiquitin (UB) levels in mitochondrial fractions were determined by western blot. B. Cells were cotransfected with GFP-UB & RFP-mito & treated with 8 μM PPI for 9 h, after which PARK2 (Alexa Fluor 405, pink) & P62 (Alexa Fluor 647, blue) immunostaining was detected using confocal microscopy. C. Cells cotransfected with GFP-UB & RFP-LC3 were treated with 8 μM PPI for 9 h, after which PARK2 (Alexa Fluor 405, pink) & TOMM20 (Alexa Fluor 647, blue) immunostaining was detected using confocal microscopy. Scale bars: 10 μm. D-E. MDA-MB-231 cells were treated with 8 μM PPI for different periods of time as indicated; whole-cell lysates were then separated on 8% SDS-PAGE gels & analyzed by western blot using the anti-PINK1 antibody. Relative full-length (∼63 kDa) & cleaved (∼52 kDa) PINK1 levels were quantified by densitometry & normalized to Tubulin. The results were expressed as a percentage of control, which was set at 100%. Data are presented as mean ± SD (*P< 0.01 vs. the control). F. Cells were treated with 8 μM PPI for different periods of time as indicated, & whole-cell lysates were then subjected to western blot analysis. G. Cells were treated with 8 μM PPI for 9 h, after which mitochondrial fractions were prepared & subjected to immunoprecipitation using anti-PINK1 antibody; associated PARK2 was detected using immunoblotting. H. RFP-mito-expressing MDA-MB-231 cells were treated with 8 μM PPI for 9 h, & PINK1 (Alexa Fluor 488, green) & PARK2 (Alexa Fluor 405, pink) immunostaining were evaluated using confocal microscopy. Scale bars: 10 μm. Image collected & cropped by CiteAb from the following publication (//www.oncotarget.com/lookup/doi/10.18632/oncotarget.14413), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/bc100-494_rabbit-polyclonal-pink1-antibody-310202415482214.jpg)
![Western Blot: PINK1 Antibody - BSA Free [BC100-494] - miR-27a/b suppress human PINK1 expression. a Schematic diagram of the conserved target sites of miR-27a/b in the 3′UTR of human PINK1 mRNA. Seed sequences were indicated in red. Asterisks (*) indicate the conserved nucleotides. b Schematic diagram of the luciferase reporter plasmids. The reporter constructs contain the full-length 3′UTR of human PINK1 mRNA with wild-type (WT) or mutated (Mut) seed match sites downstream of Renilla luciferase gene. c Overexpression of miR-27a/b decreased luciferase activities in HeLa cells. Cells were transfected with miR-27a/b or negative control (Ctl) along with reporter constructs as indicated. 48 h post-transfection, luciferase activities were measured (n = 4, one-way ANOVA). Renilla luciferase activity was normalized to the corresponding firefly luciferase activity. d-g Overexpression of miR-27a/b decreased PINK1 protein levels in HeLa (D-E) & M17 cells (F-G). Cells were transfected with miR-27a/b or negative control (Ctl). 48 h post-transfection, cells were harvested for Western blot (n = 4, t-test). PINK1 protein level was normalized to corresponding GAPDH level & quantified as a percentage of control. Data are shown as a percentage of control. Values are mean ± SEM (n.s. = non-significant, **p < 0.01, ***p < 0.001) Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/27456084), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/bc100-494_rabbit-polyclonal-pink1-antibody-310202415483618.jpg)
![Western Blot: PINK1 Antibody - BSA Free [BC100-494] - Increased p62 expression is prevented in PINK1 knock‐down cells. (a) SH‐SY5Y cells expressing scrambled shRNA or PINK1 shRNA (117‐2, 118‐3, & 118‐4) were treated with 10 μM carbonyl cyanide m‐chlorophenylhydrazone (CCCP) for 24 h & full‐length (FL) PINK1 protein levels measured by western blot. No accumulation of FL PINK1 was observed in 118‐3 & 118‐4 PINK1 shRNA clones. (b) SH‐SY5Y cells constitutively expressing scrambled (scram) or PINK1 shRNA (clone 118‐3) were treated with vehicle or 10 μM CCCP for 24 h & p62 protein expression measured by western blotting. **p < 0.05 versus scram CCCP; n = 9. (c) SH‐SY5Y cells were incubated in serum‐free culture media for up to 24 h to induce starvation‐mediated macroautophagy. p62 protein levels were measured by western blotting. *p < 0.05 versus 0 h; **p < 0.01 versus 0 h; n = 4. (d) SH‐SY5Y cells were transfected with scrambled (scram) or p62 siRNA for 72 h. For the last 24 h, cells were treated with vehicle (ethanol) or 10 μM CCCP. p62 protein expression was then measured by western blotting. p62 protein was significantly decreased in p62 siRNA cells under basal conditions & following CCCP treatment, when compared to scram cells. **p < 0.01 versus scram vehicle or scram CCCP; n = 3. (e) Mitochondrial content was measured in SH‐SY5Y cells treated with scram or p62 siRNA for 72 h by measuring citrate synthase (CS) activity. For the last 24 h, cells were treated with vehicle or 10 μM CCCP & data are expressed as % of vehicle. *p < 0.05 versus scram CCCP treatment; n = 5. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/26509433), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/bc100-494_rabbit-polyclonal-pink1-antibody-310202415482278.jpg)
![Western Blot: PINK1 Antibody - BSA Free [BC100-494] - NF kappa B upregulates human PINK1 gene expression. (A) NF kappa B increases the endogenous human PINK1 mRNA level. HEK293 cells were transfected with either the NF kappa B expression vector or empty vector pMTF. RT-PCRs were performed using either primers specific to the human PINK1 coding sequence or the human beta -actin coding sequence. (B) NF kappa B increases the endogenous human PINK1 protein levels. HEK293 cells transfected with NF kappa B were harvested 48 h after transfection for protein detection. Cell lysates were run on 10% glycine gel & images were collected by Licor. A significant increase of endogenous PINK1 was observed. (C) The endogenous human PINK1 protein level was dramatically increased by NF kappa B in SH-SY5Y cells. SH-SY5Y cells were transfected with NF kappa B p65 plasmids or the control vector pMTF & then harvested for protein detections. The human PINK1 protein & its proteolysis products ∆1-PINK1 (55kD) & ∆2-PINK1 (45kD) were all increased. beta -actin acted as the internal control. (D) LPS treatment facilitated PINK1 expression in SH-SY5Y cells. Cells were harvested after being treated for 16 h & then subjected to Western blot. The human beta -actin level was served as a control. Quantification was performed by Image J software. Values indicate means ± SEM. n = 3, *p <0.01 by Student’s t-test. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/25108683), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/bc100-494_rabbit-polyclonal-pink1-antibody-310202415485116.jpg)
