| Formulation | Catalog # | Availability | Price | |
|---|---|---|---|---|
| BSA Free | BC100-494SS | |||
| Formulation | Catalog # | Availability | Price | |
|---|---|---|---|---|
| Azide and BSA Free | NBP3-25980 | |||
| Conjugate | Catalog # | Availability | Size | Price |
|---|---|---|---|---|
| Biotin | NBP1-77728 | |||
| HRP | NBP1-77696 | |||
| Formulation | Catalog # | Availability | Price | |
|---|---|---|---|---|
| BSA Free | NBP1-82294-25ul | |||
![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: Phosphothreonine Antibody [NB110-96896] - Western blot analysis of Mouse brain cell lysates showing detection of Phosphothreonine protein using Rabbit Anti-Phosphothreonine Polyclonal Antibody (NB110-96896). Primary Antibody: Rabbit Anti-Phosphothreonine Polyclonal Antibody (NB110-96896) at 1:1000. Left: Treated with Vanadium, Right: Non-treated..](http://images.novusbio.com/fullsize/Phosphothreonine-Antibody-Western-Blot-NB110-96896-img0007.jpg "Western Blot: Phosphothreonine Antibody [NB110-96896] - Western blot analysis of Mouse brain cell lysates showing detection of Phosphothreonine protein using Rabbit Anti-Phosphothreonine Polyclonal Antibody (NB110-96896). Primary Antibody: Rabbit Anti-Phosphothreonine Polyclonal Antibody (NB110-96896) at 1:1000. Left: Treated with Vanadium, Right: Non-treated..")
![Immunocytochemistry/Immunofluorescence: Phosphothreonine Antibody [NB110-96896] - Human HeLa cells. Fixation: 2% Formaldehyde for 20 min at RT. Primary Antibody: Rabbit Anti-Phosphothreonine Polyclonal Antibody at 1:60 for 12 hours at 4C. Secondary Antibody: R-PE Goat Anti-Rabbit (yellow) at 1:200 for 2 hours at RT. Counterstain: DAPI (blue) nuclear stain at 1:40000 for 2 hours at RT. Localization: Cytoplasm. Nucleus. Magnification: 20x.](http://images.novusbio.com/fullsize/Phosphothreonine-Antibody-Immunocytochemistry-Immunofluorescence-NB110-96896-img0005.jpg)
![Immunocytochemistry/Immunofluorescence: Phosphothreonine Antibody [NB110-96896] - Human HeLa cells. Fixation: 2% Formaldehyde for 20 min at RT. Rabbit Anti-Phosphothreonine Polyclonal Antibody at 1:60 for 12 hours at 4C. Secondary Antibody: FITC Goat Anti-Rabbit (green) at 1:200 for 2 hours at RT. Counterstain: DAPI (blue) nuclear stain at 1:40000 for 2 hours at RT. Localization: Cytoplasm. Nucleus. Magnification: 100x.](http://images.novusbio.com/fullsize/Phosphothreonine-Antibody-Immunocytochemistry-Immunofluorescence-NB110-96896-img0004.jpg)
![Immunoprecipitation: Phosphothreonine Antibody (RM102) - Azide and BSA Free [NBP3-25980] - Immunoprecipitation of Calyculin A/Okadaic Acid treated A431 cells by clone RM102 rabbit Anti-Phosphothreonine mAb, at 1:500 dilution, and then blotted with RM102. (1) Whole lysate control; (2) IP by rabbit IgG control; (3) IP by RM102.](http://images.novusbio.com/fullsize/nbp3-25980_rabbit-phosphothreonine-mab-rm102-azide-and-bsa-free-22620242311086.jpg "Immunoprecipitation: Phosphothreonine Antibody (RM102) - Azide and BSA Free [NBP3-25980] - Immunoprecipitation of Calyculin A/Okadaic Acid treated A431 cells by clone RM102 rabbit Anti-Phosphothreonine mAb, at 1:500 dilution, and then blotted with RM102. (1) Whole lysate control; (2) IP by rabbit IgG control; (3) IP by RM102.")
