| Formulation | Catalog # | Availability | Price | |
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| BSA Free | BC100-494SS | |||
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| BSA Free | NB110-55288SS | |||
| Formulation | Catalog # | Availability | Price | |
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| BSA Free | NBP1-71775SS | |||
| Azide and BSA Free | NBP2-80850 | |||
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| BSA Free | NBP1-51841SS | |||
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| BSA Free | NB100-493SS | |||
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| BSA Free | NBP1-49678SS | |||
| Formulation | Catalog # | Availability | Price | |
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| BSA Free | NBP2-23489SS | |||
| Azide and BSA Free | NBP2-80702 | |||
| Formulation | Catalog # | Availability | Price | |
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| BSA Free | NBP1-89112-25ul | |||
![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: DRP1 Antibody [NB110-55288] - Total protein from human HeLa and MCF7 cells, mouse 3T3 cells and rat PC12 cells was separated on a 7.5 % gel by SDS-PAGE, transferred to PVDF membrane and blocked in 5% non-fat milk in TBST. The membrane was probed with 2.0 ug/mL anti-DRP1 in blocking buffer and detected with an anti-rabbit HRP secondary antibody using chemiluminescence.](http://images.novusbio.com/fullsize/DRP1-Antibody-Western-Blot-NB110-55288-img0012.jpg "Western Blot: DRP1 Antibody [NB110-55288] - Total protein from human HeLa and MCF7 cells, mouse 3T3 cells and rat PC12 cells was separated on a 7.5 % gel by SDS-PAGE, transferred to PVDF membrane and blocked in 5% non-fat milk in TBST. The membrane was probed with 2.0 ug/mL anti-DRP1 in blocking buffer and detected with an anti-rabbit HRP secondary antibody using chemiluminescence.")
![Immunohistochemistry-Paraffin: DRP1 Antibody [NB110-55288] - Analysis of FFPE tissue section of mouse kidney using DRP1 antibody #NB110-55288 at 1:300. The primary antibody bound to DRP1 protein in the tissue section was detected using a HRP labeled secondary antibody and DAB reagent. Nuclei of the cells were counterstained with hematoxylin. This antibody generated a diffused cytoplasmic staining of DRP1 in the epithelial cells of various tubules and in the cells of glomeruli.](http://images.novusbio.com/fullsize/DRP1-Antibody-Immunohistochemistry-Paraffin-NB110-55288-img0013.jpg)
![<b>Genetic Strategies Validation. </b>Western Blot: DRP1 Antibody [NB110-55288] - Lane 1: DRP1 knockout. Lane 2: DRP1 wildtype MEFs. Stained with NB110-55288 at 1:500.](http://images.novusbio.com/fullsize/DRP1-Antibody-Western-Blot-NB110-55288-img0004.jpg)
![Immunocytochemistry/Immunofluorescence: DRP1 Antibody [NB110-55288] - HeLa cells were fixed for 10 minutes using 10% formalin and then permeabilized for 5 minutes using 1X PBS + 0.5% Triton X-100. The cells were incubated with anti-DRP1 at 5 ug/mL overnight at 4C and detected with an anti-rabbit Dylight 488 (Green) at a 1:500 dilution. Nuclei were counterstained with DAPI (Blue). Cells were imaged using a 40X objective.](http://images.novusbio.com/fullsize/DRP1-Antibody-Immunocytochemistry-Immunofluorescence-NB110-55288-img0015.jpg)
![Immunohistochemistry: DRP1 Antibody [NB110-55288] - Staining of renal tubular epithelium and visceral epithelial cells of the glomerulus. Human kidney cortex, 40X magnification.](http://images.novusbio.com/fullsize/DRP1-Antibody-Immunohistochemistry-NB110-55288-img0005.jpg)
![Western Blot: DRP1 Antibody [NB110-55288] - Assessment of skeletal muscle mitochondrial dynamic markers. Representative western blots. Significant main effect of training: #, p < 0.05; ##, p < 0.01. Significant post-hoc training effect: *, p < 0.05; **, p < 0.01. Data are presented as mean +/- SEM. Image collected and cropped by CiteAb from the following publication (null), licensed under a CC-BY license.](http://images.novusbio.com/fullsize/DRP1-Antibody-Western-Blot-NB110-55288-img0019.jpg)
