| Formulation | Catalog # | Availability | Price | |
|---|---|---|---|---|
| BSA Free | NB400-148SS | |||
| Formulation | Catalog # | Availability | Price | |
|---|---|---|---|---|
| BSA Free | NBP1-49678SS | |||
| Formulation | Catalog # | Availability | Price | |
|---|---|---|---|---|
| BSA Free | NB300-164SS | |||
| Azide and BSA Free | NBP2-80593 | |||
| Formulation | Catalog # | Availability | Price | |
|---|---|---|---|---|
| BSA Free | NB100-493SS | |||
| Formulation | Catalog # | Availability | Price | |
|---|---|---|---|---|
| BSA Free | NB110-55290SS | |||
| Formulation | Catalog # | Availability | Price | |
|---|---|---|---|---|
| Azide and BSA Free | NBP2-80652-0.1mg | |||
| BSA Free | NB100-77417SS | |||
| Azide and BSA Free | NBP2-80652 | |||
| Formulation | Catalog # | Availability | Price | |
|---|---|---|---|---|
| BSA Free | NB110-55288SS | |||
| Formulation | Catalog # | Availability | Price | |
|---|---|---|---|---|
| BSA Free | NB300-130SS | |||
| Formulation | Catalog # | Availability | Price | |
|---|---|---|---|---|
| BSA Free | NB300-268SS | |||
| Formulation | Catalog # | Availability | Price | |
|---|---|---|---|---|
| BSA Free | NB600-1335SS | |||
| Azide and BSA Free | NBP2-80745 | |||
![Western Blot: Niemann-Pick C1 Antibody - BSA Free [NB400-148] - NPC proteins in mouse lungs. Western blot of wild type (W) littermates, NPC1 (Mut) or NPC2 (Mut) mutant mouse lungs using anti-NPC1 or -NPC2 antibody. beta-actin used as a loading control. 30 ug protein/lane. Image collected and cropped by CiteAb from the following publication (//dx.plos.org/10.1371/journal.pone.0067084), licensed under a CC-BY license.](http://images.novusbio.com/fullsize/Niemann-Pick-C1-Antibody---BSA-Free-Western-Blot-NB400-148-img0015.jpg "Western Blot: Niemann-Pick C1 Antibody - BSA Free [NB400-148] - NPC proteins in mouse lungs. Western blot of wild type (W) littermates, NPC1 (Mut) or NPC2 (Mut) mutant mouse lungs using anti-NPC1 or -NPC2 antibody. beta-actin used as a loading control. 30 ug protein/lane. Image collected and cropped by CiteAb from the following publication (//dx.plos.org/10.1371/journal.pone.0067084), licensed under a CC-BY license.")
![Immunocytochemistry/Immunofluorescence: Niemann-Pick C1 Antibody - BSA Free [NB400-148] - NPC1 antibody was tested in HeLa cells with DyLight 488 (green). Nuclei were counterstained with DAPI (blue).](http://images.novusbio.com/fullsize/Niemann-Pick-C1-Antibody---BSA-Free-Immunocytochemistry-Immunofluorescence-NB400-148-img0010.jpg)
![Immunohistochemistry-Paraffin: Niemann-Pick C1 Antibody - BSA Free [NB400-148] - Staining of human brain, cortex, neurons and astrocytes.](http://images.novusbio.com/fullsize/Niemann-Pick-C1-Antibody---BSA-Free-Immunohistochemistry-Paraffin-NB400-148-img0011.jpg)
![Western Blot: Niemann-Pick C1 Antibody - BSA Free [NB400-148] - Protein expression analysis of normal and NPC-deficient cells after HIV-1 infection. Cells were uninfected or infected with VSVG-HIV-1 and harvested 96 h post-infection. NPC2, NPC1, and beta-actin protein expression was detected via Western blotting in uninfected and infected cells. Gag expression was also detected in the infected cells. Image collected and cropped by CiteAb from the following publication (//virologyj.biomedcentral.com/articles/10.1186/1743-422X-9-31), licensed under a CC-BY license.](http://images.novusbio.com/fullsize/Niemann-Pick-C1-Antibody---BSA-Free-Western-Blot-NB400-148-img0016.jpg)
![<b>Biological Strategies Validation. </b>Immunocytochemistry/Immunofluorescence: Niemann-Pick C1 Antibody - BSA Free [NB400-148] - Immunocytochemical staining with corresponding colocalization analysis of ALIX (green) and NPC-1 (red) in fibroblasts exposed to LLOMe for 15 min. Nuclei are stained with DAPI (blue) and merged images show colocalization in yellow (n = 5). Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/32409651/) licensed under a CC-BY license.](http://images.novusbio.com/fullsize/Niemann-Pick C1 Antibody - BSA Free-Immunocytochemistry-Immunofluorescence-NB400-148-img0017.jpg)
![<b>Genetic Strategies Validation. </b>Western Blot: Niemann-Pick C1 Antibody - BSA Free [NB400-148] - Western blot shows lysates of HeLa human cervical epithelial carcinoma parental cell line and NPC1 knockout (KO) HeLa cell line. PVDF membrane was probed with 1:1000 of Rabbit Anti-Human NPC1 Polyclonal Antibody (Catalog # NB400-148) followed by HRP-conjugated Anti-Rabbit IgG Secondary Antibody (Catalog #HAF008). Specific band was detected for NPC1 at approximately 240-260 kDa (as indicated) in the parental HeLa cell line, but is not detectable in the knockout HeLa cell line. This experiment was conducted under reducing conditions.](http://images.novusbio.com/fullsize/Niemann-Pick-C1-Antibody---BSA-Free-Knockout-Validated-NB400-148-img0014.jpg)
![<b>Genetic Strategies Validation. </b>Western Blot: Niemann-Pick C1 Antibody - BSA Free [NB400-148] - HeLa lysate, BHK lysate, A431 lysate tested at 1:1000. Image from verified customer review.](http://images.novusbio.com/fullsize/Niemann-Pick-C1-Antibody---BSA-Free-Knockdown-Validated-NB400-148-img0012.jpg)
![Immunocytochemistry/ Immunofluorescence: Niemann-Pick C1 Antibody - BSA Free [NB400-148] - ESCRT complex recruited to LLOMe-damaged lysosomes promotes cell survival.Human fibroblasts were exposed to 1 mM LLOMe & when indicated, the cell permeable calcium chelator BAPTA-AM (1 µM) was added 10 min prior to LLOMe exposure. Immunocytochemical staining with corresponding colocalization analysis of a CHMP4B (green) & LAMP2 (red), b ALIX (green) & NPC-1 (red), & c CHMP4B (green) & LAMP2 (red) in fibroblasts exposed to LLOMe for 15 min. Nuclei are stained with DAPI (blue) & merged images show colocalization in yellow (n = 5). d Caspase-3 like activity in cells exposed to LLOMe for 8 h (n = 3). e Quantification of apoptotic & necrotic cells using Annexin V/PI staining in fibroblasts exposed to LLOMe for 6 h (n = 3). f Immunoblot of LAMP2 in digitonin-extracted cytosolic fractions from cells exposed to LLOMe for 2 h (n = 8) with corresponding quantitative analysis. *p < 0.05, **p < 0.01 & ***p < 0.001 compared to control (a–b) or LLOMe only (c–f). Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/32409651), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb400-148_rabbit-polyclonal-niemann-pick-c1-antibody-310202416165630.jpg)
![Western Blot: Niemann-Pick C1 Antibody - BSA Free [NB400-148] - Expression of proteins involved in extracellular lipid uptake & intracellular cholesterol trafficking following JQ1 (0.4 µM) administration to HepG2 cells for 48 hours. (A) Representative Western blot (left panel) & densitometric analysis (right panel) of SR-B1. n = 6 independent experiments. (B) Immunofluorescence analysis of SR-B1 (green). Nuclei were counterstained with DAPI. n = 3 different experiments. Scale bar: 50 µm. (C) Representative Western blot (left panel) & densitometric analysis (right panel) of LDLr. n = 5 independent experiments. (D) LDLr immunofluorescence (green). Nuclei were counterstained with DAPI. n = 3 different experiments. (E–F) Representative Western blots & densitometric analysis of NPC1 & TMEM97. Tubulin was chosen as loading control. n = 6 independent experiments. Data represent means ± SD. Statistical analysis was performed by using unpaired Student’s t test. ** p < 0.01; *** p < 0.001. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/32075110), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb400-148_rabbit-polyclonal-niemann-pick-c1-antibody-310202416163786.jpg)
![Western Blot: Niemann-Pick C1 Antibody - BSA Free [NB400-148] - Effects of p75NTR modulation by LM11A-31 on cholesterol metabolism & secretion. (A–D) Representative Western blot & densitometric analysis of HMGCR, ABCA1, NPC1, & ApoE in U373 cells treated with vehicle (Ctrl) & LM11A-31 (0.1 µM) for 48 h. n = 4 different experiments. Vinculin served as a housekeeping protein to normalize protein loading. (E) Quantification of ApoE amount (µg/mL) by ELISA assay in culture medium from vehicle- & LM11A-31-treated U373 cells. n = 3 different experiments. (F) Cholesterol quantification (total cholesterol, free cholesterol, & cholesteryl esters) in the culture medium of U373 cells treated with vehicle (Ctrl) & LM11A-31 (0.1 µM) for 48 h. n = 3 different experiments. Data represent means ± SD. Statistical analysis was carried out by using unpaired Student’s t test. *** p < 0.001. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/35563230), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb400-148_rabbit-polyclonal-niemann-pick-c1-antibody-31020241616058.jpg)
![Immunocytochemistry/Immunofluorescence: PINK1 Antibody [NBP1-49678] - PINK1 antibody was tested in HepG2 cells with DyLight 488 (green). Nuclei and alpha-tubulin were counterstained with DAPI (blue) and DyLight 550 (red).](http://images.novusbio.com/fullsize/PINK1-Antibody-Immunocytochemistry-Immunofluorescence-NBP1-49678-img0002.jpg "Immunocytochemistry/Immunofluorescence: PINK1 Antibody [NBP1-49678] - PINK1 antibody was tested in HepG2 cells with DyLight 488 (green). Nuclei and alpha-tubulin were counterstained with DAPI (blue) and DyLight 550 (red).")