![Western Blot: PINK1 Antibody - BSA Free [BC100-494] - G-TPP induces PINK1 stabilization & kinase activity in HeLa cells(A) G-TPP treatment leads to PINK1 stabilization & pS65-Ub induction in HeLa cells. HeLa cells stably expressing untagged Parkin were treated with 10 µM G-TPP for the indicated times. Western blots were prepared with cell lysates & probed with antibodies against PINK1 & pS65-Ub. GAPDH served as a loading control. (B) pS65-Ub is induced in G-TPP treated cells & co-localizes with EGFP-Parkin & mitochondria. HeLa cells stably expressing EGFP-Parkin (green) were treated with 10 µM G-TPP for the indicated times & fixed. Cells were stained with antibodies against pS65-Ub (red) & the mitochondrial marker TOM20 (cyan). Scale bars correspond to 10 µM. (C) Quantification of Parkin translocation using High Content Imaging. HeLa EGFP-Parkin cells were treated for 4 or 8 h with or without 10 µM G-TPP. CCCP treatment (10 µM for 2 h) was used as a positive control. Cells were fixed, counterstained with Hoechst dye to visualize nuclei, imaged & analyzed using the ratio of cytoplasmic to nuclear EGFP signal [21]. Data was normalized to positive (2 h 10 µM CCCP treatment) & negative (2 h DMSO) controls. G-TPP significantly induced Parkin re-localization to levels similar to or beyond 2 h CCCP treatment. Shown are the mean values of three independent experiments with triplicate wells each ± SEM (one-way ANOVA with Tukey’s posthoc, ***p < 0.0005). Image collected & cropped by CiteAb from the following publication (//www.oncotarget.com/lookup/doi/10.18632/oncotarget.22287), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/bc100-494_rabbit-polyclonal-pink1-antibody-31020241548369.jpg)
![Western Blot: PINK1 Antibody - BSA Free [BC100-494] - NF kappa B upregulates human PINK1 gene expression. (A) NF kappa B increases the endogenous human PINK1 mRNA level. HEK293 cells were transfected with either the NF kappa B expression vector or empty vector pMTF. RT-PCRs were performed using either primers specific to the human PINK1 coding sequence or the human beta -actin coding sequence. (B) NF kappa B increases the endogenous human PINK1 protein levels. HEK293 cells transfected with NF kappa B were harvested 48 h after transfection for protein detection. Cell lysates were run on 10% glycine gel & images were collected by Licor. A significant increase of endogenous PINK1 was observed. (C) The endogenous human PINK1 protein level was dramatically increased by NF kappa B in SH-SY5Y cells. SH-SY5Y cells were transfected with NF kappa B p65 plasmids or the control vector pMTF & then harvested for protein detections. The human PINK1 protein & its proteolysis products ∆1-PINK1 (55kD) & ∆2-PINK1 (45kD) were all increased. beta -actin acted as the internal control. (D) LPS treatment facilitated PINK1 expression in SH-SY5Y cells. Cells were harvested after being treated for 16 h & then subjected to Western blot. The human beta -actin level was served as a control. Quantification was performed by Image J software. Values indicate means ± SEM. n = 3, *p <0.01 by Student’s t-test. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/25108683), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/bc100-494_rabbit-polyclonal-pink1-antibody-310202415482277.jpg)
![Western Blot: PINK1 Antibody - BSA Free [BC100-494] - NF kappa B upregulates human PINK1 gene expression. (A) NF kappa B increases the endogenous human PINK1 mRNA level. HEK293 cells were transfected with either the NF kappa B expression vector or empty vector pMTF. RT-PCRs were performed using either primers specific to the human PINK1 coding sequence or the human beta -actin coding sequence. (B) NF kappa B increases the endogenous human PINK1 protein levels. HEK293 cells transfected with NF kappa B were harvested 48 h after transfection for protein detection. Cell lysates were run on 10% glycine gel & images were collected by Licor. A significant increase of endogenous PINK1 was observed. (C) The endogenous human PINK1 protein level was dramatically increased by NF kappa B in SH-SY5Y cells. SH-SY5Y cells were transfected with NF kappa B p65 plasmids or the control vector pMTF & then harvested for protein detections. The human PINK1 protein & its proteolysis products ∆1-PINK1 (55kD) & ∆2-PINK1 (45kD) were all increased. beta -actin acted as the internal control. (D) LPS treatment facilitated PINK1 expression in SH-SY5Y cells. Cells were harvested after being treated for 16 h & then subjected to Western blot. The human beta -actin level was served as a control. Quantification was performed by Image J software. Values indicate means ± SEM. n = 3, *p <0.01 by Student’s t-test. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/25108683), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/bc100-494_rabbit-polyclonal-pink1-antibody-31020241548363.jpg)
![Western Blot: PINK1 Antibody - BSA Free [BC100-494] - G-TPP leads to recruitment of autophagy adapters & degradation of mitochondria(A) HeLa cells stably expressing untagged Parkin were treated with 10 µM G-TPP for 8 h. Western blots were prepared from cell lysates & probed with antibodies against LC3, phospho-TBK1 (Ser172) & TBK1. GAPDH was used as a loading control. Upon 8 h the levels of LC3-I & LC3-II were both increased. At 8 h after treatment with G-TPP but not at 4 or 24 h, TBK1 was phosphorylated. (B) HeLa cells stably expressing EGFP-Parkin were treated with 10 µM G-TPP & fixed 8 h after treatment. Cells were stained with antibodies against the autophagy adapter proteins NBR1, NDP52, OPTN, p62, & TAX1BP1 (red). Mitochondria were counterstained with TOM20 antibodies (cyan), nuclei with Hoechst (blue). EGFP-Parkin epifluorescence is shown in green. Scale bar corresponds to 10 µM. (C) HeLa cells stably expressing EGFP-Parkin & the reporter protein mitoKeima were treated with 10 µM CCCP or G-TPP & imaged over time. The ratio of ‘neutral’ mitoKeima to ‘acidic’ mitoKeima was calculated as readout for mitophagy. Parkin translocation was monitored at the same time. Values for Parkin translocation & mitophagy were normalized to 12 h treatment with 10 µM CCCP as positive control & DMSO as negative control (two-way ANOVA with Tukey’s post-hoc test, **p < 0.005, ***p < 0.0005). Image collected & cropped by CiteAb from the following publication (//www.oncotarget.com/lookup/doi/10.18632/oncotarget.22287), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/bc100-494_rabbit-polyclonal-pink1-antibody-310202415482225.jpg)
![Western Blot: Rabbit Polyclonal PINK1 Antibody [BC100-494] - PINK1 detection in mouse and postmortem human cortex samples. 1:1000 dilution at 4 degrees overnight to detect endogenous PINK1 from mouse and postmortem human cortex samples (10 ug total protein). Image from a verified customer review.](http://images.novusbio.com/fullsize/antibody/bc100-494_rabbit-polyclonal-pink1-antibody-western-blot-231202510057..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)
![Immunohistochemistry-Paraffin: IKK alpha Antibody (14A231) - BSA Free [NB100-56704] - Analysis of human IKK alpha in tumors of the three groups B (C-IKK alpha), E (Control), H (N-IKK alpha). Specific staining of human IKK alpha-using the NB100-56704 antibody. Scale bar: 70um. Image collected and cropped by CiteAb from the following publication (//www.oncotarget.com/article/8792/text/) licensed under a CC-BY license.](http://images.novusbio.com/fullsize/IKK-alpha-Antibody-14A231-BSA-Free-Immunohistochemistry-Paraffin-NB100-56704-img0018.jpg "Immunohistochemistry-Paraffin: IKK alpha Antibody (14A231) - BSA Free [NB100-56704] - Analysis of human IKK alpha in tumors of the three groups B (C-IKK alpha), E (Control), H (N-IKK alpha). Specific staining of human IKK alpha-using the NB100-56704 antibody. Scale bar: 70um. Image collected and cropped by CiteAb from the following publication (//www.oncotarget.com/article/8792/text/) licensed under a CC-BY license.")