![Immunocytochemistry/Immunofluorescence: DRP1 Antibody [NB110-55288] - PC12 cells were fixed for 10 minutes using 10% formalin and then permeabilized for 5 minutes using 1X PBS + 0.05% Triton-X100. The cells were incubated with anti-DRP1 Antibody at 2 ug/ml overnight at 4C and detected with an anti-rabbit Dylight 488 (Green) at a 1:500 dilution. Nuclei were counterstained with DAPI (Blue). Cells were imaged using a 40X objective.](http://images.novusbio.com/fullsize/DRP1-Antibody-Immunocytochemistry-Immunofluorescence-NB110-55288-img0017.jpg)
![Flow Cytometry: DRP1 Antibody [NB110-55288] - An intracellular stain was performed on HeLa cells with DRP1 Antibody NB110-55288AF488 (blue) and a matched isotype control (orange). Cells were fixed with 4% PFA and then permeabilized with 0.1% saponin. Cells were incubated in an antibody dilution of 5 ug/mL for 30 minutes at room temperature. Both antibodies were conjugated to Alexa Fluor 488.](http://images.novusbio.com/fullsize/DRP1-Antibody-Flow-Cytometry-NB110-55288-img0018.jpg)
![Western Blot: DRP1 Antibody [NB110-55288] - Rat spinal cord-DRP1 (81kda). Image from verified customer review.](http://images.novusbio.com/fullsize/DRP1-Antibody-Western-Blot-NB110-55288-img0007.jpg)
![Immunocytochemistry/Immunofluorescence: DRP1 Antibody [NB110-55288] - HeLa cells were fixed for 10 minutes using 10% formalin and then permeabilized for 5 minutes using 1X TBS + 0.5% Triton X-100. The cells were incubated with anti-DRP1 at 5.0 ug/mL overnight at 4C and detected with an anti-rabbit Dylight 488 (Green) at 1:500. Alpha tubulin (DM1A) NB100-690 was used as a co-stain at 1:1000 and detected with an anti-mouse Dylight 550 (Red) at 1:500. Nuclei were counterstained with DAPI (Blue). Cells were imaged using a 40X objective.](http://images.novusbio.com/fullsize/DRP1-Antibody-Immunocytochemistry-Immunofluorescence-NB110-55288-img0009.jpg)
![Immunocytochemistry/Immunofluorescence: DRP1 Antibody [NB110-55288] - NIH3T3 cells were fixed for 10 minutes using 10% formalin and then permeabilized for 5 minutes using 1X PBS + 0.05% Triton-X100. The cells were incubated with anti-DRP1 Antibody at 2 ug/ml overnight at 4C and detected with an anti-rabbit Dylight 488 (Green) at a 1:500 dilution. Nuclei were counterstained with DAPI (Blue). Cells were imaged using a 40X objective.](http://images.novusbio.com/fullsize/DRP1-Antibody-Immunocytochemistry-Immunofluorescence-NB110-55288-img0016.jpg)
![Flow Cytometry: DRP1 Antibody [NB110-55288] - An intracellular stain was performed on HeLa cells with NB110-55288 and a matched isotype control. Cells were fixed with 4% PFA and then permeablized with 0.1% saponin. Cells were incubated in an antibody dilution of 2.5 ug/mL for 30 minutes at room temperature, followed by Rabbit IgG (H+L) Cross-Adsorbed Secondary Antibody, Dylight 550.](http://images.novusbio.com/fullsize/DRP1-Antibody-Flow-Cytometry-NB110-55288-img0014.jpg)
![Simple Western: DRP1 Antibody [NB110-55288] - Image shows a specific band for DUX4 in 0.5 mg/mL of HeLa lysate. This experiment was performed under reducing conditions using the 12-230 kDa separation system.](http://images.novusbio.com/fullsize/DRP1-Antibody-Simple-Western-NB110-55288-img0008.jpg)
![Simple Western: DRP1 Antibody - BSA Free [NB110-55288] - Image shows a specific band for DRP1 in 0.1 ug/uL mouse hippocampus tissue lysate. Primary antibody dilution: 1:200. Image from verified customer review.](http://images.novusbio.com/fullsize/DRP1-Antibody---BSA-Free-Simple-Western-NB110-55288-img0020.jpg)
![Western Blot: Mitofusin 1 Antibody (3C9) [H00055669-M04] - Analysis of MFN1 expression in HepG2.](http://images.novusbio.com/fullsize/Mitofusin-1-Antibody-3C9-Western-Blot-H00055669-M04-img0005.jpg "Western Blot: Mitofusin 1 Antibody (3C9) [H00055669-M04] - Analysis of MFN1 expression in HepG2.")