![Simple Western: PINK1 Antibody [NBP1-49678] - Lane view shows a specific band for PINK1 at a dilution of 1:50 in 1.0 mg/ml of HeLa lysate. Molecular weight ~61kDa. This experiment was performed under reducing conditions using the 12-230kDa separation system. * Non-specific interaction with the 230 kDa Simple Western standard may be seen with this antibody.](http://images.novusbio.com/fullsize/PINK1-Antibody-Simple-Western-NBP1-49678-img0006.jpg)
![Immunohistochemistry-Paraffin: PINK1 Antibody [NBP1-49678] - Stain in paraffin embedded mouse brain.](http://images.novusbio.com/fullsize/PINK1-Antibody-Immunohistochemistry-Paraffin-NBP1-49678-img0004.jpg)
![Immunocytochemistry/Immunofluorescence: PINK1 Antibody [NBP1-49678] - PINK1 antibody was tested at 1:50 in HeLa cells with DyLight 488 (green). Nuclei and alpha-tubulin were counterstained with DAPI (blue) and DyLight 550 (red). Image objective 40x.](http://images.novusbio.com/fullsize/PINK1-Antibody-Immunocytochemistry-Immunofluorescence-NBP1-49678-img0005.jpg)
![Western Blot: Bestrophin 1 Antibody (E6-6) - BSA Free [NB300-164] - Western blot analysis of the normal and mutant human Best1 protein in transiently transfected MDCK cells. Best1 proteins are detectable as a 68 kDa band in all transfected cells, but not in non-transfected controls (MDCK lane). Actin bands are shown to indicate equal loading of cell lysates. Image collected and cropped by CiteAb from the following publication (//www.mdpi.com/1422-0067/14/7/15121), licensed under a CC-BY license.](http://images.novusbio.com/fullsize/Bestrophin-1-Antibody-E6-6-BSA-Free-Western-Blot-NB300-164-img0007.jpg "Western Blot: Bestrophin 1 Antibody (E6-6) - BSA Free [NB300-164] - Western blot analysis of the normal and mutant human Best1 protein in transiently transfected MDCK cells. Best1 proteins are detectable as a 68 kDa band in all transfected cells, but not in non-transfected controls (MDCK lane). Actin bands are shown to indicate equal loading of cell lysates. Image collected and cropped by CiteAb from the following publication (//www.mdpi.com/1422-0067/14/7/15121), licensed under a CC-BY license.")
![Immunocytochemistry/Immunofluorescence: Bestrophin 1 Antibody (E6-6) - BSA Free [NB300-164] - X-Z confocal single image scan of transiently transfected cells with different BEST1 cDNA constructs showing mislocalization of mutants Y85H, Q96R, L100R and Y227N. Cells were stained for Best1 (green), beta-catenin (red) and nuclei (blue). Scale bar = 10 um. Image collected and cropped by CiteAb from the following publication (//www.mdpi.com/1422-0067/14/7/15121), licensed under a CC-BY license.](http://images.novusbio.com/fullsize/Bestrophin-1-Antibody-E6-6-BSA-Free-Immunocytochemistry-Immunofluorescence-NB300-164-img0008.jpg)
![Immunohistochemistry-Paraffin: Bestrophin 1 Antibody (E6-6) - BSA Free [NB300-164] - Bestrophin 1 was detected in immersion fixed paraffin sections of human small intestine using t Mouse Anti-Human Bestrophin 1 Monoclonal Antibody (Catalog # NB300-164) at 5 ug/mL for 1 hour at room temperature followed by incubation with the Anti-Mouse IgG VisUCyte™ HRP Polymer Antibody (Catalog # VC001). Tissue was stained using DAB (brown) and counterstained with hematoxylin (blue). Specific staining was localized to the cell surface and extracellular.](http://images.novusbio.com/fullsize/Bestrophin-1-Antibody-E6-6-BSA-Free-Immunohistochemistry-Paraffin-NB300-164-img0005.jpg)
![Western Blot: Bestrophin 1 Antibody (E6-6) - BSA Free [NB300-164] - Detection of Bestrophin (68 kDa) from human RPE cell lysate.](http://images.novusbio.com/fullsize/Bestrophin-1-Antibody-E6-6-BSA-Free-Western-Blot-NB300-164-img0003.jpg)
![Immunohistochemistry-Paraffin: Bestrophin 1 Antibody (E6-6) - BSA Free [NB300-164] - Bestrophin 1 was detected in immersion fixed paraffin-embedded sections of human brain using Mouse Anti-Human Bestrophin 1 (E6-6) Monoclonal Antibody (Catalog # NB300-164) at 1:300 for 1 hour at room temperature followed by incubation with the Anti-Mouse IgG VisUCyte™ HRP Polymer Antibody (Catalog # VC001). Tissue was stained using DAB (brown) and counterstained with hematoxylin (blue). Specific staining was localized to the cytoplasm in neurons.](http://images.novusbio.com/fullsize/Bestrophin-1-Antibody-E6-6-BSA-Free-Immunohistochemistry-Paraffin-NB300-164-img0004.jpg)
![<b>Genetic Strategies Validation. </b>Western Blot: Bestrophin 1 Antibody (E6-6) - BSA Free [NB300-164] - Immunoblotting showing the expression of RPE-specific proteins BEST1 (NB300-164), RPE65 (NB100-355), CRALBP, and the loading control beta-Actin in iPSC-RPE cells. Two gels/blots in the same panel were prepared from the same cell lysate of each PSC-RPE to detect BEST1 + beta-Actin, and RPE65 + CRALBP, respectively. Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/34061021/) licensed under a CC-BY license.](http://images.novusbio.com/fullsize/Bestrophin-1-Antibody-E6-6-BSA-Free-Knockout-Validated-NB300-164-img0009.jpg)
![Dual RNAscope ISH-IHC: Bestrophin 1 Antibody (E6-6) - BSA Free [NB300-164] - Formalin-fixed paraffin-embedded tissue sections of human duodenum were probed for Bestrophin 1 mRNA (ACD RNAScope Probe, catalog # 433181; Fast Red chromogen, ACD catalog # 322360). Adjacent tissue section was processed for immunohistochemistry using mouse anti-human (Novus Biologicals catalog # NB300-164) at 0.3ug/mL with overnight incubation at 4 degrees Celsius followed by incubation with anti-mouse IgG VisUCyte HRP Polymer Antibody (Catalog # VC001) and DAB chromogen (yellow-brown). Tissue was counterstained with hematoxylin (blue). IHC signal is confined to cytoplasm.](http://images.novusbio.com/fullsize/Bestrophin-1-Antibody-E6-6-BSA-Free-Dual-RNAscope-ISH-IHC-NB300-164-img0006.jpg)
![Western Blot: Bestrophin 1 Antibody (E6-6) - BSA Free [NB300-164] - (a) Schematic drawing showing localization of the different mutations (black diamonds) tested in our study (modified from [12]); (b) Western blot analysis of the normal & mutant human Best1 protein in transiently transfected MDCK cells. Best1 proteins are detectable as a 68 kDa band in all transfected cells, but not in non-transfected controls (MDCK lane). Actin bands are shown to indicate equal loading of cell lysates. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/23880862), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb300-164_mouse-monoclonal-bestrophin-1-antibody-e6-6-31020241534336.jpg)
![Immunocytochemistry/ Immunofluorescence: Bestrophin 1 Antibody (E6-6) - BSA Free [NB300-164] - Subcellular localization of WT & mutant BEST1 in iPSC-RPEs. Confocal images showing the co-staining of BEST1, Collagen IV & Hoechst in iPSC-RPEs derived from a WT donor or patients. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31836750), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb300-164_mouse-monoclonal-bestrophin-1-antibody-e6-6-310202415363746.jpg)
