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![Western Blot: HeLa Chloroquine Treated / Untreated Cell Lysate [NBP2-49689] - HeLa cells were treated with (+) or without 50 uM (-) of Chloriquine (CQ) for 24 hours. Total cell lysates were prepared and separated on a 12% gel by SDS-PAGE. Protein was transferred to PVDF membrane and blocked in 5% non-fat milk. The membrane was then probed with 2 ug/ml of p62/SQSTM1 antibody (NBP1-42821) in 1% milk and detected with an anti-rabbit HRP secondary antibody using chemiluminescence. Note the upregulation of p62 (arrowhead) in response to chloroquine treatment and the blockage of autophagy.](http://images.novusbio.com/fullsize/HeLa-Chloroquine-Treated---Untreated-Cell-Lysate-Western-Blot-NBP2-49689-img0005.jpg "Western Blot: HeLa Chloroquine Treated / Untreated Cell Lysate [NBP2-49689] - HeLa cells were treated with (+) or without 50 uM (-) of Chloriquine (CQ) for 24 hours. Total cell lysates were prepared and separated on a 12% gel by SDS-PAGE. Protein was transferred to PVDF membrane and blocked in 5% non-fat milk. The membrane was then probed with 2 ug/ml of p62/SQSTM1 antibody (NBP1-42821) in 1% milk and detected with an anti-rabbit HRP secondary antibody using chemiluminescence. Note the upregulation of p62 (arrowhead) in response to chloroquine treatment and the blockage of autophagy.")
![<b>Biological Strategies Validation. </b>Western Blot: HeLa Chloroquine Treated / Untreated Cell Lysate [NBP2-49689] - 10 ug of Chloroquine treated (+) and untreated (-) HeLa lysates in 1x Laemmli sample buffer (NBP2-49689) were separated on a 4-15% gel by SDS-PAGE, transferred to 0.2 um PVDF membrane and blocked in 5% non-fat milk in TBST. The membrane was probed with 1 ug/ml monoclonal anti-LC3 (NBP2--46892) and detected with an anti-rabbit secondary antibody using chemiluminescence.](http://images.novusbio.com/fullsize/HeLa-Chloroquine-Treated---Untreated-Cell-Lysate-Western-Blot-NBP2-49689-img0002.jpg)
![Western Blot: HeLa Chloroquine Treated / Untreated Cell Lysate [NBP2-49689] - Human Cervical carcinoma cells (HeLa) were treated with (+) and without (-) 50 uM Chloroquine overnight. Whole cell protein lysates were prepared in 1x Laemmli sample buffer and approximately 10 ug of each lysate (NBP2-49689) was separated on a 4-15% gel by SDS-PAGE, transferred to 0.2 um PVDF membrane and blocked in 5% non-fat milk in TBST. The membrane was probed with 1 ug/ml anti-LC3 (NB100-2220) and 1 ug/ml anti-alpha tubulin (NB100-690) as a loading control, and detected with the appropriate secondary antibodies using chemiluminescence.](http://images.novusbio.com/fullsize/HeLa-Chloroquine-Treated---Untreated-Cell-Lysate-Western-Blot-NBP2-49689-img0003.jpg)
![Western Blot: HeLa Chloroquine Treated / Untreated Cell Lysate [NBP2-49689] - HeLa cells were treated with vehicle (-) or with 50 uM chloriquine (+) for 24 hours and the total cell lysates were prepared. The lysates were separated on a 12% gel by SDS-PAGE. Protein was transferred to PVDF mebbrane and blocked in 5% non-fat milk. The membrane was then probed with 1 ug/ml of p62/SQSTM1 antibody (NBP1-48320) in 1% milk and dectected with an anti-rabbit HRP secondary antibody using chemiluminescence. Note the upregulation of p62 (arrowhead) in response to chloroquine treatment and the blockage of autophagy.](http://images.novusbio.com/fullsize/HeLa-Chloroquine-Treated---Untreated-Cell-Lysate-Western-Blot-NBP2-49689-img0004.jpg)
![Western Blot: HeLa Whole Cell Lysate [NB800-PC1] - WB analysis of HeLa whole cell lysate (NB800-PC1) using p14ARF antibody (NB200-111) with ECL detection method.](http://images.novusbio.com/fullsize/HeLa-Whole-Cell-Lysate-Western-Blot-NB800-PC1-img0007.jpg "Western Blot: HeLa Whole Cell Lysate [NB800-PC1] - WB analysis of HeLa whole cell lysate (NB800-PC1) using p14ARF antibody (NB200-111) with ECL detection method.")