![Immunocytochemistry/ Immunofluorescence: Phosphothreonine Antibody (RM102) - Azide and BSA Free [NBP3-25980] - Immunocytochemistry of serum-starved A431 cells nontreated or treated with Calyculin A/Okadaic Acid, using Clone RM102 at 1:500 dilution followed by a PE conjugated secondary antibody (red) and DAPI (blue).](http://images.novusbio.com/fullsize/nbp3-25980_rabbit-phosphothreonine-mab-rm102-azide-and-bsa-free-226202422174423.jpg)
![Western Blot: Phosphothreonine Antibody (RM102) - Azide and BSA Free [NBP3-25980] - Western blot of serum-starved A431 cells nontreated or treated with Calyculin A/Okadaic Acid, using Clone RM102 at 1:2000 dilution.](http://images.novusbio.com/fullsize/nbp3-25980_rabbit-phosphothreonine-mab-rm102-azide-and-bsa-free-2462024132611.jpg)
![Multiplex Immunoassay: Phosphothreonine Antibody (RM102) - Azide and BSA Free [NBP3-25980] - Clone RM102 recognizes Phosphorylated threonine in peptides with different sequences. It has minimal cross-reactivity with phosphorylated serine.](http://images.novusbio.com/fullsize/nbp3-25980_rabbit-phosphothreonine-mab-rm102-azide-and-bsa-free-22620242311037.jpg)
![Western Blot: Phosphothreonine Antibody (RM102) [NBP2-77398] - Western blot of serum-starved A431 cells nontreated or treated with Calyculin A/Okadaic Acid, using NBP2-77398.](http://images.novusbio.com/fullsize/Phosphothreonine-Antibody-RM102-Western-Blot-NBP2-77398-img0002.jpg "Western Blot: Phosphothreonine Antibody (RM102) [NBP2-77398] - Western blot of serum-starved A431 cells nontreated or treated with Calyculin A/Okadaic Acid, using NBP2-77398.")
![Immunocytochemistry/Immunofluorescence: Phosphothreonine Antibody (RM102) [NBP2-77398] - Immunocytochemistry of serum-starved A431 cells nontreated or treated with Calyculin A/Okadaic Acid, using NBP2-77398 (followed by a PE conjugated secondary antibody, red) and DAPI (blue).](http://images.novusbio.com/fullsize/Phosphothreonine-Antibody-RM102-Immunocytochemistry-Immunofluorescence-NBP2-77398-img0001.jpg)
![Multiplex Immunoassay: Phosphothreonine Antibody (RM102) [NBP2-77398] - NBP2-77398 recognizes Phosphorylated threonine in peptides with different sequences. It has minimal cross-reactivity with phosphorylated serine.](http://images.novusbio.com/fullsize/Phosphothreonine-Antibody-RM102-Multiplex-Immunoassay-NBP2-77398-img0004.jpg)
![Immunoprecipitation: Phosphothreonine Antibody (RM102) [NBP2-77398] - Immunoprecipitation of Calyculin A/Okadaic Acid treated A431 cells by NBP2-77398, and then blotted with NBP2-77398. (1) Whole lysate control; (2) IP by rabbit IgG control; (3) IP by NBP2-77398.](http://images.novusbio.com/fullsize/Phosphothreonine-Antibody-RM102-Immunoprecipitation-NBP2-77398-img0003.jpg)
![Western Blot: Phosphothreonine Antibody [NBP1-78035] - Goat anti Glucoamylase antibody was used to detect purified glucoamylase under reducing (R) and non-reducing (NR) conditions. Reduced samples of purified target proteins contained 4% BME and were boiled for 5 minutes. Samples of ~1ug of protein per lane.](http://images.novusbio.com/fullsize/Phosphothreonine-Antibody-Western-Blot-NBP1-78035-img0002.jpg "Western Blot: Phosphothreonine Antibody [NBP1-78035] - Goat anti Glucoamylase antibody was used to detect purified glucoamylase under reducing (R) and non-reducing (NR) conditions. Reduced samples of purified target proteins contained 4% BME and were boiled for 5 minutes. Samples of ~1ug of protein per lane.")