![Western Blot: Bestrophin 1 Antibody (E6-6) - BSA Free [NB300-164] - (a) HPRT & BEST1 mRNAs are expressed in MDCK & RPE-J cells. M–100 bp ladder, N–negative control; (b) Quantification of BEST1 expression levels between MDCK & RPE-J cells using quantitative Real-Time PCR. Fold change variation in BEST1 expression levels is reported as 2^-delta delta Ct value, the reference mRNA being HPRT (mean ± SEM., n = 2); (c) Western blot analysis—Best1 protein is not synthesized by RPE-J or MDCK cells. After transfection, MDCK produce human Best1 at 68 kDa. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/23880862), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb300-164_mouse-monoclonal-bestrophin-1-antibody-e6-6-310202415284544.jpg)
![Immunocytochemistry/ Immunofluorescence: Bestrophin 1 Antibody (E6-6) - BSA Free [NB300-164] - Characterization of WT iPSC & iPSC-RPE.(A) Phase picture of established WT iPSC line before differentiation. Scale bar, 400 μm. (B) Immunocytofluorescence images of pluripotency markers in established iPSC. Scale bar, 200 μm. (C) Confocal images showing plasma membrane localization of BEST1. Scale bar, 10 μm. (D) Comparison of current amplitudes in iPSC-RPEs from two BEST1 WT donors. Bar chart showing the steady-state current amplitudes at 0 [Ca2+]i, 1.2 μM [Ca2+]i, & 1.2 μM [Ca2+]i + 100 μM NFA in RPEs from two distinct BEST1 WT human donors; n = 5–6. ∗$p<0.05 compared to current amplitudes at 1.2 μM [Ca2+]i from donor #1 & #2, respectively, using two-tailed unpaired Student t test. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/29063836), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb300-164_mouse-monoclonal-bestrophin-1-antibody-e6-6-31020241535684.jpg)
![Western Blot: Bestrophin 1 Antibody (E6-6) - BSA Free [NB300-164] - CRISPR/Cas9-mediated gene silencing in combination with augmentation.(a) Augmented BEST1-GFP & endogenous BEST1 were detected by immunoblotting in hPSC-RPE cells. (b) Schematic of the baculovirus-based silencing (BVSi) vector. (c) Immunoblotting showing the knockdown of endogenous BEST1 expression with BVSi vectors & augmentation of wobble BEST1-mCherry in WT hPSC-RPE cells. (d) Immunoblotting showing the knockdown of endogenous BEST1 expression with BVSi 3–8 & augmentation of wobble BEST1-mCherry in hPSC-RPE cells carrying BEST1 gain-of-function mutations. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/34061021), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb300-164_mouse-monoclonal-bestrophin-1-antibody-e6-6-31020241537190.jpg)
![Western Blot: Bestrophin 1 Antibody (E6-6) - BSA Free [NB300-164] - CRISPR/Cas9-mediated gene silencing in combination with augmentation.(a) Augmented BEST1-GFP & endogenous BEST1 were detected by immunoblotting in hPSC-RPE cells. (b) Schematic of the baculovirus-based silencing (BVSi) vector. (c) Immunoblotting showing the knockdown of endogenous BEST1 expression with BVSi vectors & augmentation of wobble BEST1-mCherry in WT hPSC-RPE cells. (d) Immunoblotting showing the knockdown of endogenous BEST1 expression with BVSi 3–8 & augmentation of wobble BEST1-mCherry in hPSC-RPE cells carrying BEST1 gain-of-function mutations. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/34061021), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb300-164_mouse-monoclonal-bestrophin-1-antibody-e6-6-31020241539730.jpg)
![Western Blot: Bestrophin 1 Antibody (E6-6) - BSA Free [NB300-164] - Expression of RPE-specific marker proteins in hPSC-RPE & iPSC-RPE cells.(a–b) Immunoblotting showing the expression of RPE-specific proteins BEST1, RPE65, CRALBP, & the loading control beta -Actin in hPSC-RPE (a) & iPSC-RPE (b) cells. Two gels/blots in the same panel were prepared from the same cell lysate of each PSC-RPE to detect BEST1 + beta -Actin, & RPE65 + CRALBP, respectively. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/34061021), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb300-164_mouse-monoclonal-bestrophin-1-antibody-e6-6-31020241535628.jpg)
![Immunocytochemistry/ Immunofluorescence: Bestrophin 1 Antibody (E6-6) - BSA Free [NB300-164] - Impact of BEST1 pathogenic variants in bestrophin-1 RPE localization. Cryosections obtained from the BD donors & an 88-year-old control were labeled with antibodies specific to bestrophin-1 (green), while cell nuclei have been labeled with TO-PRO-3 (blue). Bruch’s membrane is indicated by the hashed white line. Arrow = mislocalized apical RPE distribution of bestrophin-1; arrowheads = basolateral RPE distribution of bestrophin-1; double arrowheads = intracellular bestrophin-1. Scale bar = 40 μm (all images). Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/33154968), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb300-164_mouse-monoclonal-bestrophin-1-antibody-e6-6-310202415395959.jpg)
![Immunocytochemistry/ Immunofluorescence: Bestrophin 1 Antibody (E6-6) - BSA Free [NB300-164] - Subcellular localization of WT & mutant BEST1 in iPSC-RPEs. Confocal images showing the co-staining of BEST1, Collagen IV & Hoechst in iPSC-RPEs derived from a WT donor or patients. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31836750), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb300-164_mouse-monoclonal-bestrophin-1-antibody-e6-6-310202415175245.jpg)
![Immunocytochemistry/ Immunofluorescence: Bestrophin 1 Antibody (E6-6) - BSA Free [NB300-164] - (a) X-Z confocal single image scan of transiently transfected cells with different BEST1 cDNA constructs showing mislocalization of mutants Y85H, Q96R, L100R & Y227N. Cells were stained for Best1 (green), beta -catenin (red) & nuclei (blue). Scale bar = 10 μm; (b) Z-series confocal stack signals corresponding to each labeling were quantified. Curves indicate the pixel intensity of each section along the Z-axis for each cell (Best1, green; beta -catenin, red; nuclei, blue). The black vertical line indicates the Z-focal plane chosen as threshold for apical & basolateral domains separation. Basolateral & apical sides are as indicated. Horizontal axis represents μm distance & vertical axis shows pixel intensities; (c) Bar graph illustrating quantification of Best1 mutants distribution in the basolateral & apical domains of the cells compared with normal protein (mean ± SEM., n = 10, *p < 0.01, ***p < 0.0001). Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/23880862), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb300-164_mouse-monoclonal-bestrophin-1-antibody-e6-6-31020241621835.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.")
![Simple Western: OPA1 Antibody [NB110-55290] - Lane view shows a specific band for OPA1 in 0.5 mg/ml of MEF lysate. This experiment was performed under reducing conditions using the 12-230 kDa separation system.](http://images.novusbio.com/fullsize/OPA1-Antibody-Simple-Western-NB110-55290-img0007.jpg "Simple Western: OPA1 Antibody [NB110-55290] - Lane view shows a specific band for OPA1 in 0.5 mg/ml of MEF lysate. This experiment was performed under reducing conditions using the 12-230 kDa separation system.")