![Western Blot: IKK alpha Antibody (14A231) - BSA Free [NB100-56704] - Western blot showing the increased expression of IKK-alpha in transgenic mice. Image collected and cropped by CiteAb from the following publication (oncotarget.com/fulltext/8792), licensed under a CC-BY license.](http://images.novusbio.com/fullsize/IKK-alpha-Antibody-14A231-BSA-Free-Western-Blot-NB100-56704-img0021.jpg)
![Flow Cytometry: IKK alpha Antibody (14A231) - BSA Free [NB100-56704] - An intracellular stain was performed on Hek293 cells with IKK alpha Antibody (14A231) NB100-56704 (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, followed by Mouse IgG (H+L) Cross-Adsorbed Secondary Antibody, Dylight 550 (35503, Thermo Fisher).](http://images.novusbio.com/fullsize/IKK-alpha-Antibody-14A231-BSA-Free-Flow-Cytometry-NB100-56704-img0017.jpg)
![Western Blot: IKK alpha Antibody (14A231) - BSA Free [NB100-56704] - IKK alpha Antibody (14A231) [NB100-56704] - Total protein from various Human, Mouse and Rat cell lines were separated on a 12% gel by SDS-PAGE, transferred to PVDF membrane and blocked in 5% non-fat milk in TBST. The membrane was probed with 1.0 ug/mL anti-IKK-alpha in 1% non-fat milk in TBST and detected with an anti-mouse HRP secondary antibody using chemiluminescence.](http://images.novusbio.com/fullsize/IKK-alpha-Antibody-14A231-BSA-Free-Western-Blot-NB100-56704-img0010.jpg)
![Immunocytochemistry/Immunofluorescence: IKK alpha Antibody (14A231) - BSA Free [NB100-56704] - Antibody was tested in HeLa cells with Dylight 488 (green). Nuclei and alpha-tubulin were counterstained with DAPI (blue) and Dylight 550 (red). An antibody dilution of 1:10 was used. Image objective 40X.](http://images.novusbio.com/fullsize/IKK-alpha-Antibody-14A231-BSA-Free-Immunocytochemistry-Immunofluorescence-NB100-56704-img0008.jpg)
![Immunohistochemistry: IKK alpha Antibody (14A231) - BSA Free [NB100-56704] - B-I. Immunohistochemistry showing the expression of the transgenic protein in N-IKKa and C-IKKa tumors. Staining with NB100-56704 antibody is shown. (B, C) Representative images showing the expression of transgenic IKKa in tumors and adjacent skin of N-IKKa/TgAC mice (B), and C-IKKa/TgAC animals (C). (D, E) Detail showing the nuclear (D) or cytoplasmic (E) localization of the transgenic IKKa in tumors. (F, G) Similar levels of expression of the transgenic IKKa in different N-IKKa tumors. By contrast variable levels of expression of the transgene are observed between different C-IKKa tumors (H, I). t: tumor; s: non-tumoral skin. Scale bar: (B, C) 100um; (D, E) 80 um; (F-I) 200 um. Image collected and cropped by CiteAb from the following publication (//www.oncotarget.com/article/8792/text/) licensed under a CC-BY license.](http://images.novusbio.com/fullsize/IKK-alpha-Antibody-14A231-BSA-Free-Immunohistochemistry-NB100-56704-img0022.jpg)
![Western Blot: IKK alpha Antibody (14A231) - BSA Free [NB100-56704] - IKK alpha Antibody (14A231) [NB100-56704] - Analysis of IKK alpha in Daudi cell lysate using IKK alpha antibody at 1 ug/mL.](http://images.novusbio.com/fullsize/IKK-alpha-Antibody-14A231-BSA-Free-Western-Blot-NB100-56704-img0005.jpg)
![Immunocytochemistry/Immunofluorescence: IKK alpha Antibody (14A231) - BSA Free [NB100-56704] - A431 cells were fixed for 10 minutes using 10% formalin and then permeabilized for 5 minutes using 1X PBS + 0.05% Triton X-100. The cells were incubated with anti-IKK alpha Antibody (14A231) at 2 ug/mL overnight at 4C and detected with an anti-mouse DyLight 488 (Green) at a 1:500 dilution. Actin was detected with Phalloidin 568 (Red) at a 1:200 dilution. Nuclei were counterstained with DAPI (Blue). Cells were imaged using a 40X objective.](http://images.novusbio.com/fullsize/IKK-alpha-Antibody-14A231-BSA-Free-Immunocytochemistry-Immunofluorescence-NB100-56704-img0014.jpg)
![Immunocytochemistry/Immunofluorescence: IKK alpha Antibody (14A231) - BSA Free [NB100-56704] - HeLa cells were fixed for 10 minutes using 10% formalin and then permeabilized for 5 minutes using 1X PBS + 0.05% Triton X-100. The cells were incubated with anti-IKK alpha Antibody (14A231) at 2 ug/mL overnight at 4C and detected with an anti-mouse DyLight 488 (Green) at a 1:500 dilution. Actin was detected with Phalloidin 568 (Red) at a 1:200 dilution. Nuclei were counterstained with DAPI (Blue). Cells were imaged using a 40X objective.](http://images.novusbio.com/fullsize/IKK-alpha-Antibody-14A231-BSA-Free-Immunocytochemistry-Immunofluorescence-NB100-56704-img0015.jpg)
![Immunohistochemistry-Paraffin: IKK alpha Antibody (14A231) - BSA Free [NB100-56704] - Analysis of a FFPE tissue section of human kidney using 1:200 dilution of IKK alpha clone 14A231 antibody. The staining was developed using HRP labeled anti-rabbit secondary antibody and DAB reagent, and nuclei of cells were counter-stained with hematoxylin.](http://images.novusbio.com/fullsize/IKK-alpha-Antibody-14A231-BSA-Free-Immunohistochemistry-Paraffin-NB100-56704-img0016.jpg)
![Immunohistochemistry-Paraffin: IKK alpha Antibody (14A231) - BSA Free [NB100-56704] - Expression of the transgenic IKK alpha protein in skin of C-IKK alpha and N-IKK alpha mice. D-E. Expression of exogenous IKK alpha protein in back skin of 1-month-old mice. Immunostaining with the NB100-56704 anti-IKK alpha antibody is shown. Note the cytoplasmic expression of the transgene in the C-IKK alpha mice (D). By contrast, it is located in the nuclei of cells in the N-IKK alpha mice (E). In both types of transgenic mice the exogenous IKK alpha is expressed in basal keratinocytes (bk), in the outer root sheath of hair follicles (ORS) and in cells surrounding the sebaceous glands (sb). Scale bar: 60um. Image collected and cropped by CiteAb from the following publication (//www.oncotarget.com/article/8792/text/) licensed under a CC-BY license.](http://images.novusbio.com/fullsize/IKK-alpha-Antibody-14A231-BSA-Free-Immunohistochemistry-Paraffin-NB100-56704-img0020.jpg)