![Western Blot: Mitofusin 1 Antibody (3C9) [H00055669-M04] - MFN1 monoclonal antibody (M04), clone 3C9 Western Blot analysis of MFN1 expression in HeLa ( Cat # L013V1 ).](http://images.novusbio.com/fullsize/Mitofusin-1-Antibody-3C9-Western-Blot-H00055669-M04-img0001.jpg)
![Western Blot: Mitofusin 1 Antibody (3C9) [H00055669-M04] - Western blot analysis of MFN1 over-expressed 293 cell line, cotransfected with MFN1 Validated Chimera RNAi or non-transfected control. Blot probed with H00055669-M04. GAPDH (36.1 kDa) used as loading control.](http://images.novusbio.com/fullsize/Mitofusin-1-Antibody-3C9-Western-Blot-H00055669-M04-img0003.jpg)
![Western Blot: Mitofusin 1 Antibody (3C9) [H00055669-M04] - Analysis of MFN1 expression in transfected 293T cell line by MFN1 monoclonal antibody (M04), clone 3C9. Lane 1: MFN1 transfected lysatE (84.2 KDa). Lane 2: Non-transfected lysate.](http://images.novusbio.com/fullsize/Mitofusin-1-Antibody-3C9-Western-Blot-H00055669-M04-img0006.jpg)
![ELISA: Mitofusin 1 Antibody (3C9) [H00055669-M04] - Detection limit for recombinant GST tagged MFN1 is 0.3 ng/ml as a capture antibody.](http://images.novusbio.com/fullsize/Mitofusin-1-Antibody-3C9-ELISA-H00055669-M04-img0007.jpg)
![Western Blot: Mitofusin 1 Antibody (11E9-1H12) [NBP1-71775] - Effect of AIF overexpression on mitochondrial fission and fusion in the cortex. Immunoblotting of OPA1 and Mitofusin 1 in the mitochondrial fraction from cortical tissue of the CL and IL hemispheres at 24 h after HI in WT and AIF Tg mice. The expression of Mitofusin 1 was significantly decreased at 24 h post-HI both in WT and AIF Tg mice, while the short form (82 kDa) and cleavage band of OPA1 were significantly increased at 24 h post-HI in both the WT and AIF Tg mice. Quantification of OPA1 and Mitofusin 1 did not show any significant differences in the CL and IL hemispheres between WT and AIF Tg mice (n=6/group). Image collected and cropped by CiteAb from the following publication (//www.nature.com/articles/s41419-020-2280-z), licensed under a CC-BY license.](http://images.novusbio.com/fullsize/Mitofusin-1-Antibody-11E9-1H12-Western-Blot-NBP1-71775-img0014.jpg "Western Blot: Mitofusin 1 Antibody (11E9-1H12) [NBP1-71775] - Effect of AIF overexpression on mitochondrial fission and fusion in the cortex. Immunoblotting of OPA1 and Mitofusin 1 in the mitochondrial fraction from cortical tissue of the CL and IL hemispheres at 24 h after HI in WT and AIF Tg mice. The expression of Mitofusin 1 was significantly decreased at 24 h post-HI both in WT and AIF Tg mice, while the short form (82 kDa) and cleavage band of OPA1 were significantly increased at 24 h post-HI in both the WT and AIF Tg mice. Quantification of OPA1 and Mitofusin 1 did not show any significant differences in the CL and IL hemispheres between WT and AIF Tg mice (n=6/group). Image collected and cropped by CiteAb from the following publication (//www.nature.com/articles/s41419-020-2280-z), licensed under a CC-BY license.")