![Western Blot: OPA1 Antibody [NB110-55290] - Depletion of Oma1 in fish affects development. Immunoblot of protein extracts from injected fish (yolk removed) at 24, 48 and 72 hpf. Expression of Oma1, Opa1 isoforms (a-f) and Cox4 (mitochondrial abundance marker) was analyzed with respective antibodies. Actin and Ponceau S staining were loading controls. Source data (full-length blots) are available online in Supplementary information. Image collected and cropped by CiteAb from the following publication (//www.nature.com/articles/srep13989), licensed under a CC-BY license.](http://images.novusbio.com/fullsize/OPA1-Antibody-Western-Blot-NB110-55290-img0010.jpg)
![Western Blot: OPA1 Antibody [NB110-55290] - Total protein from Human HeLa cells, Mouse MEF cells and Rat Brain 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-OPA1 in 1% blocking buffer. Precision Plus Protein All Blue molecular weight markers (BioRad) were detected with 1 ug/ml Anti-Blue Marker antibody (NBP2-33376). The protein ladder was detected with an anti-mouse HRP secondary antibody and OPA1 with an anti-rabbit HRP secondary antibody using chemiluminescence.](http://images.novusbio.com/fullsize/OPA1-Antibody-Western-Blot-NB110-55290-img0009.jpg)
![Immunohistochemistry: OPA1 Antibody [NB110-55290] - Staining in prostatic smooth muscle and glandular epithelium. Human Prostate 40X magnification.](http://images.novusbio.com/fullsize/OPA1-Antibody-Immunohistochemistry-NB110-55290-img0005.jpg)
![Western Blot: OPA1 Antibody [NB110-55290] - Detection of OPA1 protein in post-nuclear extracts of mouse embryonic fibroblasts.](http://images.novusbio.com/fullsize/OPA1-Antibody-Western-Blot-NB110-55290-img0006.jpg)
![Western Blot: OPA1 Antibody [NB110-55290] - Analysis of OPA1 in porcine retinal pigment epithelium lysate using anti-OPA1 antibody. Image from verified customer review.](http://images.novusbio.com/fullsize/OPA1-Antibody-Western-Blot-NB110-55290-img0008.jpg)
![Western Blot: OPA1 Antibody - BSA Free [NB110-55290] - High content screening of the preadipocytes & beige cells, & detection of mitochondrial fission- & fusion-related proteins: (A) Representative high content screening images showing mitochondrial morphology in TG2+/+ & TG2−/− preadipocytes, scale bars represent 50 μm; (B) fractions of fragmented & tubular mitochondrial morphology in preadipocytes (%); (C) quantitative analysis of mitochondrial morphology in preadipocytes; (D) representative high content screening images showing mitochondrial morphology in TG2+/+ & TG2−/− beige cells; (E) fractions of fragmented & tubular mitochondrial morphology in beige cells (%); (F) quantitative analysis of mitochondrial morphology in beige cells, DAPI staining was used to determine the number of nuclei, the mitochondria were stained with Mito Tracker Deep Red either in the absence or presence of 10 μM antimycin A, Texas Red-X phalloidin was used to stain actin filaments for the detection of cell shapes (n = 3); (G–J) representative Western blot analyses & quantitative analyses of the mitochondrial fusion proteins (MFN2, OPA1) & mitochondrial fission proteins (DRP1, MFF) in preadipocytes & differentiated beige cells. beta -ACTIN was used as a loading control. Columns represent the mean values ± SD. Statistical analyses were performed using Student’s t-test. n = 5. * p < 0.05. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/35563567), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb110-55290_rabbit-polyclonal-opa1-antibody-31020241624918.jpg)
![Flow Cytometry: CD45 Antibody (30-F11) [NB100-77417] - Analysis of CD45 (30F11) in freshly isolated mouse (Balb C) splenocytes (1x10^6) were stained with [NB100-77417] at 1:1000 dilution and detected with FITC conjugated donkey anti-rat IgG secondary (orange). Shown with rat IgG isotype control (blue).](http://images.novusbio.com/fullsize/CD45-Antibody-30-F11-Flow-Cytometry-NB100-77417-img0004.jpg "Flow Cytometry: CD45 Antibody (30-F11) [NB100-77417] - Analysis of CD45 (30F11) in freshly isolated mouse (Balb C) splenocytes (1x10^6) were stained with [NB100-77417] at 1:1000 dilution and detected with FITC conjugated donkey anti-rat IgG secondary (orange). Shown with rat IgG isotype control (blue).")
![Immunohistochemistry-Paraffin: CD45 Antibody (30-F11) [NB100-77417] - Analysis of FFPE section of mouse spleen using rat monoclonal CD45 antibody (30-F11) [NB100-77417] at 1:50 dilution. The antibody generated an expected membrane staining in the red and white pulp spleenocytes of the tested spleen section.](http://images.novusbio.com/fullsize/CD45-Antibody-30-F11-Immunohistochemistry-Paraffin-NB100-77417-img0006.jpg)
![Immunohistochemistry-Paraffin: CD45 Antibody (30-F11) [NB100-77417] - Mouse glomeruli stained with CD45 antibody. 4% formaldehyde fixed paraffin sections. EDTA was used for antigen retrieval. IHC-P image submitted by a verified customer review.](http://images.novusbio.com/fullsize/CD45-Antibody-30-F11-Immunohistochemistry-Paraffin-NB100-77417-img0013.jpg)
![Immunohistochemistry: CD45 Antibody (30-F11) [NB100-77417] - Analysis of a FFPE embedded tissue section of mouse liver using 1:100 dilution of CD45 antibody (30-F11) [NB100-77417]. The signal was developed using AEC reagent based method with hematoxylin counterstaining.](http://images.novusbio.com/fullsize/CD45-Antibody-30-F11-Immunohistochemistry-NB100-77417-img0003.jpg)
![Immunohistochemistry-Frozen: CD45 Antibody (30-F11) [NB100-77417] - Analysis of a mouse spleen cryosection using CD45 antibody (30-F11) [NB100-77417] at 1:50 dilution. The signal was detected using goat anti-rat Alexa fluor 488 secondary with DAPI counterstaining. IHC-P image submitted by a verified customer review.](http://images.novusbio.com/fullsize/CD45-Antibody-30-F11-Immunohistochemistry-Frozen-NB100-77417-img0008.jpg)
![Immunohistochemistry-Paraffin: CD45 Antibody (30-F11) [NB100-77417] - Staining of a FFPE mouse liver tissue section using 1:100 dilution of CD45 antibody (30-F11) [NB100-77417]. Signal was detected using AF488 conjugated donkey anti-rat secondary antibody at 1:500 dilution. IHC-P image submitted by a verified customer review.](http://images.novusbio.com/fullsize/CD45-Antibody-30-F11-Immunohistochemistry-Paraffin-NB100-77417-img0002.jpg)
![Immunohistochemistry: CD45 Antibody (30-F11) [NB100-77417] - Severe apoptosis and pathology in the orally infected heart. Experimental design is as outlined in Fig. 1B. Heart sections from moribund mice were examined with H&E, and immunohistochemistry staining for pan-leukocyte infiltration using an anti-CD45 antibody. Image collected and cropped by CiteAb from the following publication (//www.nature.com/articles/s41598-019-47455-3), licensed under a CC-BY license.](http://images.novusbio.com/fullsize/CD45-Antibody-30-F11-Immunohistochemistry-NB100-77417-img0009.jpg)
![Immunohistochemistry: CD45 Antibody (30-F11) [NB100-77417] - Severe apoptosis and pathology in the orally infected heart. Experimental design is as outlined in Fig. 1B. Heart sections from moribund mice were examined with H&E, and immunohistochemistry staining for pan-leukocyte infiltration using an anti-CD45 antibody. Image collected and cropped by CiteAb from the following publication (//www.nature.com/articles/s41598-019-47455-3), licensed under a CC-BY license.](http://images.novusbio.com/fullsize/CD45-Antibody-30-F11-Immunohistochemistry-NB100-77417-img0012.jpg)
![Immunohistochemistry: CD45 Antibody (30-F11) [NB100-77417] - VP1-positive infiltrating M2 macrophage and VP1-positive pneumocytes were detectable in the orally infected lung. Adjacent lung sections were examined with H&E and IHC staining for a pan-leukocyte marker CD45. Image collected and cropped by CiteAb from the following publication (//www.nature.com/articles/s41598-019-47455-3), licensed under a CC-BY license.](http://images.novusbio.com/fullsize/CD45-Antibody-30-F11-Immunohistochemistry-NB100-77417-img0011.jpg)
![Western Blot: GAPDH Antibody [NB300-327] - Representative immunoblot of KDR and FGFR CAM protein expression levels examined by Western blotting. GNS, graphene nanosheet; NG, graphite nanoparticle; ND, diamond nanoparticle; C60, fullerene C60; MWNT, multi-wall nanotube; KDR, vascular endothelial growth factor receptor; FGFR, fibroblast growth factor receptor; GAPDH, glyceraldehyde-3-phosphate dehydrogenase. Image collected and cropped by CiteAb from the following publication (//nanoscalereslett.springeropen.com/articles/10.1186/1556-276X-8-195), licensed under a CC-BY license.](http://images.novusbio.com/fullsize/GAPDH-Antibody-Western-Blot-NB300-327-img0009.jpg "Western Blot: GAPDH Antibody [NB300-327] - Representative immunoblot of KDR and FGFR CAM protein expression levels examined by Western blotting. GNS, graphene nanosheet; NG, graphite nanoparticle; ND, diamond nanoparticle; C60, fullerene C60; MWNT, multi-wall nanotube; KDR, vascular endothelial growth factor receptor; FGFR, fibroblast growth factor receptor; GAPDH, glyceraldehyde-3-phosphate dehydrogenase. Image collected and cropped by CiteAb from the following publication (//nanoscalereslett.springeropen.com/articles/10.1186/1556-276X-8-195), licensed under a CC-BY license.")