![Western Blot: HeLa Whole Cell Lysate [NB800-PC1] - Ponceau S staining of HeLa whole cell lysate using NB800-PC1.](http://images.novusbio.com/fullsize/HeLa-Whole-Cell-Lysate-Western-Blot-NB800-PC1-img0003.jpg)
![Western Blot: HeLa Whole Cell Lysate [NB800-PC1] - Analysis of STIM-1 antibody (NB110-60547) using HeLa whole cell lysate [NB800-PC1].](http://images.novusbio.com/fullsize/HeLa-Whole-Cell-Lysate-Western-Blot-NB800-PC1-img0004.jpg)
![Western Blot: HeLa Whole Cell Lysate [NB800-PC1] - WB analysis of 30ug of HeLa whole cell lysate (NB800-PC1) using rabbit polyclonal Survivin antibody (NB 500-201) at 1ug/ml concentration. Detection was performed using ECL based method with 1 minute exposure time.](http://images.novusbio.com/fullsize/HeLa-Whole-Cell-Lysate-Western-Blot-NB800-PC1-img0005.jpg)
![Western Blot: HeLa Whole Cell Lysate [NB800-PC1] - WB analysis of HeLa whole cell lysate (NB800-PC1) using rabbit polyclonal NBS1 antibody (NB100-143) with detection employing ECL method.](http://images.novusbio.com/fullsize/HeLa-Whole-Cell-Lysate-Western-Blot-NB800-PC1-img0006.jpg)
![Western Blot: HeLa Hypoxic / Normoxic Tissue Lysate [NBP2-36452] - Western blot analysis of HIF-1 alpha antibody (NB100-134) in HeLa hypoxic and normoxic lysates (NBP2-36452). Tubulin loading control is shown below.](http://images.novusbio.com/fullsize/HeLa-Hypoxic---Normoxic-Tissue-Lysate-Western-Blot-NBP2-36452-img0002.jpg "Western Blot: HeLa Hypoxic / Normoxic Tissue Lysate [NBP2-36452] - Western blot analysis of HIF-1 alpha antibody (NB100-134) in HeLa hypoxic and normoxic lysates (NBP2-36452). Tubulin loading control is shown below.")
![Western Blot: HeLa Hypoxic Simulated / Normoxic Tissue Lysate [NBP2-36450] - Western blot analysis of HIF-1 alpha antibody (NB100-134) in HeLa cobalt chloride treated and normoxic lysates (NBP2-36450). Tubulin loading control is shown below.](http://images.novusbio.com/fullsize/HeLa-Hypoxic-Simulated---Normoxic-Tissue-Lysate-Western-Blot-NBP2-36450-img0002.jpg "Western Blot: HeLa Hypoxic Simulated / Normoxic Tissue Lysate [NBP2-36450] - Western blot analysis of HIF-1 alpha antibody (NB100-134) in HeLa cobalt chloride treated and normoxic lysates (NBP2-36450). Tubulin loading control is shown below.")
![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)
![Simple Western: beta-Actin Antibody [NB600-532] - Simple Western lane view shows a specific band for Beta Actin using NB600-532 at 1:200 in A431, C2C12 and C6 cell lysates. This experiment was performed under reducing conditions using the 12-230 kDa separation system.](http://images.novusbio.com/fullsize/beta-Actin-Antibody-Simple-Western-NB600-532-img0016.jpg "Simple Western: beta-Actin Antibody [NB600-532] - Simple Western lane view shows a specific band for Beta Actin using NB600-532 at 1:200 in A431, C2C12 and C6 cell lysates. This experiment was performed under reducing conditions using the 12-230 kDa separation system.")