![Simple Western: IKK alpha Antibody (14A231) - BSA Free [NB100-56704] - IKK alpha Antibody (14A231) [NB100-56704] - Image shows a specific band for IKK alpha in 0.5 mg/mL of Daudi (left) and U937 (right) lysate. This exeriment was performed under reducing conditions using the 12-230 kDa separation system.](http://images.novusbio.com/fullsize/IKK-alpha-Antibody-14A231-BSA-Free-Simple-Western-NB100-56704-img0009.jpg)
![Western Blot: IKK alpha Antibody (14A231) - BSA Free [NB100-56704] - NEMO-Ub binding is essential for TNF alpha signaling, but not for IL-1 beta signaling.(a) Schematic illustration of NEMO deletions or point mutations. (b,c) Effects of NEMO C-terminal deletion mutants on TNF alpha & IL-1 beta signaling. NEMO−/Y MEFs were reconstituted with mock, NEMO WT or different C-terminal deletion constructs & stimulated with TNF alpha (b) or IL-1 beta (c). Effects on NF-kappa B signaling were investigated by determining I kappa B alpha phosphorylation & degradation in Western Blots as well as NF-kappa B-DNA binding by EMSA. (d,e) Effects of NEMO D311N on TNF alpha & IL-1 beta signaling. NEMO−/Y MEFs were reconstituted with mock, NEMO WT or NEMO D311N point mutant & stimulated with TNF alpha (d) or IL-1 beta (e). Analysis on NF-kappa B signaling were performed as in (b,c). Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/26740240), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-56704_mouse-monoclonal-ikk-alpha-antibody-14a231-bsa-free-310202415392529.jpg)
![Western Blot: IKK alpha Antibody (14A231) - BSA Free [NB100-56704] - Expression of the transgenic IKK alpha protein in skin of C-IKK alpha & N-IKK alpha miceA. Recombinant DNA constructs employed to generate both transgenic mice lines. For C-IKK alpha mice generation, the nuclear localization signal (NLS) was removed from the sequence of the human IKK alpha cDNA employed. In the construct used for generation of the N-IKK alpha mice an extra NLS signal was added. WT IKK alpha ; wild type IKK alpha . B. Western blot of total protein extracts showing IKK alpha expression in back skin of Control & C-and N-IKK alpha mice. Actin was used as a loading control. C. Representative example of the K5 staining in back skin section of Control mice. D-E. Expression of exogenous IKK alpha protein in back skin of 1-month-old mice. Immunostaining with the NB100-56704 anti-IKK alpha antibody is showed; similar results were obtained with the H00001147-M04 IKK alpha antibody (not shown). Note the cytoplasmic expression of the transgene in the C-IKK alpha mice (D). By contrast, it is located in the nuclei of cells in the N-IKK alpha mice (E). In both types of transgenic mice the exogenous IKK alpha is expressed in basal keratinocytes (bk), in the outer root sheath of hair follicles (ORS) & in cells surrounding the sebaceous glands (sb). F. Back skin section of Control mice. The NB100-56704 antibody used does not recognize the endogenous IKK alpha in immunohistochemical assays. G. Endogenous IKK alpha expression in control mice using the IKK alpha (sc-7182) antibody. Scale bar: (C) 70 μm; (D-G) 60 μm. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/27121058), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-56704_mouse-monoclonal-ikk-alpha-antibody-14a231-bsa-free-310202415523920.jpg)
![Immunohistochemistry-Paraffin: IKK alpha Antibody (14A231) - BSA Free [NB100-56704] - Expression of the transgenic IKK alpha protein in skin of C-IKK alpha & N-IKK alpha miceA. Recombinant DNA constructs employed to generate both transgenic mice lines. For C-IKK alpha mice generation, the nuclear localization signal (NLS) was removed from the sequence of the human IKK alpha cDNA employed. In the construct used for generation of the N-IKK alpha mice an extra NLS signal was added. WT IKK alpha ; wild type IKK alpha . B. Western blot of total protein extracts showing IKK alpha expression in back skin of Control & C-and N-IKK alpha mice. Actin was used as a loading control. C. Representative example of the K5 staining in back skin section of Control mice. D-E. Expression of exogenous IKK alpha protein in back skin of 1-month-old mice. Immunostaining with the NB100-56704 anti-IKK alpha antibody is showed; similar results were obtained with the H00001147-M04 IKK alpha antibody (not shown). Note the cytoplasmic expression of the transgene in the C-IKK alpha mice (D). By contrast, it is located in the nuclei of cells in the N-IKK alpha mice (E). In both types of transgenic mice the exogenous IKK alpha is expressed in basal keratinocytes (bk), in the outer root sheath of hair follicles (ORS) & in cells surrounding the sebaceous glands (sb). F. Back skin section of Control mice. The NB100-56704 antibody used does not recognize the endogenous IKK alpha in immunohistochemical assays. G. Endogenous IKK alpha expression in control mice using the IKK alpha (sc-7182) antibody. Scale bar: (C) 70 μm; (D-G) 60 μm. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/27121058), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-56704_mouse-monoclonal-ikk-alpha-antibody-14a231-bsa-free-3102024168399.jpg)
![Western Blot: RIPK3/RIP3 Antibody [NBP1-77299] - Analysis of RIP3 in HeLa cell lysate with RIPK3/RIP3 antibody [NBP1-77299] at (A) 1 and (B) 2 ug/mL. Observed molecular weight ~60 kDa. Theoretical molecular weight 53 kDa.](http://images.novusbio.com/fullsize/RIPK3-RIP3-Antibody-Western-Blot-NBP1-77299-img0014.jpg "Western Blot: RIPK3/RIP3 Antibody [NBP1-77299] - Analysis of RIP3 in HeLa cell lysate with RIPK3/RIP3 antibody [NBP1-77299] at (A) 1 and (B) 2 ug/mL. Observed molecular weight ~60 kDa. Theoretical molecular weight 53 kDa.")