![Immunocytochemistry/Immunofluorescence: GAPDH Antibody [NB300-327] - Analysis of HeLa cells stained with rabbit pAb to GAPDH, dilution 1:2000 in red. Blue is Hoescht staining of nuclear DNA. The GAPDH antibody produces diffuse cytoplasmic staining of cells.](http://images.novusbio.com/fullsize/GAPDH-Antibody-Immunocytochemistry-Immunofluorescence-NB300-327-img0007.jpg)
![Western Blot: GAPDH Antibody [NB300-327] - Theoretical molecular weight: 36 kDa. Detection of GAPDH in mouse liver.](http://images.novusbio.com/fullsize/GAPDH-Antibody-Western-Blot-NB300-327-img0002.jpg)
![Western Blot: GAPDH Antibody [NB300-327] - Western blot analysis of extracts from Jurkat and HeLa cells using NB300-327 at 1:1000. Theoretical molecular weight: 36 kDa.](http://images.novusbio.com/fullsize/GAPDH-Antibody-Western-Blot-NB300-327-img0003.jpg)
![Western Blot: GAPDH Antibody [NB300-327] - Analysis of different cell cytosolic or nuclear enriched fractions, GAPDH antibody, dilution 1:20,000 (Red): [1] protein standard, [2] NIH-3T3 cytosolic, [3] NIH-3T3 nuclear, [4] HeLa cytosolic, and [5] HeLa nuclear fractions. Strong band at 37kDa corresponds to GAPDH protein, mainly detected in the cytosolic fractions. The same blot was simultaneously probed with mouse mAb to the nuclear RNA binding protein SF3B4, dilution 1:1,000 (Green). In contrast to GAPDH, SF3B4 is exclusively expressed in the nuclear fraction.](http://images.novusbio.com/fullsize/GAPDH-Antibody-Western-Blot-NB300-327-img0008.jpg)
![Immunocytochemistry/Immunofluorescence: GAPDH Antibody [NB300-327] - The GAPDH antibody was tested in Hela cells at a 1:500 dilution against Dylight 488 (Green). Alpha-tubulin and nuclei were counterstained with Dylight 550 (Red) and DAPI (Blue), respectively.](http://images.novusbio.com/fullsize/GAPDH-Antibody-Immunocytochemistry-Immunofluorescence-NB300-327-img0001.jpg)
![Immunocytochemistry/Immunofluorescence: GAPDH Antibody [NB300-327] - Confocal immunofluorescence analysis of HeLa cells using GAPDH (NB300-327) antibody (green). Nuclei was counterstained with DAPI (blue).](http://images.novusbio.com/fullsize/GAPDH-Antibody-Immunocytochemistry-Immunofluorescence-NB300-327-img0004.jpg)
![Immunocytochemistry/Immunofluorescence: GAPDH Antibody [NB300-327] - IF Confocal analysis of C2C12 cells using GAPDH antibody (NB300-327, 1:20). An Alexa Fluor 488-conjugated Goat to rabbit IgG was used as secondary antibody (green). Actin filaments were labeled with Alexa Fluor 568 phalloidin (red). DAPI was used to stain the cell nuclei (blue).](http://images.novusbio.com/fullsize/GAPDH-Antibody-Immunocytochemistry-Immunofluorescence-NB300-327-img0005.jpg)
![Simple Western: GAPDH Antibody [NB300-327] - Simple Western lane view shows a specific band for GAPDH in 0.2 mg/ml of HeLa lysate. This experiment was performed under reducing conditions using the 12-230 kDa separation system. Note: band observed higer than predicted 36 kDa molecular weight.](http://images.novusbio.com/fullsize/GAPDH-Antibody-Simple-Western-NB300-327-img0006.jpg)
![Western Blot: GAPDH Antibody [NB300-327] - Effects of subchronic administration (7 and 14 days) of therapeutic relevant concentration of Brex (Brex: 300 nM) and interaction between Brex and 5-HT1A receptor (5-HT1AR) antagonist WAY (10 uM) on protein expression of 5-HT1A receptor in the plasma membrane fraction of cortical primary cultured astrocytes. In left side histograms, ordinate: mean +/- SD (n = 6) of the relative protein level of 5-HT1AR per GAPDH. * p < 0.05, ** p < 0.01: relative to control (Brex-free) by one-way analysis of variance (ANOVA) with Tukey’s post-hoc test, and @ p < 0.05: relative to Brex for 14 days by Student’s T-test. Right side panels indicate their pseudo-gel images using capillary immunoblotting. Antibodies used: 5-HT1A (NBP2-21590) and GAPDH (NB300-327). Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/35743014/) licensed under a CC-BY license.](http://images.novusbio.com/fullsize/nb300-327_rabbit-polyclonal-gapdh-antibody-25520231539521.jpg)
![Western Blot: GAPDH Antibody [NB300-327] - Increased PIP expression in the lungs of PF‐PH compared to PF ratsA, BRelative expression of PIP mRNA (A) & protein (B) normalized to GAPDH.CRepresentative images & PIP quantification.Data information: Values are expressed as mean ± SEM. The number of samples per group for each experiment is included within each bar graph (t‐test; *P < 0.05, **P < 0.01). Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31468711), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb300-327_rabbit-polyclonal-gapdh-antibody-3102024153562.jpg)
![Western Blot: GAPDH Antibody [NB300-327] - Effects of subchronic administration (7 & 14 days) of therapeutic relevant concentration of Brex (Brex: 300 nM) & interaction between Brex & 5-HT1A receptor (5-HT1AR) antagonist WAY100635 (WAY: 10 μM) on protein expression of 5-HT1A (panel A) & 5-HT7 (panel B) receptor in the plasma membrane fraction of cortical primary cultured astrocytes. In left side histograms, ordinate: mean ± SD (n = 6) of the relative protein level of 5-HT1AR & 5-HT7R per GAPDH. * p < 0.05, ** p < 0.01: relative to control (Brex-free) by one-way analysis of variance (ANOVA) with Tukey’s post-hoc test, & @ p < 0.05: relative to Brex for 14 days by Student’s T-test. Right side panels indicate their pseudo-gel images using capillary immunoblotting. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/35743014), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb300-327_rabbit-polyclonal-gapdh-antibody-31020241534337.jpg)
![Western Blot: GAPDH Antibody [NB300-327] - Online lung microarray analysis revealed PIP as one of the Slug transcriptional targets mediating vascular cell proliferation in PF‐PHAHeatmap of the 20 genes upregulated in GSE24988 microarray & known to be Slug transcriptional target.BVenn diagram showing the overlap between Slug targets implicated in cell proliferation & known to be extracellular.CHeatmap of the seven transcriptional targets of Slug known to promote proliferation & to be extracellular.D, ERelative expression of prolactin‐induced protein (PIP) mRNA (D) & protein (E) expression normalized to GAPDH in PF & PF‐PH patients.FRepresentative images of PIP immunohistochemistry showing its extracellular localization & quantification.G–JProliferation assay on healthy fibroblast (G), pulmonary arterial EC (H), & healthy pulmonary arterial SMC (I & J) in the presence or absence of PIP.Data information: Values are expressed as mean ± SEM. The number of samples per group for each experiment is included within each bar graph. Statistical test: panels (D–F): t‐test; panels (G–J): ANOVA (*P < 0.05, **P < 0.01 ***P < 0.001). Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31468711), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb300-327_rabbit-polyclonal-gapdh-antibody-310202416212393.jpg)
![Western Blot: GAPDH Antibody [NB300-327] - Growth of lactobacilli on IECs & their influence towards C. albicans cytotoxicity, adhesion, hyphal length & translocation. (A) LDH release of IECs colonized (Pre-Inc.) or simultaneously colonized (w/o Pre-Inc.) with L. rhamnosus (L.r.) at different MOI (5, 50 or 250) & infected or not with C. albicans (C.a.) (MOI 1) & measured at 24 h post-infection. (B) Growth of L. paracasei (L.p.), L. rhamnosus, L. salivarius (L.s.), L. fermentum (L.f.), & L. brevis (L.b.) on IECs. (C) Percentage of C. albicans adhered to IECs colonized with different Lactobacillus species (MOI 50) at 1 h post-infection. (D) C. albicans hyphal induction on IECs or on plastic colonized with L. rhamnosus or L. brevis (MOI 50) at 4 h post-infection. Results were normalized to C. albicans single infection. (E) Translocation of C. albicans (MOI 1) across IECs colonized with L. rhamnosus or L. brevis (MOI 50) at 24 h post-infection. (F) Assessment of epithelial barrier integrity measured as the loss of transepithelial electrical resistance (TEER) in response to L. rhamnosus or L. brevis (MOI 50) colonization & C. albicans infection in the presence or absence of Lactobacillus colonization at 24 h post-infection. Data are TEER loss in percentage of uninfected host cells (before pre-incubation). (G) E-Cadherin protein expression analyzed by western blot compared to GAPDH in IECs that were left uninfected or colonized with L. rhamnosus (MOI 50) & infected with C. albicans for 6, 12 & 24 h. Data are mean±s.e.m. *P<0.05, **P<0.01, ***P<0.005 (t-test). Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31413153), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb300-327_rabbit-polyclonal-gapdh-antibody-31020241621819.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)
![Immunocytochemistry/Immunofluorescence: Synapsin I Antibody [NB300-104] - hPDLSCs-derived neural-like cells are connected by synapse-like interactions. hPDLSCs-derived neural-like cells connect to one another. Synapse-associated protein Synapsin1 is found in the cell membrane of hPDLSCs-derived neural-like cells at the neurite contact areas. Scale bar: 25 um. Image collected and cropped by CiteAb from the following publication (//www.nature.com/articles/s41598-019-54745-3) licensed under a CC-BY license.](http://images.novusbio.com/fullsize/Synapsin-I-Antibody-Immunocytochemistry-Immunofluorescence-NB300-104-img0013.jpg "Immunocytochemistry/Immunofluorescence: Synapsin I Antibody [NB300-104] - hPDLSCs-derived neural-like cells are connected by synapse-like interactions. hPDLSCs-derived neural-like cells connect to one another. Synapse-associated protein Synapsin1 is found in the cell membrane of hPDLSCs-derived neural-like cells at the neurite contact areas. Scale bar: 25 um. Image collected and cropped by CiteAb from the following publication (//www.nature.com/articles/s41598-019-54745-3) licensed under a CC-BY license.")