![Western Blot: beta-Actin Antibody [NB600-532] - Detection of actin in 3T3 lysates (20ug). ECL detection 30 seconds. A specific band is seen using different dilutions: Lane 1 (1:15,000), Lane 2 (1:10,000), and Lane 3 (1:15,000).](http://images.novusbio.com/fullsize/beta-Actin-Antibody-Western-Blot-NB600-532-img0009.jpg)
![Western Blot: beta-Actin Antibody [NB600-532] - Detection of human and mouse Cytoskeletal Actin by western blot. Samples: Whole cell lysate (50 ug) from HeLa, HEK293T, Jurkat, mouse TCMK-1, and mouse NIH 3T3 cells prepared using NETN lysis buffer. Antibody: Affinity purified rabbit anti-Cytoskeletal Actin antibody NB600-532 used for WB at 0.1 ug/ml. Detection: Chemiluminescence with an exposure time of 1 second.](http://images.novusbio.com/fullsize/beta-Actin-Antibody-Western-Blot-NB600-532-img0014.jpg)
![Western Blot: beta-Actin Antibody [NB600-532] - Mouse colon whole cell lysate. PVDF membrane was probed with Rabbit Anti-B actin Antibody (Catalog # NB600-532) followed by HRP-conjugated Anti-Rabbit IgG Secondary Antibody. WB image submitted by a verified customer review.](http://images.novusbio.com/fullsize/beta-Actin-Antibody-Western-Blot-NB600-532-img0019.jpg)
![Immunohistochemistry: beta-Actin Antibody [NB600-532] - Detection of human Cytoskeletal Actin by immunohistochemistry. Sample: FFPE section of human ovarian cancer. Antibody: Affinity purified rabbit anti-Cytoskeletal Actin (NB600-532). Detection: DAB](http://images.novusbio.com/fullsize/beta-Actin-Antibody-Immunohistochemistry-NB600-532-img0015.jpg)
![Western Blot: beta-Actin Antibody [NB600-532] - Western blot analysis of Actin (NB600-532) using RCC4 whole cell lysate [NBP1-30412].](http://images.novusbio.com/fullsize/beta-Actin-Antibody-Western-Blot-NB600-532-img0006.jpg)
![Western Blot: beta-Actin Antibody [NB600-532] - Western blot analysis of Actin (NB600-532) using HepG2 whole cell lysate [NBP1-42569].](http://images.novusbio.com/fullsize/beta-Actin-Antibody-Western-Blot-NB600-532-img0007.jpg)
![Western Blot: beta-Actin Antibody [NB600-532] - Analysis using the HRP conjugate of NB600-532. Detection of Beta Actin in MCF-7 cell lysate (20ug) using anti-Beta Actin antibody. WB image submitted by a verified customer review.](http://images.novusbio.com/fullsize/beta-Actin-Antibody-Western-Blot-NB600-532-img0011.jpg)
![Western Blot: beta-Actin Antibody [NB600-532] - Treatments of periplocin and/or TRAIL activate DR4, FADD, and proapoptotic proteins in HCC cells. The effect of periplocin treatment on the expression of DR4, DR5, and FADD was analyzed by western blot. Image collected and cropped by CiteAb from the following publication (//www.hindawi.com/journals/ecam/2013/958025/), licensed under a CC-BY license.](http://images.novusbio.com/fullsize/beta-Actin-Antibody-Western-Blot-NB600-532-img0018.jpg)
![Western Blot: beta-Actin Antibody [NB600-532] - Hypoxic preconditioning increases PBMNC sensitivity to apelin-13 via upregulation of APJ expression, leading to growth factor secretion.(a) APJ protein expression was significantly increased in hypoxic PBMNCs. *p <0.05 vs. N-PBMNCs. Image collected and cropped by CiteAb from the following publication (//www.nature.com/articles/srep19379), licensed under a CC-BY license.](http://images.novusbio.com/fullsize/beta-Actin-Antibody-Western-Blot-NB600-532-img0017.jpg)
![Immunohistochemistry: beta-Actin Antibody [NB600-532] - Sample: FFPE section of human lung carcinoma. Antibody: Affinity purified rabbit anti-Cytoskeletal Actin used at a dilution of 1:1,000 (1ug/ml). Detection: DAB](http://images.novusbio.com/fullsize/beta-Actin-Antibody-Immunohistochemistry-NB600-532-img0012.jpg)