![Immunocytochemistry/Immunofluorescence: Mitofusin 1 Antibody (11E9-1H12) [NBP1-71775] - Antibody was tested in 3T3 cells with DyLight 488 (green). Nuclei and alpha-tubulin were counterstained with DAPI (blue) and Dylight 550 (red).](http://images.novusbio.com/fullsize/Mitofusin-1-Antibody-11E9-1H12-Immunocytochemistry-Immunofluorescence-NBP1-71775-img0013.jpg)
![Immunohistochemistry-Paraffin: Mitofusin 1 Antibody (11E9-1H12) [NBP1-71775] - Analysis of Mitofusin-1 in mouse liver.](http://images.novusbio.com/fullsize/Mitofusin-1-Antibody-11E9-1H12-Immunohistochemistry-Paraffin-NBP1-71775-img0011.jpg)
![<b>Genetic Strategies Validation. </b>Western Blot: Mitofusin 1 Antibody (11E9-1H12) [NBP1-71775] - Analysis of Mitofusin-1 expression in (1) MEF wild-type and (2) MEF Mitofusin-1-null whole cell lysates using NBP1-71775.](http://images.novusbio.com/fullsize/Mitofusin-1-Antibody-11E9-1H12-Western-Blot-NBP1-71775-img0009.jpg)
![Western Blot: Mitofusin 1 Antibody (11E9-1H12) - BSA Free [NBP1-71775] - Effect of AIF overexpression on mitochondrial fission & fusion in the cortex.a Representative immunoblots of mitochondrial fission proteins (P-DRP1 & FIS1) in the mitochondrial fraction from cortical tissue of P9 WT & AIF Tg mice under physiological conditions. Quantification of P-DRP1 & FIS1 did not show a significant difference between WT & AIF Tg mice (n = 6/group). b Representative immunoblots of mitochondrial fusion proteins (OPA1 & MFN1) in the mitochondrial fraction from cortical tissue of P9 WT & AIF Tg mice under physiological conditions. Quantification of OPA1 & MFN1 did not show any significant difference between WT & AIF Tg mice (n = 6/group). c Immunoblotting of P-DRP1and FIS1 in the mitochondrial fraction from the cortical tissue of the CL & IL hemispheres in WT & AIF Tg mice at 24 h after HI. Quantification of P-DRP1 & FIS1 did not show any significant differences in the CL & IL hemispheres between WT & AIF Tg mice (n = 6/group). d Immunoblotting of OPA1 & MFN1 in the mitochondrial fraction from cortical tissue of the CL & IL hemispheres at 24 h after HI in WT & AIF Tg mice. The expression of MFN1 was significantly decreased at 24 h post-HI both in WT & AIF Tg mice, while the short form (82 kDa) & cleavage band of OPA1 were significantly increased at 24 h post-HI in both the WT & AIF Tg mice. Quantification of OPA1 & MFN1 did not show any significant differences in the CL & IL hemispheres between WT & AIF Tg mice (n = 6/group). Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/32001673), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nbp1-71775_mouse-monoclonal-mitofusin-1-antibody-11e9-1h12-310202416163735.jpg)
![Western Blot: Mitofusin 1 Antibody [NBP1-51841] - Densitometric analyses of protein expression levels relative to the sedentary group with representative image of western blot are shown. n = 5-6/group. Values are expressed by mean +/- SEM expressed as fold change relative to the sedentary group. * P < 0.05, significantly different from the sedentary group. Black bar: fetal hearts from sedentary dams; gray bar: fetal hearts from exercised dams. Image collected and cropped by CiteAb from the following publication (//www.ncbi.nlm.nih.gov/pmc/articles/PMC5350185/) licensed under a CC-BY license.](http://images.novusbio.com/fullsize/Mitofusin-1-Antibody-Western-Blot-NBP1-51841-img0010.jpg "Western Blot: Mitofusin 1 Antibody [NBP1-51841] - Densitometric analyses of protein expression levels relative to the sedentary group with representative image of western blot are shown. n = 5-6/group. Values are expressed by mean +/- SEM expressed as fold change relative to the sedentary group. * P < 0.05, significantly different from the sedentary group. Black bar: fetal hearts from sedentary dams; gray bar: fetal hearts from exercised dams. Image collected and cropped by CiteAb from the following publication (//www.ncbi.nlm.nih.gov/pmc/articles/PMC5350185/) licensed under a CC-BY license.")