![<b>Orthogonal Strategies Validation. </b>Immunocytochemistry/Immunofluorescence: Synapsin I Antibody [NB300-104] - Characterization of WT and slow ESCs differentiated to neurons. Immunofluorescence staining for neuronal markers Map2, and Syn1 in neurons cultured on poly-ornithine-/laminin-coated plates. Expression of neuronal markers in neurons cultured on poly-ornithine-/laminin-coated plates from RNA-seq analysis, n = 3. Image collected and cropped by CiteAb from the following publication (//onlinelibrary.wiley.com/doi/10.15252/embj.2018101244) licensed under a CC-BY license.](http://images.novusbio.com/fullsize/Synapsin-I-Antibody-Immunocytochemistry-Immunofluorescence-NB300-104-img0014.jpg)
![Western Blot: Synapsin I Antibody [NB300-104] - Western blot analysis showing induced expression of neuronal functional marker Synapsin I at protein levels in MNC (meningial neuronal construct). Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/30443545/) licensed under a CC-BY license.](http://images.novusbio.com/fullsize/Synapsin I Antibody-Western Blot-NB300-104-img0015.jpg)
![Immunohistochemistry-Paraffin: Synapsin I Antibody [NB300-104] - Human cerebellum section, formalin fixed paraffin embedded. Stained with Synpasin-1 at 1:250. Citrate antigen retrieval at pH 6. Image from verified customer review.](http://images.novusbio.com/fullsize/Synapsin-I-Antibody-Immunohistochemistry-Paraffin-NB300-104-img0012.jpg)
![Western Blot: Synapsin I Antibody [NB300-104] - 10 ug of rat hippocampal (Hipp) lysate showing specific immunolabeling of the ~78k synapsin I doublet protein.](http://images.novusbio.com/fullsize/Synapsin-I-Antibody-Western-Blot-NB300-104-img0007.jpg)
![Western Blot: Synapsin I Antibody [NB300-104] - 10 ug of rat brain lysate showing specific immunolabeling of the ~78 kDa Synapsin I doublet.](http://images.novusbio.com/fullsize/Synapsin-I-Antibody-Western-Blot-NB300-104-img0008.jpg)
![Immunocytochemistry/Immunofluorescence: Synapsin I Antibody [NB300-104] - ICC-IF validation analysis of Synapsin 1 Antibody on cultured rat caudate neurons. This representative image shows the punctate distribution of Synapsin 1 (green) and MAP (red) proteins in a neuronal cell.](http://images.novusbio.com/fullsize/Synapsin-I-Antibody-Immunocytochemistry-Immunofluorescence-NB300-104-img0011.jpg)
![Immunocytochemistry/ Immunofluorescence: Synapsin I Antibody [NB300-104] - Characterization of WT & slow ESCs differentiated to neurons (related to Fig 4)Immunofluorescence staining for neuronal markers Map2, Syn1, & NeuN in neurons cultured on poly‐ornithine‐/laminin‐coated plates.Expression of neuronal markers in neurons cultured on poly‐ornithine‐/laminin‐coated plates from RNA‐seq analysis, n = 3. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/30988016), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb300-104_rabbit-polyclonal-synapsin-i-antibody-310202415394528.jpg)
![Immunocytochemistry/ Immunofluorescence: Synapsin I Antibody [NB300-104] - hPDLSCs-derived neural-like cells are connected by synapse-like interactions. hPDLSCs-derived neural-like cells connect to one another (a) through different types of synapses-like interactions, including dendrodendritic-like, axoaxonic-like & axodendritic-like synapses (b). (c) Synapse-associated proteins Cx43, Synaptophysin & Synapsin1 are found in the cell membrane of hPDLSCs-derived neural-like cells at the neurite contact areas. Scale bar: 25 μm. AA, axoaxonic-like synapse; AD, axodendritic-like synapse; DD, dendrodendritic-like synapse; LM, light microscopy; SEM, scanning electron microscopy. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31792338), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb300-104_rabbit-polyclonal-synapsin-i-antibody-310202415371980.jpg)
![Western Blot: Synapsin I Antibody [NB300-104] - Synaptic localization of TA at the PC–PF synaptic contacts.Western blot of TA, V1, V2, VGAT proteins in cerebellar synaptosomal fractions (SYN) from P14 mice. Synaptosomal preparations are enriched of post synaptic density protein (PSD95) & Synapsin-I (Syn-I) in comparison to equal amount (ACT) of total cerebellar protein extract (LYS). TA is clearly present in synaptosomal enriched preparations. B) Cerebellar sagittal section immunostained for Cb (green), V1 (cyan) & TA (red). In the ML, anti-V1 specifically labels PF-terminals contacting PC-spines. C–E) The high magnification of the inset in B is reproduced in different merge images & by the relative split channels. C) Merge image of Cb & V1 staining plus the colocalization mask Cb/V1 (mCb/V1 in white); it represents the negative CTR (CTR-). D) Merge image of TA & Cb staining plus the colocalization mask TA/Cb (mTA/Cb in white), highlighting TA expression in PC-spines. E) Merge image of TA & V1 staining plus the colocalization mask TA/V1 (m TA/V1 in white), indicating the presence of TA also in this synaptic terminal. F) Quantitative colocalization analysis shows the mean overlap coefficients of TA/Cb (gray column) & TA/V1 (black column) significantly different from the negative CTR Cb/V1 (white column). The small insets (white boxes in C–D-E) are high magnifications of a representative PC-spine (green) contacted by a PF synaptic terminal (cyan) with the appropriate colocalization mask (white). * p < 0.05. Data are represented as mean ± SEM. Scale bars in B, 10 µm; in C–D-E, 5 µm; in F, 1 µm. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/23840813), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb300-104_rabbit-polyclonal-synapsin-i-antibody-31020241621237.jpg)
![Western Blot: Synapsin I Antibody [NB300-104] - Tau oligomers induce synaptic dysfunction. (A) Representative Western blot of mouse hippocampus homogenate. The levels of synaptophysin, synapsin-1, & septin-11 were measured by band quantification & normalized with the levels of tubulin. PBSo indicates representative bands of hippocampal area injected with PBS in mice also injected with tau oligomers, PBSf indicates PBS injection in mice also injected with tau fibrils, & PBSm indicates PBS injection in mice also injected with tau monomers. (B) Synaptophysin levels were significantly lower in the hemispheres injected with tau oligomers in comparison with the ones injected with fibrils, monomers, or PBS. (C) No significant differences in the levels of synapsin-1 were observed. (D) Only the hemisphere injected with tau oligomers presents a decrease in the level of septin-11. Data are represented as the mean ± SE. *p < 0.01, n = 6 Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/21645391), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb300-104_rabbit-polyclonal-synapsin-i-antibody-31020241620516.jpg)
![Western Blot: Ubiquitin Antibody (Ubi-1) [NB300-130] - Ubiquitination of PML in response to As2O3. PML-/- MEFs were transiently transfected with the empty vector (EV) or PMLIII (left panel) or contructs encoding PMLIII, PMLIII-SIM or PMLVI (right panel). Two days later, they were treated with As2O3 for 1 h. The cell extracts were immunoprecipitated with rabbit anti-PML antibody and the immunoprecipitate was analyzed by Western blot using anti-ubiquitin and anti-PML antibodies. Image collected and cropped by CiteAb from the following publication (//doi.org/10.1371/journal.pone.0044949) licensed under a CC-BY license.](http://images.novusbio.com/fullsize/Ubiquitin-Antibody-Ubi-1-Western-Blot-NB300-130-img0014.jpg "Western Blot: Ubiquitin Antibody (Ubi-1) [NB300-130] - Ubiquitination of PML in response to As2O3. PML-/- MEFs were transiently transfected with the empty vector (EV) or PMLIII (left panel) or contructs encoding PMLIII, PMLIII-SIM or PMLVI (right panel). Two days later, they were treated with As2O3 for 1 h. The cell extracts were immunoprecipitated with rabbit anti-PML antibody and the immunoprecipitate was analyzed by Western blot using anti-ubiquitin and anti-PML antibodies. Image collected and cropped by CiteAb from the following publication (//doi.org/10.1371/journal.pone.0044949) licensed under a CC-BY license.")