![Western Blot: RIPK3/RIP3 Antibody [NBP1-77299] - Mouse Cell lines. 15 ug of lysates per lane. Antibodies: [NBP1-77299], (0.5 ug/mL), 1h incubation at RT in 5% NFDM/TBST. Secondary: Goat anti-rabbit IgG HRP conjugate at 1:10000 dilution. Observed molecular weight ~50 kDa. Theoretical molecular weight 53 kDa.](http://images.novusbio.com/fullsize/RIPK3-RIP3-Antibody-Western-Blot-NBP1-77299-img0022.jpg)
![Western Blot: RIPK3/RIP3 Antibody [NBP1-77299] - Analysis using RIPK3/RIP3 antibody [NBP1-77299]. L929 cell line (mouse). 20 ug whole cell lysate. Primary antibody: 1:2000. Secondary antibody: 1:20000. Western blot image submitted by a verified customer review. Observed molecular weight ~57 kDa. Theoretical molecular weight 53 kDa.](http://images.novusbio.com/fullsize/RIPK3-RIP3-Antibody-Western-Blot-NBP1-77299-img0024.jpg)
![Western Blot: RIPK3/RIP3 Antibody [NBP1-77299] - C2C12 Cells. 15 ug of lysates per lane. Antibodies: RIPK3/RIP3 antibody [NBP1-77299], 1h incubation at RT in 5% NFDM/TBST. Secondary: Goat anti-rabbit IgG HRP conjugate at 1:10000 dilution. Lane 1: NBP1-77299, 0.1 ug/mL in the presence of peptide blocking. Lane 2: NBP1-77299, 0.1 ug/mL Lane 3: NBP1-77299, 0.2 ug/mL Lane 4: NBP1-77299, 0.5 ug/mL. Observed molecular weight ~55 kDa. Theoretical molecular weight 53 kDa.](http://images.novusbio.com/fullsize/RIPK3-RIP3-Antibody-Western-Blot-NBP1-77299-img0021.jpg)
![<b>Genetic Strategies Validation. </b>Western Blot: RIPK3/RIP3 Antibody [NBP1-77299] - Bone-marrow-derived macrophages exhibit significant reduction in RIPK3/RIP3 levels in RIPK3/RIP3deltaGlobal, RIPK3/RIP3deltaMphi-Cre and RIPK3/RIP3deltaEC-Cre mice. Protein lysates were immunoblotted to identify CD11b, RIPK3/RIP3 and beta-actin (loading control). Image collected and cropped by CiteAb from the following publication (www.dmm.biologists.org/lookup/doi/10.1242/dmm.041962) licensed under a CC-BY license.](http://images.novusbio.com/fullsize/RIPK3-RIP3-Antibody-Knockout-Validated-NBP1-77299-img0025.jpg)
![<b>Genetic Strategies Validation. </b>Knockdown Validated: RIPK3/RIP3 Antibody [NBP1-77299] - RIPK3/RIP3-deficiency impacts MCP-1 and IL-1beta expression in BMDMs and MCP-1 and E-Selectin/CD62E expression in cultured endothelial cells. Protein lysates were immunoblotted for RIPK3/RIP3 and the loading control, GAPDH (n=4 independent experiments). Image collected and cropped by CiteAb from the following publication (www.dmm.biologists.org/content/13/1/dmm041962) licensed under a CC-BY license.](http://images.novusbio.com/fullsize/RIPK3-RIP3-Antibody-Knockdown-Validated-NBP1-77299-img0026.jpg)
![Western Blot: RIPK3/RIP3 Antibody - BSA Free [NBP1-77299] - Bone-marrow-derived macrophages exhibit significant reduction in RIPK3 levels in Ripk3 delta Global, Ripk3 delta MΦ-Cre & Ripk3 delta EC-Cre mice. (A,B) BMDMs were isolated, differentiated on chamber slides for 7 days, immunostained for macrophage markers CD68 (red; A) & CD11b (pink; B), & co-stained for nuclei (Hoechst; blue). All cells from seven separate BMDM isolations were positive for these markers (n=7). (C) A phagocytosis assay was performed on BMDMs with fluorescent polystyrene beads. Phagocytic cells display TRITC+/Hoechst+ signal, & 85% of cells from two separate BMDM isolations were double positive (n=2). (D-F) Protein or RNA was collected from control, Ripk3 delta Global, Ripk3 delta MΦ-Cre & Ripk3 delta EC-Cre BMDMs. RNA was converted to cDNA & analyzed by qPCR for Ripk3 levels (D). Protein lysates were immunoblotted to identify CD11b, RIPK3 & beta -actin (loading control) (E) & quantified (F). (G) RNA from control & Ripk3 delta Global BMDMs was converted to cDNA & analyzed by qPCR for Ripk3-Exon 10 levels. For panels D,F,G, each dot represents a BMDM isolation from an individual animal. Statistics for panels D & F were calculated using one-way ANOVA with Dunnett's multiple comparisons test. Overall ANOVA P-values (prior to the post hoc tests) are 0.0002 (D) & <0.0001 (F). Statistics for panel G were calculated using an unpaired t-test with Welch's correction. *P<0.05, **P<0.01, ***P<0.001, ****P<0.0001. Data are mean±s.d. Scale bars: 25 µm. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31953345), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nbp1-77299_rabbit-polyclonal-ripk3-rip3-antibody-310202416171485.jpg)
![Western Blot: RIPK3/RIP3 Antibody - BSA Free [NBP1-77299] - p-MLKL levels are nearly undetectable in advanced plaques. (A-C) After 3 months on a Western diet, protein was collected from control (n=7), Ripk3 delta MΦ-Cre (n=5), Ripk3 delta EC-Cre (n=3) & Ripk3 delta SMC-Cre (n=3) aortas. Protein lysates were immunoblotted to identify p-MLKL (Abcam; #ab196436), MLKL & beta -actin (loading control) (A) & quantified (B,C). A faint positive p-MLKL signal can be seen in the representative blot in the control arch region; however, we could only detect p-MLKL in two out of the 18 aortas analyzed (B). Note that the same transfer membrane used for detecting CD11b (in Fig. 4S) was reprobed for p-MLKL & MLKL in A; the beta -actin control blots are therefore the same in both figures. (D,E) Protein lysates were immunoblotted to identify RIPK3 & GAPDH (loading control) (D) & quantified (E). For panels B,C,E, each dot represents an individual animal. Statistics were calculated using two-way ANOVA. Overall ANOVA P-values are 0.76 (B), 0.07 (C) & 0.46 (E). Data are mean±s.d. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31953345), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nbp1-77299_rabbit-polyclonal-ripk3-rip3-antibody-31020241616072.jpg)
![Immunocytochemistry/ Immunofluorescence: RIPK3/RIP3 Antibody - BSA Free [NBP1-77299] - Validation of RIPK3/RIP3 in Rat Kidney Tissue. Immunofluorescent analysis of 4% paraformaldehyde-fixed Rat Kidney tissue labeling RIPK3/RIP3 with at 20 ug/mL, followed by goat anti-rabbit IgG secondary antibody at 1/500 dilution (red).](http://images.novusbio.com/fullsize/nbp1-77299_rabbit-polyclonal-ripk3-rip3-antibody-2711202419562182.jpg)
![Immunohistochemistry: RIPK3/RIP3 Antibody - BSA Free [NBP1-77299] - Validation of RIPK3/RIP3 in Mouse Kidney Tissue. Immunohistochemical analysis of paraffin-embedded mouse kidney tissue using anti-RIPK3/RIP3 antibody at 2.5 ug/ml. Tissue was fixed with formaldehyde and blocked with 10% serum for 1 h at RT; antigen retrieval was by heat mediation with a citrate buffer (pH6). Samples were incubated with primary antibody overnight at 4C. A goat anti-rabbit IgG H&L (HRP) at 1/250 was used as secondary. Counter stained with Hematoxylin.](http://images.novusbio.com/fullsize/nbp1-77299_rabbit-polyclonal-ripk3-rip3-antibody-2711202419333448.gif)