![Western Blot: beta-Actin Antibody [NB600-532] - Cotreatment of periplocin & TRAIL activated IAP. (a) The expression levels of Bax, Bad, Mcl-1, apaf-1, & caspase 9 in HA22T/VGH in response to 1 μM periplocin and/or 100 ng/mL TRAIL treatment were examined by western blot. (b) The expression levels of Bcl-2, cIAP-1, cIAP-2, XIAP, & survivin in HA22T/VGH in response to 1 μM periplocin and/or 100 ng/mL TRAIL treatment were examined by western blot. The original blots are shown in supplemental Figure 2. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/23365613), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb600-532_rabbit-polyclonal-beta-actin-antibody-310202415284538.jpg)
![Western Blot: beta-Actin Antibody [NB600-532] - Treatments of periplocin and/or TRAIL activate DR4, FADD, & proapoptotic proteins in HCC cells. (a) The effect of periplocin treatment on the expression of DR4, DR5, & FADD was analyzed by western blot. (b) HA22T/VGH cells were treated with different doses of the indicated compounds for 24 h. Expressions of both proforms & cleaved forms of caspase-8, caspase 3, PARP, & BID were analyzed by western blotting. (c) Huh-7 cells were treated with different concentrations of the indicated compounds for 4 h or 24 h. The expression of caspase-8, caspase-9 was analyzed after indicated compounds treatment for 4 h, & the expression of caspase 3, PARP, BID was analyzed after the treatment of indicated compounds for 24 h. (d) HA22T/VGH cells were pretreated with 20 μM or 50 μM inhibitors against caspase-3 (Z-DEVD-FMK), caspasae-8 (Z-IETD-FMK), caspase-9 (Z-LEHD-FMK), & general caspase inhibitor (Z-VAD-FMK) for 3 hours prior to periplocin and/or TRAIL treatment. Cell viability was examined by MTT assay. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/23365613), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb600-532_rabbit-polyclonal-beta-actin-antibody-310202416182625.jpg)
![Western Blot: beta-Actin Antibody [NB600-532] - GRN PTC readthrough rescues FTLD/NCL lysosomal pathological CSTD maturation phenotype in hiPSC-derived R493X−/− KI cortical neurons. a DIV 80 WT & R493X−/− KI hiPSC-derived cortical neurons were treated with vehicle solution, G418 alone, G418 in combination with CDX5–288, & rec. Human PGRN at the indicated concentrations for 72 h. Expression of mature CSTD in treated WT & R493X−/− KI cortical neuron lysates analyzed by western blotting, using actin as the loading control. b Densitometric quantification of CSTD expression in the aforementioned cortical neuron lysates normalized to vehicle-treated WT levels. n = 3–6 independent cultures; values are shown as mean ± SEM; * p < 0.05, ** p < 0.01, was determined by one-way ANOVA with Tukey’s multiple comparison test Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/32178712), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb600-532_rabbit-polyclonal-beta-actin-antibody-31020241618923.jpg)
![Western Blot: beta-Actin Antibody [NB600-532] - Induction of PTC readthrough by G418 & enhancers in hiPSC-derived R493X−/− KI astrocytes. a R493X−/− KI hiPSC-derived astrocytes were treated with vehicle solution, G418 alone, G418 in combination with CDX5–288, & rec. Human PGRN at the indicated concentrations for 72 h. Expression of PGRN & GRN-2,3 peptides in treated WT & R493X−/− KI astrocyte samples were analyzed by western blotting, using actin as the loading control. b Densitometric quantification of ~ 70 kDa PGRN (i) & GRN-2,3 peptide (ii) in astrocyte lysates (a) normalized to vehicle-treated (VT) WT levels. VT WT was excluded from ii due to oversaturation of GRN-2,3 signal in long