![Immunocytochemistry/Immunofluorescence: Ubiquitin Antibody (Ubi-1) [NB300-130] - Study of mutant BRAF protein found within the inclusions. BRAFV600E/ubiquitin double-IF labeling. A nucleus with a large inclusion is shown with positive immunoreactivity for both mutant BRAF (red staining) and ubiquitin (green staining); the merged color yellow (arrow) points out the co-localisation of BRAFV600E and ubiquitin in the same inclusion. Image collected and cropped by CiteAb from the following publication (////doi.org/10.1371/journal.pone.0226199) licensed under a CC-BY license.](http://images.novusbio.com/fullsize/Ubiquitin-Antibody-Ubi-1-Immunocytochemistry-Immunofluorescence-NB300-130-img0013.jpg)
![Western Blot: Ubiquitin Antibody (Ubi-1) [NB300-130] - Analysis of HEK293 cell lysates using mouse mAb Ubiquitin, dilution 1:1000 (Green). [1] protein standard (Red), [2] cells maintained in normal medium, [3] cells treated with 10uM of proteasome inhibitor lactacystin (Lc) for 16hrs. Lysed cells were electrophoresed on 4-20% SDS-PAGE and transferred to PVDF membranes. The smear detected above the 200kDa standard represent accumulation of ubiquitinated proteins in proteasome inhibitor-Lc treated cells. The prominent band at 8kDa corresponds to monoubiquitin. Rabbit pAb to HSP60, dilution 1:5000 (Red) was used as a loading control.](http://images.novusbio.com/fullsize/Ubiquitin-Antibody-Ubi-1-Western-Blot-NB300-130-img0012.jpg)
![Immunohistochemistry-Paraffin: Ubiquitin Antibody (Ubi-1) [NB300-130] - FFPE section of cerebral cortex of an Alzheimer patient processed with Ubiquitin antibody using HRP/DAB (Brown) and also stained with haemotoxylin (Blue). A typical flame shaped tangle is seen in a pyramidal neuron in the center and is surrounded by some dystrophic neurites, also strongly ubiquitin positive. Both are commonly seen in cortical and hippocampal Alzheimer brain sections and are typical for this disease, but are rare or absent in healthy brain.](http://images.novusbio.com/fullsize/Ubiquitin-Antibody-Ubi-1-Immunohistochemistry-Paraffin-NB300-130-img0011.jpg)
![Immunohistochemistry-Paraffin: Ubiquitin Antibody (Ubi-1) [NB300-130] - Staining of Ubiquitin in hippocampal tissue from an Alzheimer patient.](http://images.novusbio.com/fullsize/Ubiquitin-Antibody-Ubi-1-Immunohistochemistry-Paraffin-NB300-130-img0008.jpg)
![Western Blot: Ubiquitin Antibody (Ubi-1) [NB300-130] - Molecular Analysis of XopD Ub/Ubl Specificity. S. lycopersicum protein extract blotted for total Ub (Ubiquitin; Novus Biologicals) following a 1 hr room temperature treatment with the XopD variants used in (K) at 1 uM final concentration. Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/27425412/) licensed under a CC-BY license.](http://images.novusbio.com/fullsize/Ubiquitin-Antibody-Ubi-1-Western-Blot-NB300-130-img0015.jpg)
![Western Blot: Ubiquitin Antibody (Ubi-1) [NB300-130] - Western blot of Ubiquitin expression on (Lane 1) poly-ubiquitin (lys63 linked), (Lane 2) pure ubiquitin and crude homogenates of adult rat, (Lane 3) cortex, (Lane 4) cerebellum and (Lane 5) brain stem.](http://images.novusbio.com/fullsize/Ubiquitin-Antibody-Ubi-1-Western-Blot-NB300-130-img0009.jpg)
![Immunohistochemistry-Paraffin: Ubiquitin Antibody (Ubi-1) [NB300-130] - IHC staining of Ubiquitin in human rectal cancer using DAB with hematoxylin counterstain.](http://images.novusbio.com/fullsize/Ubiquitin-Antibody-Ubi-1-Immunohistochemistry-Paraffin-NB300-130-img0010.jpg)
![Western Blot: Ubiquitin Antibody (Ubi-1) [NB300-130] - In Vivo Applications of Affimers(A) HA-NleL 293 T-Rex cells were induced with 1 μg/mL doxycycline for 12 hr or left untreated. Whole-cell lysate (WCL) blots are shown for actin, HA(-NleL), Ub, & K6 chains. Western blots with the K6 affimer are also shown after Ub enrichment using TUBEs.(B) TUBE-PD of HEK293 cells after 1 hr of MG132 (10 μM) without further treatment (−) or with additional UV (40 J/m2) or CCCP treatment (10 μM for 1 hr) & subsequently blotted with the K6 affimer. Input controls are shown for total Ub & actin & gamma H2AX. The relative signal increase from two experiments is shown below the respective lanes.(C) Expression of WT or catalytically inactive (C431S) Parkin in HeLa Flp-In cells was induced with 0.2 μg/mL doxycycline for 16 hr. Mitochondria were depolarized with O/A for 2 hr. WCL inputs are shown for total Ub, expressed Parkin, TOM20, & actin. The TUBE-PD was also blotted using the K6 affimer & total Ub.(D) Confocal fluorescence microscopy images of cells as in (B) stained with K6 affimer (green), TOM20 (red), & DAPI (blue). Cells & a magnified area are outlined in white. Scale bars correspond to 20 μm.See also Figure S5. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/28943312), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb300-130_mouse-monoclonal-ubiquitin-antibody-ubi-1-imgenex-img-5021-310202416205188.jpg)
![Western Blot: Ubiquitin Antibody (Ubi-1) [NB300-130] - In Vivo Applications of Affimers(A) HA-NleL 293 T-Rex cells were induced with 1 μg/mL doxycycline for 12 hr or left untreated. Whole-cell lysate (WCL) blots are shown for actin, HA(-NleL), Ub, & K6 chains. Western blots with the K6 affimer are also shown after Ub enrichment using TUBEs.(B) TUBE-PD of HEK293 cells after 1 hr of MG132 (10 μM) without further treatment (−) or with additional UV (40 J/m2) or CCCP treatment (10 μM for 1 hr) & subsequently blotted with the K6 affimer. Input controls are shown for total Ub & actin & gamma H2AX. The relative signal increase from two experiments is shown below the respective lanes.(C) Expression of WT or catalytically inactive (C431S) Parkin in HeLa Flp-In cells was induced with 0.2 μg/mL doxycycline for 16 hr. Mitochondria were depolarized with O/A for 2 hr. WCL inputs are shown for total Ub, expressed Parkin, TOM20, & actin. The TUBE-PD was also blotted using the K6 affimer & total Ub.(D) Confocal fluorescence microscopy images of cells as in (B) stained with K6 affimer (green), TOM20 (red), & DAPI (blue). Cells & a magnified area are outlined in white. Scale bars correspond to 20 μm.See also Figure S5. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/28943312), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb300-130_mouse-monoclonal-ubiquitin-antibody-ubi-1-imgenex-img-5021-310202416205134.jpg)
![Western Blot: Ubiquitin Antibody (Ubi-1) [NB300-130] - HUWE1 Assembles K6 Chains In Vitro & In Vivo(A) Table summarizing proteins identified with the corresponding number peptide-spectrum matches (PSMs) in three replicates of DUB-treated K6 affimer pull-downs.(B) In vitro assembly reaction of the HECT E3 HUWE1 with Ub WT, Ub K6R, Ub K11R, & Ub K48R on Coomassie. Arrows indicate K6 diUb.(C) Linkage composition of HUWE1-generated diUb after 1 hr as determined by AQUA MS.(D) AQUA-derived total cellular chain composition of HUWE1−/− HeLa & parental cells after TUBE-based enrichment. Error bars indicate mean ± SD from n = 3. ∗p < 0.05, according to a two-tailed Student’s t test. N.S., not significant.(E) TUBE-PD from a doxycycline-inducible HUWE1 shRNA Ls174T cell line blotted with the K6-specific affimer, with input controls for actin, total Ub, & HUWE1.(F) K6 affimer pull-down in doxycycline-inducible HUWE1 shRNA Ls174T cells blotted against Mfn2. Cells were left untreated or treated with 10 μg/mL MG132 for 4 hr and/or 1 μg/mL doxycycline for 72 hr. Pull-downs were incubated with 250 nM USP21 as indicated, with a K48 blot to show completeness of the deubiquitination reaction. Input controls are shown for Mfn2, actin, & HUWE1.See also Figure S7. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/28943312), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb300-130_mouse-monoclonal-ubiquitin-antibody-ubi-1-imgenex-img-5021-3102024162181.jpg)
![Western Blot: Ubiquitin Antibody (Ubi-1) [NB300-130] - In Vivo Applications of Affimers(A) HA-NleL 293 T-Rex cells were induced with 1 μg/mL doxycycline for 12 hr or left untreated. Whole-cell lysate (WCL) blots are shown for actin, HA(-NleL), Ub, & K6 chains. Western blots with the K6 affimer are also shown after Ub enrichment using TUBEs.(B) TUBE-PD of HEK293 cells after 1 hr of MG132 (10 μM) without further treatment (−) or with additional UV (40 J/m2) or CCCP treatment (10 μM for 1 hr) & subsequently blotted with the K6 affimer. Input controls are shown for total Ub & actin & gamma H2AX. The relative signal increase from two experiments is shown below the respective lanes.(C) Expression of WT or catalytically inactive (C431S) Parkin in HeLa Flp-In cells was induced with 0.2 μg/mL doxycycline for 16 hr. Mitochondria were depolarized with O/A for 2 hr. WCL inputs are shown for total Ub, expressed Parkin, TOM20, & actin. The TUBE-PD was also blotted using the K6 affimer & total Ub.(D) Confocal fluorescence microscopy images of cells as in (B) stained with K6 affimer (green), TOM20 (red), & DAPI (blue). Cells & a magnified area are outlined in white. Scale bars correspond to 20 μm.See also Figure S5. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/28943312), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb300-130_mouse-monoclonal-ubiquitin-antibody-ubi-1-imgenex-img-5021-310202416205121.jpg)
![Western Blot: LRRK2 Antibody [NB300-268] - Western blotting of LRRK2. Recombinant LRRK2 (arrowhead) from transfected (+) HEK 293T and M17 cells was specifically recognized by all four LRRK2 antibodies (Ab1, Ab2, Ab3, and Ab4) used in this study. LRRK2 was not recognized in non-transfected cells (-). Image collected and cropped by CiteAb from the following publication (//molecularneurodegeneration.biomedcentral.com/articles/10.1186/1750-1326-1-17), licensed under a CC-BY license.](http://images.novusbio.com/fullsize/LRRK2-Antibody-Western-Blot-NB300-268-img0023.jpg "<b>Independent Antibodies Validation. </b>Western Blot: LRRK2 Antibody [NB300-268] - Western blotting of LRRK2. Recombinant LRRK2 (arrowhead) from transfected (+) HEK 293T and M17 cells was specifically recognized by all four LRRK2 antibodies (Ab1, Ab2, Ab3, and Ab4) used in this study. LRRK2 was not recognized in non-transfected cells (-). Image collected and cropped by CiteAb from the following publication (//molecularneurodegeneration.biomedcentral.com/articles/10.1186/1750-1326-1-17), licensed under a CC-BY license.")