![Immunohistochemistry: RIPK3/RIP3 Antibody - BSA Free [NBP1-77299] - Validation of RIPK3/RIP3 in Rat Kidney Tissue.Immunohistochemical analysis of paraffin-embedded rat kidney tissue using anti-RIPK3/RIP3 antibody at 5 ug/ml. Tissue was fixed with formaldehyde and blocked with 10% serum for 1 h at RT; antigen retrieval was by heat mediation with a citrate buffer (pH6). Samples were incubated with primary antibody overnight at 4C. A goat anti-rabbit IgG H&L (HRP) at 1/250 was used as secondary. Counter stained with Hematoxylin.](http://images.novusbio.com/fullsize/nbp1-77299_rabbit-polyclonal-ripk3-rip3-antibody-271120242074698.jpg)
![Western Blot: RIPK3/RIP3 Antibody - BSA Free [NBP1-77299] - Validation in Human Cell Lines. Loading: 15 ug of lysates per lane.Antibodies: RIPK3/RIP3 , (0.5 ug/mL), 1h incubation at RT in 5% NFDM/TBST.Secondary: Goat anti-rabbit IgG HRP conjugate at 1:10000 dilution.](http://images.novusbio.com/fullsize/nbp1-77299_rabbit-polyclonal-ripk3-rip3-antibody-2711202420243399.gif)
![Western Blot: IKK beta Antibody (10AG2) [NB100-56509] - Representative western blot of IKKB (E) in monocytes with quantification on the right. All data are representative of 5 separate experiments. Unpaired student t-test. ***p < 0.001. Image collected and cropped by CiteAb from the following publication (doi.org/10.3389/fimmu.2020.01478) licensed under a CC-BY license.](http://images.novusbio.com/fullsize/IKK-beta-Antibody-10AG2-Western-Blot-NB100-56509-img0015.jpg "<b>Biological Strategies Validation. </b>Western Blot: IKK beta Antibody (10AG2) [NB100-56509] - Representative western blot of IKKB (E) in monocytes with quantification on the right. All data are representative of 5 separate experiments. Unpaired student t-test. ***p < 0.001. Image collected and cropped by CiteAb from the following publication (doi.org/10.3389/fimmu.2020.01478) licensed under a CC-BY license.")
![<b>Biological Strategies Validation. </b>Immunocytochemistry/Immunofluorescence: IKK beta Antibody (10AG2) [NB100-56509] - Analysis of IKK beta Antibody in HeLa cells. Antibody dilution 5 ug/ml. Image from verified customer review.](http://images.novusbio.com/fullsize/IKK-beta-Antibody-10AG2-Immunocytochemistry-Immunofluorescence-NB100-56509-img0016.jpg)
![Immunohistochemistry-Paraffin: IKK beta Antibody (10AG2) [NB100-56509] - Analysis of a FFPE tissue section of human placenta using 1:200 dilution of IKK beta clone 10AG2 antibody. The staining was developed using HRP labeled anti-rabbit secondary antibody and DAB reagent, and nuclei of cells were counter-stained with hematoxylin.](http://images.novusbio.com/fullsize/IKK-beta-Antibody-10AG2-Immunohistochemistry-Paraffin-NB100-56509-img0014.jpg)
![Flow Cytometry: IKK beta Antibody (10AG2) [NB100-56509] - Analysis of PE conjugate of NB100-56509. An intracellular stain was performed on Jurkat cells with IKK Beta antibody (10AG2) NB100-56509PE (blue) and a matched isotype control NBP2-27287AF488 (orange). Cells were fixed with 4% PFA and then permeablized wi](http://images.novusbio.com/fullsize/IKK-beta-Antibody-10AG2-Flow-Cytometry-NB100-56509-img0012.jpg)
![Western Blot: IKK beta Antibody (10AG2) [NB100-56509] - Analysis of A) human Daudi, B) HeLa, and C) mouse NIH3T3 lysate probed with IKKbeta antibody at 2 ug/ml.](http://images.novusbio.com/fullsize/IKK-beta-Antibody-10AG2-Western-Blot-NB100-56509-img0007.jpg)
![Immunocytochemistry/Immunofluorescence: IKK beta Antibody (10AG2) [NB100-56509] - U-87 cells were fixed for 10 minutes using 10% formalin and then permeabilized for 5 minutes using 1X PBS + 0.5% Triton-X100. The cells were incubated with anti-IKK beta Antibody (10AG2) at 2 ug/ml overnight at 4C and detected with an anti-mouse Dylight 488 (Green) at a 1:500 dilution. Actin was detected with Phalloidin 568 (Red) at a 1:500 dilution. Nuclei were counterstained with DAPI (Blue). Cells were imaged using a 40X objective.](http://images.novusbio.com/fullsize/IKK-beta-Antibody-10AG2-Immunocytochemistry-Immunofluorescence-NB100-56509-img0013.jpg)
![Flow Cytometry: IKK beta Antibody (10AG2) [NB100-56509] - Analysis using the Alexa Fluor (R) 488 conjugate of NB100-56509. Staining of IKKbeta in HEK 293 cells using 0.1 ug of Alexa Fluor 488-conjugated antibody. Green histogram represents the isotype control , red represents the IKKbeta antibody.](http://images.novusbio.com/fullsize/IKK-beta-Antibody-10AG2-Flow-Cytometry-NB100-56509-img0010.jpg)
![Flow Cytometry: IKK beta Antibody (10AG2) [NB100-56509] - Analysis using Alexa Fluor (R) 647 conjugate of NB100-56509. An intracellular stain was performed on HeLa cells with IKK beta antibody (10AG2) NB100-56509 (blue) and a matched isotype control NBP2-27287 (orange). Cells were fixed with 4% PFA and then permeablized with 0.1% saponin. 1 ug of antibody was added to 100 uL of staining buffer and cells were incubated for 30 minutes at room temperature. Both antibodies were conjugated to Alexa Fluor 647.](http://images.novusbio.com/fullsize/IKK-beta-Antibody-10AG2-Flow-Cytometry-NB100-56509-img0011.jpg)
![Simple Western: IKK beta Antibody (10AG2) [NB100-56509] - Lane view shows a specific band for IKK beta 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/IKK-beta-Antibody-10AG2-Simple-Western-NB100-56509-img0008.jpg)
![Western Blot: IKK beta Antibody (10AG2) - BSA Free [NB100-56509] - TRAM is required for the pro-inflammatory polarization of macrophages by SLD-LPS. (A,B) Flow cytometry analysis of Ly6C (A) or CD200R (B) expression in WT or TRAM−/− live-cell-gated macrophages with geometric MFI quantification on right. Pink = PBS, Blue = 100 pg/ml LPS. (C–E) Representative Western blots of IKK-beta (C), p-p65 (D), & total NF-kappa B p65 (E) expression in WT & TRAM−/− monocytes treated with either PBS or 100 pg/mL LPS for 5 days. Quantification is depicted on the right. (F) Ratio of p-p65/total p65 (p-p65 levels from (D) divided by corresponding total p65 levels). All data are representative of at least 3 separate experiments (n = 3) for (A,B) & n = 6 for (C–F). ANOVA with Tukey's multiple comparisons test (A,B); unpaired student t-test (C–F) *p < 0.05, **p < 0.01, ***p < 0.001, ****p < 0.0001, n.s, non-significant; MFI, Mean fluorescence intensity. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/32765513), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-56509_mouse-monoclonal-ikk-beta-antibody-10ag2-31020241554520.jpg)
![Western Blot: DYRK1A Antibody (7D10) [H00001859-M01] - DYRK1A monoclonal antibody (M01), clone 7D10. Western Blot analysis of DYRK1A expression in Raw 264.7.](http://images.novusbio.com/fullsize/DYRK1A-Antibody-7D10-Western-Blot-H00001859-M01-img0011.jpg "Western Blot: DYRK1A Antibody (7D10) [H00001859-M01] - DYRK1A monoclonal antibody (M01), clone 7D10. Western Blot analysis of DYRK1A expression in Raw 264.7.")