![Western Blot: Phosphothreonine Antibody [NBP1-78035] - shown to detect phosphorylated proteins present in mouse spleen cell lysates. Left Lane: extract of spleen from mouse treated with vanadium. Right lane: extract of spleen from untreated mouse.](http://images.novusbio.com/fullsize/Phosphothreonine-Antibody-Western-Blot-NBP1-78035-img0001.jpg)
![Western Blot: Phosphothreonine Antibody (18F6) [NB600-878] - Phospho Threonine monoclonal antibody, clone 18F6 is shown to detect threonine phosphorylation of proteins in a lysate from A-431 cells stimulated with EGF.](http://images.novusbio.com/fullsize/Phosphothreonine-Antibody-18F6-Western-Blot-NB600-878-img0003.jpg "Western Blot: Phosphothreonine Antibody (18F6) [NB600-878] - Phospho Threonine monoclonal antibody, clone 18F6 is shown to detect threonine phosphorylation of proteins in a lysate from A-431 cells stimulated with EGF.")
![ELISA: Phosphothreonine Antibody (18F6) [NB600-878] - was tested against BSA conjugates of phosphothreonine (grey squares), phosphotyrosine (black triangles) and phosphoserine (open circles). Each well was coated with 0.1 ug of conjugate. The starting dilution of antibody was 1/1000 and each point on the X axis represents a 2-fold dilution. For detection, an HRP-conjugated Goat anti-Mouse IgG was used as secondary antibody, with a TMB substrate. Absorbance is represented on the Y axis.](http://images.novusbio.com/fullsize/Phosphothreonine-Antibody-18F6-ELISA-NB600-878-img0004.jpg)
![Western Blot: Phosphothreonine Antibody (6K2H0) [NBP3-33576] - Western blot analysis of lysates from NIH 3T3 or NIH 3T3 treat with Calyculin A, using Phosphothreonine Rabbit mAb at 1:1000 dilution. NIH/3T3 cells were treated by Calyculin A (100 nM) at 37C for 30 minutes after serum-starvation overnight.Secondary antibody: HRP-conjugated Goat anti-Rabbit IgG (H+L) at 1:10000 dilution.Lysates/proteins: 25ug per lane.Blocking buffer: 3% nonfat dry milk in TBST.Detection: ECL Enhanced Kit.Exposure time: 60s.](http://images.novusbio.com/fullsize/nbp3-33576_rabbit-phosphothreonine-mab-6k2h0-912202415171146.jpg "Western Blot: Phosphothreonine Antibody (6K2H0) [NBP3-33576] - Western blot analysis of lysates from NIH 3T3 or NIH 3T3 treat with Calyculin A, using Phosphothreonine Rabbit mAb at 1:1000 dilution. NIH/3T3 cells were treated by Calyculin A (100 nM) at 37C for 30 minutes after serum-starvation overnight.Secondary antibody: HRP-conjugated Goat anti-Rabbit IgG (H+L) at 1:10000 dilution.Lysates/proteins: 25ug per lane.Blocking buffer: 3% nonfat dry milk in TBST.Detection: ECL Enhanced Kit.Exposure time: 60s.")