exposure blot. For clarity, rec. Human PGRN treated R493X−/− KI astrocytes expressed 20.9% ± 0.027 of VT WT GRN-2,3 levels based on quantification of the short exposure blot (data not shown). c R493X−/− KI hiPSC-derived astrocytes were treated with vehicle solution, G418 in combination with CDX5–288, & G418 CDX5–288 combination with either 10 or 30 μM of Z-Phe-Phe-FMK for 72 h. Again, expression of PGRN in WT & R493X−/− KI astrocyte lysates was also analyzed by western blotting, using actin as the loading control. d Densitometric quantification of full-length PGRN in astrocyte lysates (c) normalized to VT WT levels. n = 3 independent cultures (except in dn = 2); values are shown as mean ± SEM; p < 0.05, ** p < 0.01, *** p < 0.0001 was determined by one-way ANOVA with Tukey’s multiple comparison test Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/32178712), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb600-532_rabbit-polyclonal-beta-actin-antibody-310202416163749.jpg)
![Simple Western: beta-Actin Antibody [NB600-532] - Induction of PTC readthrough by G418 & CDX5 enhancers in cells expressing GRN-V5. a Schematic of full-length PGRN highlighting the position of the S116X (UAA), R418X (UGA), & R493X (UGA) nonsense mutations in relation to the position of individual granulin peptides & the C-terminal V5 tag. b HEK293 cell lines stably expressing GRN-V5 with the indicated nonsense mutations were treated with G418 & the indicated concentrations of CDX5–1, CDX5–196, & CDX5–288 for 72 h. Cell culture supernatants (extracellular) & cell lysates (intracellular) were subjected to automated capillary electrophoresis western analysis. Full-length PGRN was detected with a V5 antibody. Actin was measured in cell lysates as a loading control. The readthrough enhancement ratios are indicated under the lanes. The proportion loaded was 15–20 fold lower for the extracellular samples than for the intracellular samples Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/32178712), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb600-532_rabbit-polyclonal-beta-actin-antibody-310202416173532.jpg)
![Western Blot: UbcH10/UBE2C Antibody [NB100-1084] - (2ug/ml) staining of HEK293 (A) and HeLa (B) cell lysate (35ug protein in RIPA buffer). Detected by chemiluminescence.](http://images.novusbio.com/fullsize/UbcH10-UBE2C-Antibody-Western-Blot-NB100-1084-img0004.jpg "Western Blot: UbcH10/UBE2C Antibody [NB100-1084] - (2ug/ml) staining of HEK293 (A) and HeLa (B) cell lysate (35ug protein in RIPA buffer). Detected by chemiluminescence.")
![Immunocytochemistry/Immunofluorescence: UbcH10/UBE2C Antibody [NB100-1084] - Analysis of paraformaldehyde fixed U2OS cells, permeabilized with 0.15% Triton. Primary incubation 1hr (10ug/ml) followed by Alexa Fluor 488 secondary antibody (4ug/ml), showing cytoplasmic /Plasma Membrane staining. The nuclear stain is DAPI (blue). Negative control: Unimmunized goat IgG (10ug/ml) followed by Alexa Fluor 488 secondary antibody (4ug/ml).](http://images.novusbio.com/fullsize/UbcH10-UBE2C-Antibody-Immunocytochemistry-Immunofluorescence-NB100-1084-img0003.jpg)
![Flow Cytometry: UbcH10/UBE2C Antibody [NB100-1084] - Analysis of paraformaldehyde fixed HeLa cells (blue line), permeabilized with 0.5% Triton. Primary incubation 1hr (10ug/ml) followed by Alexa Fluor 488 secondary antibody (2ug/ml). IgG control: Unimmunized goat IgG (black line) followed by Alexa Fluor 488 secondary antibody.](http://images.novusbio.com/fullsize/UbcH10-UBE2C-Antibody-Flow-Cytometry-NB100-1084-img0001.jpg)