![Western Blot: DYRK1A Antibody (7D10) [H00001859-M01] - DYRK1A monoclonal antibody (M01), clone 7D10. Western Blot analysis of DYRK1A expression in PC-12 ( Cat # L012V1 ).](http://images.novusbio.com/fullsize/DYRK1A-Antibody-7D10-Western-Blot-H00001859-M01-img0001.jpg)
![Western Blot: DYRK1A Antibody (7D10) [H00001859-M01] - DYRK1A monoclonal antibody (M01), clone 7D10. Western Blot analysis of DYRK1A expression in 293 ( Cat # L026V1 ).](http://images.novusbio.com/fullsize/DYRK1A-Antibody-7D10-Western-Blot-H00001859-M01-img0002.jpg)
![Western Blot: DYRK1A Antibody (7D10) [H00001859-M01] - DYRK1A monoclonal antibody (M01), clone 7D10 Western Blot analysis of DYRK1A expression in Hela NE ( Cat # L013V3 ).](http://images.novusbio.com/fullsize/DYRK1A-Antibody-7D10-Western-Blot-H00001859-M01-img0003.jpg)
![Western Blot: DYRK1A Antibody (7D10) [H00001859-M01] - DYRK1A monoclonal antibody (M01), clone 7D10. Western Blot analysis of DYRK1A expression in Raw 264.7 ( Cat # L024V1 ).](http://images.novusbio.com/fullsize/DYRK1A-Antibody-7D10-Western-Blot-H00001859-M01-img0004.jpg)
![Western Blot: DYRK1A Antibody (7D10) [H00001859-M01] - DYRK1A monoclonal antibody (M01), clone 7D10. Western Blot analysis of DYRK1A expression in NIH/3T3 ( Cat # L018V1 ).](http://images.novusbio.com/fullsize/DYRK1A-Antibody-7D10-Western-Blot-H00001859-M01-img0005.jpg)
![Western Blot: DYRK1A Antibody (7D10) [H00001859-M01] - DYRK1A monoclonal antibody (M01), clone 7D10. Analysis of DYRK1A expression in Hela S3 NE.](http://images.novusbio.com/fullsize/DYRK1A-Antibody-7D10-Western-Blot-H00001859-M01-img0009.jpg)
![Western Blot: DYRK1A Antibody (7D10) [H00001859-M01] - DYRK1A monoclonal antibody (M01), clone 7D10. Western Blot analysis of DYRK1A expression in K-562.](http://images.novusbio.com/fullsize/DYRK1A-Antibody-7D10-Western-Blot-H00001859-M01-img0012.jpg)
![ELISA: DYRK1A Antibody (7D10) [H00001859-M01] - Detection limit for recombinant GST tagged DYRK1A is approximately 0.03ng/ml as a capture antibody.](http://images.novusbio.com/fullsize/DYRK1A-Antibody-7D10-ELISA-H00001859-M01-img0010.jpg)
![Immunocytochemistry/Immunofluorescence: PINK1 Antibody [NBP1-49678] - PINK1 antibody was tested in HepG2 cells with DyLight 488 (green). Nuclei and alpha-tubulin were counterstained with DAPI (blue) and DyLight 550 (red).](http://images.novusbio.com/fullsize/PINK1-Antibody-Immunocytochemistry-Immunofluorescence-NBP1-49678-img0002.jpg "Immunocytochemistry/Immunofluorescence: PINK1 Antibody [NBP1-49678] - PINK1 antibody was tested in HepG2 cells with DyLight 488 (green). Nuclei and alpha-tubulin were counterstained with DAPI (blue) and DyLight 550 (red).")
![Simple Western: PINK1 Antibody [NBP1-49678] - Lane view shows a specific band for PINK1 at a dilution of 1:50 in 1.0 mg/ml of HeLa lysate. Molecular weight ~61kDa. This experiment was performed under reducing conditions using the 12-230kDa separation system. * Non-specific interaction with the 230 kDa Simple Western standard may be seen with this antibody.](http://images.novusbio.com/fullsize/PINK1-Antibody-Simple-Western-NBP1-49678-img0006.jpg)
![Immunohistochemistry-Paraffin: PINK1 Antibody [NBP1-49678] - Stain in paraffin embedded mouse brain.](http://images.novusbio.com/fullsize/PINK1-Antibody-Immunohistochemistry-Paraffin-NBP1-49678-img0004.jpg)
![Immunocytochemistry/Immunofluorescence: PINK1 Antibody [NBP1-49678] - PINK1 antibody was tested at 1:50 in HeLa cells with DyLight 488 (green). Nuclei and alpha-tubulin were counterstained with DAPI (blue) and DyLight 550 (red). Image objective 40x.](http://images.novusbio.com/fullsize/PINK1-Antibody-Immunocytochemistry-Immunofluorescence-NBP1-49678-img0005.jpg)
![Western Blot: PINK1 Antibody [NB100-493] - Detection of murine PINK1 using NB100-493. Lane 1: molecular weight marker. Lane 2. MES cell Mitochondria (20 ug) with a band at the observed molecular weight of 63 kDa. Lane 3. MES cytosol (20 ug). Lane 4. MES nuclear (20 ug) as negative control.Lane 5. Purified human cytochrome C (0.1 ug) as PINK1 negative control.](http://images.novusbio.com/fullsize/PINK1-Antibody-Western-Blot-NB100-493-img0003.jpg "Western Blot: PINK1 Antibody [NB100-493] - Detection of murine PINK1 using NB100-493. Lane 1: molecular weight marker. Lane 2. MES cell Mitochondria (20 ug) with a band at the observed molecular weight of 63 kDa. Lane 3. MES cytosol (20 ug). Lane 4. MES nuclear (20 ug) as negative control.Lane 5. Purified human cytochrome C (0.1 ug) as PINK1 negative control.")