![Western Blot: Phosphothreonine Antibody (6K2H0) [NBP3-33576] - Western blot analysis of lysates from A-431, using Phosphothreonine Rabbit mAb at 1:1000 dilution. A 431 treated by Calyculin A (100 nM) at 37C for 30 minutes after serum-starvation overnight.Secondary antibody: HRP-conjugated Goat anti-Rabbit IgG (H+L) at 1:10000 dilution.Lysates/proteins: 25ug per lane.Blocking buffer: 3% nonfat dry milk in TBST.Detection: ECL Enhanced Kit.Exposure time: 60s.](http://images.novusbio.com/fullsize/nbp3-33576_rabbit-phosphothreonine-mab-6k2h0-91220241512131.jpg)
![Western Blot: MED12 Antibody [NB100-2357] - Components from all modules of Mediator are found in TAP-wtICP4 samples. Western blot analysis of nuclear extracts (NE) or affinity purified (PD) samples using either wtICP4 (KOS) or TAP-wtICP4 (TAP) expressing viruses at 6 hpi. Results of the Western blot analysis for components of the head (Med6), middle (Med4 and Med1), tail (Med23), kinase (cdk8, Med12, and Med13), and the Med26 protein are shown. Image collected and cropped by CiteAb from the following publication (//dx.plos.org/10.1371/journal.pone.0078242), licensed under a CC-BY license.](http://images.novusbio.com/fullsize/MED12-Antibody-Western-Blot-NB100-2357-img0015.jpg "Western Blot: MED12 Antibody [NB100-2357] - Components from all modules of Mediator are found in TAP-wtICP4 samples. Western blot analysis of nuclear extracts (NE) or affinity purified (PD) samples using either wtICP4 (KOS) or TAP-wtICP4 (TAP) expressing viruses at 6 hpi. Results of the Western blot analysis for components of the head (Med6), middle (Med4 and Med1), tail (Med23), kinase (cdk8, Med12, and Med13), and the Med26 protein are shown. Image collected and cropped by CiteAb from the following publication (//dx.plos.org/10.1371/journal.pone.0078242), licensed under a CC-BY license.")
![Immunohistochemistry: MED12 Antibody [NB100-2357] - Representative examples of immunohistochemically stained sections positive for MED12 (A, B and C) in tumor specimens. Examples are from the same patients, respectively. A. TS = 5, B. TS = 6, C. TS = 6 (x20 original magnification [A, B and C]. Scale bars represent 100 um. TS, total score = intensity score (0-3) plus proportion score (0-3). Image collected and cropped by CiteAb from the following publication (//www.oncotarget.com/abstract/14410), licensed under a CC-BY license.](http://images.novusbio.com/fullsize/MED12-Antibody-Immunohistochemistry-NB100-2357-img0014.jpg)
![Western Blot: MED12 Antibody [NB100-2357] - Samples: Whole cell lysate (10 ug) from NIH 3T3, CT26, CH27, TCMK-1, and BW5147.3 cells prepared using NETN lysis buffer. Antibody: Affinity purified rabbit anti-Med12 antibody (NB100-2357 lot 3) used for WB at 0.04 ug/ml. Detection: Chemiluminescence with an exposure time of 10 seconds.](http://images.novusbio.com/fullsize/nb100-2357_rabbit-polyclonal-med12-antibody-4122023957332.jpg)
![Western Blot: MED12 Antibody [NB100-2357] - Samples: Whole cell lysate (10 ug) from HeLa, A-549, GaMG, Hep-G2, and K-562 cells prepared using NETN lysis buffer. Antibody: Affinity purified rabbit anti-Med12 antibody (NB100-2357 lot 3) used for WB at 0.04 ug/ml. Detection: Chemiluminescence with an exposure time of 10 seconds.](http://images.novusbio.com/fullsize/nb100-2357_rabbit-polyclonal-med12-antibody-4122023957333.jpg)
![Immunohistochemistry-Paraffin: MED12 Antibody [NB100-2357] - Sample: FFPE section of human prostate carcinoma. Antibody: Affinity purified rabbit anti-MED12 (NB100-2357 Lot 3) used at a dilution of 1:5,000 (0.2ug/ml). Detection: DAB](http://images.novusbio.com/fullsize/nb100-2357_rabbit-polyclonal-med12-antibody-4122023957330.jpg)