![Immunocytochemistry/Immunofluorescence: UbcH10/UBE2C Antibody [NB100-1084] - Analysis of paraformaldehyde fixed MCF7 cells, permeabilized with 0.15% Triton. Primary incubation 1hr (10ug/ml) followed by Alexa Fluor 488 secondary antibody (4ug/ml), showing cytoplasmic staining. The nuclear stain is DAPI (blue). Negative control: Unimmunized goat IgG (10ug/ml) followed by Alexa Fluor 488 secondary antibody (4ug/ml).](http://images.novusbio.com/fullsize/UbcH10-UBE2C-Antibody-Immunocytochemistry-Immunofluorescence-NB100-1084-img0002.jpg)
![Western Blot: RelA/NFkB p65 Antibody (27F9.G4) [NBP1-77815] - RelA/RelA/NFkB p65 p65 antibody (27F9.G4) was used to detect p65 by Western blot. Samples were prepared in RIPA lysis buffer, boiled with NuPage 4x LDS Sample Buffer and run on NuPage 4-12% Bis-Tris Gels. Blot was incubated with primary antibody at a dilution of 1:500 and detected with HRP conjugated anti-mouse antibody at a dilution of 1:10000.](http://images.novusbio.com/fullsize/RelA-NFkB-p65-Antibody-27F9-G4-Western-Blot-NBP1-77815-img0018.jpg "Western Blot: RelA/NFkB p65 Antibody (27F9.G4) [NBP1-77815] - RelA/RelA/NFkB p65 p65 antibody (27F9.G4) was used to detect p65 by Western blot. Samples were prepared in RIPA lysis buffer, boiled with NuPage 4x LDS Sample Buffer and run on NuPage 4-12% Bis-Tris Gels. Blot was incubated with primary antibody at a dilution of 1:500 and detected with HRP conjugated anti-mouse antibody at a dilution of 1:10000.")
![Immunocytochemistry/Immunofluorescence: RelA/NFkB p65 Antibody (27F9.G4) [NBP1-77815] - Tissue: Human Fibroblasts Top: Before activation Bottom: After activation with poly IC Left: anti p65 NLS specific Right: Monoclonal antibody C-Term The two antibodies that are shown target different regions of the p65 protein. The different staining patterns are thought to correspond with different functional regions of the protein.](http://images.novusbio.com/fullsize/RelA-NFkB-p65-Antibody-27F9-G4-Immunocytochemistry-Immunofluorescence-NBP1-77815-img0020.jpg)
![Immunohistochemistry: RelA/NFkB p65 Antibody (27F9.G4) [NBP1-77815] - Antibody has been tested in immunohistochemistry, analyzed by an anatomic pathologist and validated for use in IHC applications against formalin-fixed, paraffin-embedded human tissues. Showed moderate to strong staining within many tissues, including epithelium of the breast, small intestine, kidney, pancreas, prostate, skin, placenta, and uterus, as well as within neurons and lymphoid tissues such as spleen, thymus, and tonsil. The antibody produced an excellent signal with almost no background staining at a concentration of 2.5ug/ml. The image displayed shows specific staining in colon carcinoma as the precipitated red signal, with a hematoxylin purple nuclear counterstain.](http://images.novusbio.com/fullsize/RelA-NFkB-p65-Antibody-27F9-G4-Immunohistochemistry-NBP1-77815-img0019.jpg)
![Western Blot: RelA/NFkB p65 Antibody (27F9.G4) [NBP1-77815] - RelA/NFkB p65 antibody (27F9.G4) was used to detect ~65 kD band (red arrow) in HeLa whole cell lysate. Lysate was run on 4-20% gradient gel transferred under standard conditions and blocked in 1% BSA-TBST for 30 min at RT. Blot was probed with monoclonal anti-NFkB p65 at 1:1000 in 1% BSA-TBST at 4C and detected with HRP conjugated Rb-anti-Mouse antibody at 1:40,000 in for 30 min at RT.](http://images.novusbio.com/fullsize/RelA-NFkB-p65-Antibody-27F9-G4-Western-Blot-NBP1-77815-img0017.jpg)