![Western Blot: TBK1 Antibody (108A429) [NB100-56705] - Western blot using lysates from U20S parental cell line and TBK1 knockout U20S cell line (KO), collected in RIPA buffer. Nitrocellulose membrane was probed with Mouse Anti-Human/Mouse/Rat TBK1 Monoclonal Antibody (Catalog # NB100-56705) at 1 ug/ul O/N at 4C, followed by HRP-conjugated Anti-Mouse IgG Secondary Antibody and ECL detection. A specific band at 83 kDa was detected for TBK1 in the parental U20S cell line, but is not detectable in knockout U20S cell line. The Ponceau stained transfers of each blot are shown to confirm equal protein loading. Image, protocol and testing courtesy of YCharOS Inc. (ycharos.com).](http://images.novusbio.com/fullsize/TBK1-Antibody-108A429-Knockout-Validated-NB100-56705-img0023.jpg "<b>Genetic Strategies Validation. </b>Western Blot: TBK1 Antibody (108A429) [NB100-56705] - Western blot using lysates from U20S parental cell line and TBK1 knockout U20S cell line (KO), collected in RIPA buffer. Nitrocellulose membrane was probed with Mouse Anti-Human/Mouse/Rat TBK1 Monoclonal Antibody (Catalog # NB100-56705) at 1 ug/ul O/N at 4C, followed by HRP-conjugated Anti-Mouse IgG Secondary Antibody and ECL detection. A specific band at 83 kDa was detected for TBK1 in the parental U20S cell line, but is not detectable in knockout U20S cell line. The Ponceau stained transfers of each blot are shown to confirm equal protein loading. Image, protocol and testing courtesy of YCharOS Inc. (ycharos.com).")
![<b>Genetic Strategies Validation. </b>Simple Western: TBK1 Antibody (108A429) [NB100-56705] - Lane view shows a specific band for NAK/TBK1 in 0.5 mg/ml of Daudi (left) and Raw 264.7 (right) lysate. This experiment was performed under reducing conditions using the 12-230 kDa separation system. * Non-specific interaction with the 230 kDa Simple Western standard may be seen with this antibody](http://images.novusbio.com/fullsize/TBK1-Antibody-108A429-Simple-Western-NB100-56705-img0014.jpg)
![Immunohistochemistry-Paraffin: TBK1 Antibody (108A429) [NB100-56705] - Analysis of FFPE human testis tissue section using Peripheral Node Addressin antibody (clone MECA-79R) at 1:200. The staining was developed with HRP-DAB detection method and the counterstaining was performed using hematoxylin.](http://images.novusbio.com/fullsize/TBK1-Antibody-108A429-Immunohistochemistry-Paraffin-NB100-56705-img0021.jpg)
![Western Blot: TBK1 Antibody (108A429) [NB100-56705] - Analysis using Azide and BSA Free version of NB100-56705. Lysate from 293 cells untransfected (lane 1) and transfected with human TBK1 cDNA (lane 2) probed with TBK1 antibody at 2 ug/ml.](http://images.novusbio.com/fullsize/TBK1-Antibody-108A429-Western-Blot-NB100-56705-img0016.jpg)
![Immunocytochemistry/Immunofluorescence: TBK1 Antibody (108A429) [NB100-56705] - Antibody was tested in HeLa cells with DyLight 488 (green). Nuclei and alpha-tubulin were counterstained with DAPI (blue) and DyLight 550 (red). A dilution of 1:10 was used. Image objective 40x.](http://images.novusbio.com/fullsize/TBK1-Antibody-108A429-Immunocytochemistry-Immunofluorescence-NB100-56705-img0013.jpg)
![Immunohistochemistry-Paraffin: TBK1 Antibody (108A429) [NB100-56705] - Immunohistochemistry: TBK1 Antibody (108A429) - Azide and BSA Free [NBP2-33243] - Staining on human testis (Formalin-Fixed Paraffin-Embedded (FFPE)) Image from the Azide and BSA Free version of this antibody.](http://images.novusbio.com/fullsize/TBK1-Antibody-108A429-Immunohistochemistry-Paraffin-NB100-56705-img0022.jpg)
![Western Blot: TBK1 Antibody (108A429) [NB100-56705] - Analysis of Human Daudi (A) and mouse RAW (B) cell lysate probed with TBK1 antibody at 2 ug/ml.](http://images.novusbio.com/fullsize/TBK1-Antibody-108A429-Western-Blot-NB100-56705-img0012.jpg)
![Immunocytochemistry/Immunofluorescence: TBK1 Antibody (108A429) [NB100-56705] - HeLa cells were fixed for 10 minutes using 10% formalin and then permeabilized for 5 minutes using 1X PBS + 0.05% Triton X-100. The cells were incubated with anti-TBK1 at 20 ug/ml overnight at 4C and detected with an anti-mouse DyLight 488 (Green) at a 1:500 dilution. Actin was detected with Phalloidin 568 (Red) at a 1:200 dilution. Nuclei were counterstained with DAPI (Blue). Cells were imaged using a 40X objective.](http://images.novusbio.com/fullsize/TBK1-Antibody-108A429-Immunocytochemistry-Immunofluorescence-NB100-56705-img0019.jpg)
![Immunocytochemistry/Immunofluorescence: SLC31A1/CTR1 Antibody [NB100-402] - CTR1 antibody was tested in NIH-3T3 cells with DyLight 488 (green). Nuclei and alpha-tubulin were counterstained with DAPI (blue) and DyLight 550 (red).](http://images.novusbio.com/fullsize/SLC31A1-CTR1-Antibody-Immunocytochemistry-Immunofluorescence-NB100-402-img0004.jpg "Immunocytochemistry/Immunofluorescence: SLC31A1/CTR1 Antibody [NB100-402] - CTR1 antibody was tested in NIH-3T3 cells with DyLight 488 (green). Nuclei and alpha-tubulin were counterstained with DAPI (blue) and DyLight 550 (red).")
![Immunohistochemistry: SLC31A1/CTR1 Antibody [NB100-402] - Panel 1: human CTR1 staining of breast cancer tissue. Panel 2: human CTR1-antigen competition in breast cancer tissue.](http://images.novusbio.com/fullsize/SLC31A1-CTR1-Antibody-Immunohistochemistry-NB100-402-img0002.jpg)
![Immunohistochemistry: SLC31A1/CTR1 Antibody [NB100-402] - Left panel: Antibody staining of hCTR1 overexpressing cell line. Right panel: Antibody plus peptide competition staining.](http://images.novusbio.com/fullsize/SLC31A1-CTR1-Antibody-Immunohistochemistry-NB100-402-img0003.jpg)