![Immunocytochemistry/Immunofluorescence: Mitofusin 1 Antibody [NBP1-51841] - Mfn-1 expressed in mouse neural stem cells. Image from verified customer review.](http://images.novusbio.com/fullsize/Mitofusin-1-Antibody-Immunocytochemistry-Immunofluorescence-NBP1-51841-img0008.jpg)
![Immunohistochemistry: Mitofusin 1 Antibody [NBP1-51841] - IHC staining of Mfn1 in mouse intestine.](http://images.novusbio.com/fullsize/Mitofusin-1-Antibody-Immunohistochemistry-NBP1-51841-img0009.jpg)
![Immunocytochemistry/Immunofluorescence: Mitofusin 1 Antibody [NBP1-51841] - Mitofusin-1 antibody was tested in HeLa cells with DyLight 488 (green). Nuclei and alpha-tubulin were counterstained with DAPI (blue) and Dylight 550 (red).](http://images.novusbio.com/fullsize/Mitofusin-1-Antibody-Immunocytochemistry-Immunofluorescence-NBP1-51841-img0007.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: DRP1 Antibody (3B5) [H00010059-M01] - DNM1L monoclonal antibody (M01), clone 3B5 Analysis of DNM1L expression in K-562.](http://images.novusbio.com/fullsize/DRP1-Antibody-3B5-Western-Blot-H00010059-M01-img0008.jpg "Western Blot: DRP1 Antibody (3B5) [H00010059-M01] - DNM1L monoclonal antibody (M01), clone 3B5 Analysis of DNM1L expression in K-562.")
![Immunohistochemistry-Paraffin: DRP1 Antibody (3B5) [H00010059-M01] - Analysis of monoclonal antibody to DNM1L on formalin-fixed paraffin-embedded human leiomyosarcoma tissue. Antibody concentration 1 ug/ml.](http://images.novusbio.com/fullsize/DRP1-Antibody-3B5-Immunohistochemistry-Paraffin-H00010059-M01-img0006.jpg)
![Western Blot: DRP1 Antibody (3B5) [H00010059-M01] - Analysis of DNM1L expression in transfected 293T cell line by DNM1L monoclonal antibody (M01), clone 3B5.Lane 1: DNM1L transfected lysate(79 KDa).Lane 2: Non-transfected lysate.](http://images.novusbio.com/fullsize/DRP1-Antibody-3B5-Western-Blot-H00010059-M01-img0009.jpg)
![ELISA: DRP1 Antibody (3B5) [H00010059-M01] - Detection limit for recombinant GST tagged DNM1L is approximately 0.3ng/ml as a capture antibody.](http://images.novusbio.com/fullsize/DRP1-Antibody-3B5-Sandwich-ELISA-H00010059-M01-img0007.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)
![SDS-Page: Recombinant Human DRP1 Protein [H00010059-P01] - 12.5% SDS-PAGE Stained with Coomassie Blue.](http://images.novusbio.com/fullsize/Recombinant-Human-DRP1-Protein-SDS-Page-H00010059-P01-img0002.jpg "SDS-Page: Recombinant Human DRP1 Protein [H00010059-P01] - 12.5% SDS-PAGE Stained with Coomassie Blue.")
![Western Blot: DRP1 Antibody (4E11B11) [NBP2-23489] - Analysis using DRP1 mouse mAb in (1) A549 and (2) Jurkat cell lysates.](http://images.novusbio.com/fullsize/DRP1-Antibody-4E11B11-Western-Blot-NBP2-23489-img0003.jpg "Western Blot: DRP1 Antibody (4E11B11) [NBP2-23489] - Analysis using DRP1 mouse mAb in (1) A549 and (2) Jurkat cell lysates.")
![Immunohistochemistry: DRP1 Antibody (4E11B11) [NBP2-23489] - Analysis of paraffin-embedded human cerebellum tissues using DRP1 mouse mAb with DAB staining.](http://images.novusbio.com/fullsize/DRP1-Antibody-4E11B11-Immunohistochemistry-NBP2-23489-img0005.jpg)
![Western Blot: DRP1 Antibody (4E11B11) [NBP2-23489] - Analysis using DRP1 mAb in human DRP1 recombinant protein. (Expected MW is 41.8 kDa)](http://images.novusbio.com/fullsize/DRP1-Antibody-4E11B11-Western-Blot-NBP2-23489-img0001.jpg)
![Western Blot: DRP1 Antibody (4E11B11) [NBP2-23489] - Analysis using DRP1 mAb in (1) HEK293 and (2) DRP1 hIgGFc transfected HEK293 cell lysate.](http://images.novusbio.com/fullsize/DRP1-Antibody-4E11B11-Western-Blot-NBP2-23489-img0002.jpg)
![Immunohistochemistry: DRP1 Antibody (4E11B11) [NBP2-23489] - Analysis of paraffin-embedded human ovarian cancer tissues using DRP1 mouse mAb with DAB staining.](http://images.novusbio.com/fullsize/DRP1-Antibody-4E11B11-Immunohistochemistry-NBP2-23489-img0004.jpg)
![Western Blot: PINK1 Antibody [NB600-973] - Lane 1: The primary band with the observed molecular weight of 66 kDa was detected in mouse liver (30ug). Also, a truncated form of the protein at about 33 kDa was detected.](http://images.novusbio.com/fullsize/PINK1-Antibody-Western-Blot-NB600-973-img0001.jpg "Western Blot: PINK1 Antibody [NB600-973] - Lane 1: The primary band with the observed molecular weight of 66 kDa was detected in mouse liver (30ug). Also, a truncated form of the protein at about 33 kDa was detected.")