![Immunocytochemistry/Immunofluorescence: RelA/NFkB p65 Antibody (27F9.G4) [NBP1-77815] - Used at a dilution of 1:5000. Hela cells were grown to sub-confluent on 18 mm2 glass coverslips #1.5. Cells were either unstimulated (A), or stimulated (B) with 50 ng/ml of TNF alpha for 30 min prior fixation. Cells were then fixed in methanol and blocked with 10% normal goat serum (NGS), in PBS, and TritonX 0.2% (Tx) and incubated for 1 hr at RT with primary ab, counterstained with DAPI and washed in PBS/NGS/Tx. Cells were incubated for 1 hr at RT with Atto 425 conjugated anti mouse secondary antibody for STED CW imaging.](http://images.novusbio.com/fullsize/RelA-NFkB-p65-Antibody-27F9-G4-Immunocytochemistry-Immunofluorescence-NBP1-77815-img0012.jpg)
![Immunocytochemistry/Immunofluorescence: RelA/NFkB p65 Antibody (27F9.G4) [NBP1-77815] - Mouse endothelial cells. Unstimulated control cells (left) show cytoplasmic staining, TNF-alpha stimulated cells (right) show nuclear staining. For staining, cells were washed with PBS to remove all traces of culture media and fixed with paraformaldehyde 4 % (45 min). Slides were washed with PBT (phosphate buffer 0.1M + Triton-X-100 0.1 %), 3 times 10 min each, then, blocked with PBT + 5 % normal goat serum, 1 hour. Sample was Incubated overnight in primary antibody (1:600 in blocking buffer). After 3X wash in PBT for 10 min, slides were incubated 1 hour with secondary antibody (1:1000) and mounted in 1:1 PB glycerol.](http://images.novusbio.com/fullsize/RelA-NFkB-p65-Antibody-27F9-G4-Immunocytochemistry-Immunofluorescence-NBP1-77815-img0013.jpg)
![Immunocytochemistry/Immunofluorescence: RelA/NFkB p65 Antibody (27F9.G4) [NBP1-77815] - RelA/NFkB p65 antibody (27F9.G4) was used to detect p65 by immunofluorescence at a dilution of 1:5000. Hela cells were grown to sub-confluent on 18 mm2 glass coverslips #1.5. Cells were either unstimulated (A), or stimulated (B) with 50 ng/ml of TNF alpha for 30 min prior fixation. Cells were then fixed in methanol and blocked with 10% normal goat serum (NGS), in PBS, and TritonX 0.2% (Tx) and incubated for 1 hr at RT with primary ab, counterstained with DAPI and washed in PBS/NGS/Tx. Cells were incubated for 1 hr at RT with Atto 425 conjugated anti mouse secondary antibody for STED CW imaging. Data was collected on a STED-CW TCS-SP5 Confocal system equipped with a DFC 350FX camera allowing sequential acquisition in widefiled, confocal and STED CW imaging on the same system.](http://images.novusbio.com/fullsize/RelA-NFkB-p65-Antibody-27F9-G4-Immunocytochemistry-Immunofluorescence-NBP1-77815-img0015.jpg)
![Western Blot: Pin1 Antibody [NBP1-77757] - Lane 1: T9ug cells treated with scrambled (scr). Lane 2: T9ug cells treated with PIN1 kd1 shRNA. Lane 3: T9ug cells treated with PIN1-overexpressing plasmid HAP1. Lane 4: T9ug cells treated with PIN1-overexpressing plasmid HAP1S67E. Lane 5: T9ug cells treated with PIN1 kd2 shRNA. Load: 25 ug per lane. Primary antibody: PIN 1 antibody at 1:400 for overnight at 4C. Secondary antibody: IRDye800 (TM) rabbit secondary antibody at 1:10,000 for 45 min at RT. Block: 5% BLOTTO overnight at 4C. Predicted size: 18 kDa for PIN-1. Other band(s): normalized with a-tubulin (a-tub) antibody.](http://images.novusbio.com/fullsize/Pin1-Antibody-Western-Blot-NBP1-77757-img0003.jpg "Western Blot: Pin1 Antibody [NBP1-77757] - Lane 1: T9ug cells treated with scrambled (scr). Lane 2: T9ug cells treated with PIN1 kd1 shRNA. Lane 3: T9ug cells treated with PIN1-overexpressing plasmid HAP1. Lane 4: T9ug cells treated with PIN1-overexpressing plasmid HAP1S67E. Lane 5: T9ug cells treated with PIN1 kd2 shRNA. Load: 25 ug per lane. Primary antibody: PIN 1 antibody at 1:400 for overnight at 4C. Secondary antibody: IRDye800 (TM) rabbit secondary antibody at 1:10,000 for 45 min at RT. Block: 5% BLOTTO overnight at 4C. Predicted size: 18 kDa for PIN-1. Other band(s): normalized with a-tubulin (a-tub) antibody.")