![Western Blot: MED12 Antibody [NB100-2357] - Samples: Whole cell lysate (1.0 mg per IP reaction; 20% of IP loaded) from HeLa cells prepared using NETN lysis buffer. Antibodies: Affinity purified rabbit anti-Med12 antibody (NB100-2357 lot 3) used for IP at 6 ug per reaction. Med12 was also immunoprecipitated by a previous lot of this antibody (NB100-2357 lot 2) and a second antibody against a different epitope of Med12 (NBP2-80138). For blotting immunoprecipitated Med12, NB100-2357 was used at 0.04 ug/ml. Detection: Chemiluminescence with an exposure time of 1 second.](http://images.novusbio.com/fullsize/nb100-2357_rabbit-polyclonal-med12-antibody-4122023957334.jpg)
![Immunohistochemistry-Paraffin: MED12 Antibody [NB100-2357] - Sample: FFPE section of mouse renal cell carcinoma. Antibody: Affinity purified rabbit anti-MED12 (NB100-2357 Lot 3) used at a dilution of 1:1,000 (1ug/ml). Detection: DAB](http://images.novusbio.com/fullsize/nb100-2357_rabbit-polyclonal-med12-antibody-4122023957331.jpg)
![Western Blot: TARS2 Antibody [NBP1-82294] - Lane 1: NIH-3T3 cell lysate (Mouse embryonic fibroblast cells). Lane 2: NBT-II cell lysate (Rat Wistar bladder tumor cells).](http://images.novusbio.com/fullsize/TARS2-Antibody-Western-Blot-NBP1-82294-img0007.jpg "Western Blot: TARS2 Antibody [NBP1-82294] - Lane 1: NIH-3T3 cell lysate (Mouse embryonic fibroblast cells). Lane 2: NBT-II cell lysate (Rat Wistar bladder tumor cells).")
![Immunocytochemistry/Immunofluorescence: TARS2 Antibody [NBP1-82294] - Immunofluorescent staining of human cell line U-2 OS shows localization to nucleoplasm, cytosol & intermediate filaments.](http://images.novusbio.com/fullsize/TARS2-Antibody-Immunocytochemistry-Immunofluorescence-NBP1-82294-img0008.jpg)
![Immunohistochemistry-Paraffin: TARS2 Antibody [NBP1-82294] - Staining of human heart muscle shows strong nuclear and cytoplasmic positivity in myocytes.](http://images.novusbio.com/fullsize/TARS2-Antibody-Immunohistochemistry-Paraffin-NBP1-82294-img0009.jpg)
![Western Blot: TARS2 Antibody [NBP1-82294] - Lane 1: Marker [kDa] 230, 130, 95, 72, 56, 36, 28, 17, 11. Lane 2: Human cell line RT-4. Lane 3: Human cell line U-251MG sp](http://images.novusbio.com/fullsize/TARS2-Antibody-Western-Blot-NBP1-82294-img0005.jpg)
![Western Blot: TARS2 Antibody [NBP2-20568] - Sample (30 ug of whole cell lysate) A: Hela 7. 5% SDS PAGE gel, diluted at 1:1000.](http://images.novusbio.com/fullsize/TARS2-Antibody-Western-Blot-NBP2-20568-img0001.jpg "Western Blot: TARS2 Antibody [NBP2-20568] - Sample (30 ug of whole cell lysate) A: Hela 7. 5% SDS PAGE gel, diluted at 1:1000.")
![Immunohistochemistry-Paraffin: TARS2 Antibody [NBP2-20568] - Immunohistochemical analysis of paraffin-embedded GASTRIC CA, using antibody at 1:500 dilution.](http://images.novusbio.com/fullsize/TARS2-Antibody-Immunohistochemistry-Paraffin-NBP2-20568-img0002.jpg)
![Western Blot: TARS2 Antibody [H00080222-B01P] - Analysis of TARSL1 expression in human kidney.](http://images.novusbio.com/fullsize/TARS2-Antibody-Western-Blot-H00080222-B01P-img0001.jpg "Western Blot: TARS2 Antibody [H00080222-B01P] - Analysis of TARSL1 expression in human kidney.")
![Western Blot: TARS2 Antibody [H00080222-B01P] - Analysis of TARS2 expression in transfected 293T cell line by TARS2 polyclonal antibody. Lane 1: TARSL1 transfected lysate(78.98 KDa). Lane 2: Non-transfected lysate.](http://images.novusbio.com/fullsize/TARS2-Antibody-Western-Blot-H00080222-B01P-img0002.jpg)