![Immunocytochemistry/Immunofluorescence: PINK1 Antibody [NB600-973] - LRRK2 accumulates in globules in alphaS tg mice. Double immunofluorescence for alphaS with parkin, PINK1, DJ-1, LRRK2, or negative control (the immunopeptide-preabsorbed anti-LRRK2 antibody) in alphaS tg mice. Scale bar = 5 um for all panels. Image collected and cropped by CiteAb from the following publication (//molecularbrain.biomedcentral.com/articles/10.1186/1756-6606-5-34) licensed under a CC-BY license.](http://images.novusbio.com/fullsize/PINK1-Antibody-Immunocytochemistry-Immunofluorescence-NB600-973-img0003.jpg)
![Immunohistochemistry-Paraffin: PINK1 Antibody [NB600-973] - Staining in human liver tissue using a 1:200 dilution.](http://images.novusbio.com/fullsize/PINK1-Antibody-Immunohistochemistry-Paraffin-NB600-973-img0002.jpg)
![Western Blot: VAP-B Antibody [NBP1-89112] - Analysis in human cell lines Caco-2 and HEK293 using anti-VAPB antibody. Corresponding VAPB RNA-seq data are presented for the same cell lines. Loading control: anti-COX4I1.](http://images.novusbio.com/fullsize/VAP-B-Antibody-Western-Blot-NBP1-89112-img0023.jpg "<b>Orthogonal Strategies Validation. </b>Western Blot: VAP-B Antibody [NBP1-89112] - Analysis in human cell lines Caco-2 and HEK293 using anti-VAPB antibody. Corresponding VAPB RNA-seq data are presented for the same cell lines. Loading control: anti-COX4I1.")
![<b>Orthogonal Strategies Validation. </b>Immunocytochemistry/Immunofluorescence: VAP-B Antibody [NBP1-89112] - Staining of human cell line U-2 OS shows positivity in endoplasmic reticulum. Antibody staining is shown in green.](http://images.novusbio.com/fullsize/VAP-B-Antibody-Immunocytochemistry-Immunofluorescence-NBP1-89112-img0021.jpg)
![Immunohistochemistry-Paraffin: VAP-B Antibody [NBP1-89112] - Staining of human small intestine shows strong cytoplasmic positivity in glandular cells.](http://images.novusbio.com/fullsize/VAP-B-Antibody-Immunohistochemistry-Paraffin-NBP1-89112-img0019.jpg)
![Western Blot: VAP-B Antibody [NBP1-89112] - Analysis in mouse cell line NIH-3T3 and rat cell line NBT-II.](http://images.novusbio.com/fullsize/VAP-B-Antibody-Western-Blot-NBP1-89112-img0007.jpg)
![Immunohistochemistry-Paraffin: VAP-B Antibody [NBP1-89112] - Staining of human cerebral cortex shows strong cytoplasmic positivity in neuronal cells.](http://images.novusbio.com/fullsize/VAP-B-Antibody-Immunohistochemistry-Paraffin-NBP1-89112-img0016.jpg)
![Immunohistochemistry-Paraffin: VAP-B Antibody [NBP1-89112] - Staining of human kidney shows moderate cytoplasmic positivity in cells in tubules.](http://images.novusbio.com/fullsize/VAP-B-Antibody-Immunohistochemistry-Paraffin-NBP1-89112-img0017.jpg)
![Immunohistochemistry-Paraffin: VAP-B Antibody [NBP1-89112] - Staining of human liver shows moderate cytoplasmic positivity in hepatocytes.](http://images.novusbio.com/fullsize/VAP-B-Antibody-Immunohistochemistry-Paraffin-NBP1-89112-img0018.jpg)