![Immunohistochemistry: Pin1 Antibody [NBP1-77757] - Tissue: testis. Fixation: formalin fixed paraffin embedded. Primary antibody: Anti-PIN1 at 5 ug/mL for 1 h at RT. Secondary antibody: Peroxidase rabbit secondary antibody at 1:10,000 for 45 min at RT. Staining: PIN-1 as precipitated red signal with hematoxylin purple nuclear counterstain.](http://images.novusbio.com/fullsize/Pin1-Antibody-Immunohistochemistry-NBP1-77757-img0004.jpg)
![Western Blot: Pin1 Antibody [NBP1-77757] - Detection of endogenous Pin1 in HeLa whole cell lysates. The sample was run in duplicate. A band representing Pin1 is indicated by the arrowhead. Cell lysates were electrophoresed using a straight 15% polyacrylamide gel, followed by transfer to nitrocellulose. The membrane was probed with the primary antibody at a 1:700 dilution. A 1:5,000 dilution of HRP Gt-a-Rabbit IgG was used with a 15 sec exposure time.](http://images.novusbio.com/fullsize/Pin1-Antibody-Western-Blot-NBP1-77757-img0001.jpg)
![Western Blot: Pin1 Antibody [NBP1-77757] - Lane 1: T9ug cells incubated with GST-Pin1. Lane 2: T9ug cells incubated with GST-CDK4/cyclinD1. Lane 3: T9ug cells incubated with GST-Pin1 and GST-CDK4/cyclinD1. Immunoprecipitated with pRb antibody. Load: 25 ug per lane. Primary antibody: anti-GST 1:400 for overnight at 4C. Secondary antibody: IRDye800 (TM) secondary antibody at 1:10,000 for 45 min at RT. Block: 5% BLOTTO overnight at 4C.](http://images.novusbio.com/fullsize/Pin1-Antibody-Western-Blot-NBP1-77757-img0002.jpg)
![N/A: Apc11 Antibody [NBP1-78050] - Most modifiers mature by proteolytic processing from inactive precursors (a; amino acid). Arrowheads point to the cleavage sites. Ubiquitin is expressed either as polyubiquitin or as a fusion with ribosomal proteins. Conjugation requires activating (E1) & conjugating (E2) enzymes that form thiolesters (S) with the modifiers. Modification of cullins by RUB involves SCF(SKP1/cullin-1/F-box protein) /CBC(cullin-2/elongin B/elonginC) -like E3 enzymes that are also involved in ubiquitination. UBLs do not seem to form multi-UBL chains. UCRP(ISG15) resembles two ubiquitin moieties linked head-to-tail. Whether HUB1 functions as a modifier is currently unclear. APG12 and URM1 are distinct from the other modifiers because they are unrelated in sequence to ubiquitin.](http://images.novusbio.com/fullsize/Apc11-Antibody-N-A-NBP1-78050-img0001.jpg "N/A: Apc11 Antibody [NBP1-78050] - Most modifiers mature by proteolytic processing from inactive precursors (a; amino acid). Arrowheads point to the cleavage sites. Ubiquitin is expressed either as polyubiquitin or as a fusion with ribosomal proteins. Conjugation requires activating (E1) & conjugating (E2) enzymes that form thiolesters (S) with the modifiers. Modification of cullins by RUB involves SCF(SKP1/cullin-1/F-box protein) /CBC(cullin-2/elongin B/elonginC) -like E3 enzymes that are also involved in ubiquitination. UBLs do not seem to form multi-UBL chains. UCRP(ISG15) resembles two ubiquitin moieties linked head-to-tail. Whether HUB1 functions as a modifier is currently unclear. APG12 and URM1 are distinct from the other modifiers because they are unrelated in sequence to ubiquitin.")