![<b>Independent Antibodies Validation. </b>Immunohistochemistry-Frozen: LRRK2 Antibody [NB300-268] - Staining as described in PMID 24312256. Image from verified customer review.](http://images.novusbio.com/fullsize/LRRK2-Antibody-Immunohistochemistry-Frozen-NB300-268-img0014.jpg)
![Western Blot: LRRK2 Antibody [NB300-268] - LRRK2 N-terminal sequences show increased aggregation. Western blots of cell lysates of SH-SY5Y cells transfected with indicated LRRK2 construct showed equal expression of the LRRK2 protein with anti-HA (top panel) or anti-C-terminal- (bottom panel) LRRK2 antibody. Equal lysate loading is indicated by Beta-actin loading control. Image collected and cropped by CiteAb from the following publication (//doi.org/10.1371/journal.pone.0045149) licensed under a CC-BY license.](http://images.novusbio.com/fullsize/LRRK2-Antibody-Western-Blot-NB300-268-img0028.jpg)
![Immunohistochemistry-Paraffin: LRRK2 Antibody [NB300-268] - Specificity of immunostaining for LRRK2. Specificity of the antibodies used for immunocytochemistry was determined by performing adsorptions with the corresponding peptide sequences. Immunochemical localization of LBs (arrows) by Ab1 against LRRK2900-100 (left) was blocked using respective peptide antigens (right). Adjacent sections with LB within pigmented neurons from the substantia nigra of a case of PD were used. Scale bar: 20 um. Image collected and cropped by CiteAb from the following publication (//molecularneurodegeneration.biomedcentral.com/articles/10.1186/1750-1326-1-17), licensed under a CC-BY license.](http://images.novusbio.com/fullsize/LRRK2-Antibody-Immunohistochemistry-Paraffin-NB300-268-img0026.jpg)
![<b>Independent Antibodies Validation. </b>Immunohistochemistry-Paraffin: LRRK2 Antibody [NB300-268] - Immunocytochemistry of LRRK2 in PD using antibodies (Ab1, Ab4) raised against sequences corresponding to various regions shown on the schematic diagram of LRRK2 (red bars) were used on brainstem sections of PD. Scale bars: 10 um (top); E-L = 100 um (bottom). Image collected and cropped by CiteAb from the following publication (//molecularneurodegeneration.biomedcentral.com/articles/10.1186/1750-1326-1-17), licensed under a CC-BY license.](http://images.novusbio.com/fullsize/LRRK2-Antibody-Immunohistochemistry-Paraffin-NB300-268-img0025.jpg)
![Flow Cytometry: LRRK2 Antibody [NB300-268] - Analysis using the Alexa Fluor 647 conjugate of NB300-268. Staining of LRRK2 in normal human peripheral blood cells (anticoagulated Lithium-Heparin) using anti-LRRK2 antibody conjugated with AF647. The primary antibody was used at a dilution of 1:200 and incubated for 20 min at room temperature. Image from verified customer review.](http://images.novusbio.com/fullsize/LRRK2-Antibody-Flow-Cytometry-NB300-268-img0019.jpg)
![Immunohistochemistry-Paraffin: LRRK2 Antibody [NB300-268] - LRRK2 accumulates in globules in alphaS tg mice. Triple immunofluorescence for alphaS, LRRK2 and Rab5B for basal ganglia in alphaS tg mice. LRRK2 and Rab5B were colocalized in axon terminal (arrow), but were not colocalized in the alphaS-globule (arrowhead) Scale bar = 10 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/LRRK2-Antibody-Immunohistochemistry-Paraffin-NB300-268-img0024.jpg)
![Immunocytochemistry/Immunofluorescence: LRRK2 Antibody [NB300-268] - HeLa cells were fixed in 4% paraformaldehyde for 10 minutes and permeabilized in 0.05% Triton X-100 in PBS for 5 minutes. The cells were incubated with anti-LRRK2 Antibody NB300-268 at 2 ug/ml overnight at 4C and detected with an anti-mouse Dylight 488 (Green) at a 1:1000 dilution for 60 minutes. Nuclei were counterstained with DAPI (Blue). Cells were imaged using a 100X objective and digitally deconvolved.](http://images.novusbio.com/fullsize/LRRK2-Antibody-Immunocytochemistry-Immunofluorescence-NB300-268-img0031.jpg)
![Flow Cytometry: LRRK2 Antibody [NB300-268] - An intracellular stain was performed on U2OS cells with LRRK2 Antibody NB300-268 (blue) and a matched isotype control (orange). Cells were fixed with 4% PFA and then permeabilized with 0.1% saponin. Cells were incubated in an antibody dilution of 2.5 ug/mL for 30 minutes at room temperature, followed by Rabbit IgG (H+L) Cross-Adsorbed Secondary Antibody, Dylight 550 (SA5-10033, Thermo Fisher).](http://images.novusbio.com/fullsize/LRRK2-Antibody-Flow-Cytometry-NB300-268-img0030.jpg)
![Immunocytochemistry/Immunofluorescence: LRRK2 Antibody [NB300-268] - LRRK2 antibody was tested in SH-SY-5Y cells at a 1:200 dilution against DyLight 488 (Green). Alpha tubulin and nuclei were counterstained against DyLight 568 (Red), and DAPI (Blue), respectively.](http://images.novusbio.com/fullsize/LRRK2-Antibody-Immunocytochemistry-Immunofluorescence-NB300-268-img0015.jpg)
![Immunohistochemistry-Paraffin: LRRK2 Antibody [NB300-268] - Staining of human brain, Putamen, Neurons and Glia using a 60X magnification.](http://images.novusbio.com/fullsize/LRRK2-Antibody-Immunohistochemistry-Paraffin-NB300-268-img0020.jpg)
![Flow Cytometry: LRRK2 Antibody [NB300-268] - An intracellular stain was performed on U2OS cells with LRRK Antibody NB300-268AF647 (blue) and a matched isotype control (orange). Cells were fixed with 4% PFA and then permeabilized with 0.1% saponin. Cells were incubated in an antibody dilution of 2.5 ug/mL for 30 minutes at room temperature. Both antibodies were conjugated to Alexa Fluor 647.](http://images.novusbio.com/fullsize/LRRK2-Antibody-Flow-Cytometry-NB300-268-img0022.jpg)
![Flow Cytometry: LRRK2 Antibody [NB300-268] - An intracellular stain was performed on Neuro2a cells with LRRK2 Antibody NB300-268 (blue) and a matched isotype control (orange). Cells were fixed with 4% PFA and then permeabilized with 0.1% saponin. Cells were incubated in an antibody dilution of 2.5 ug/mL for 30 minutes at room temperature, followed by Rabbit IgG (H+L) Cross-Adsorbed Secondary Antibody, Dylight 550 (SA5-10033, Thermo Fisher).](http://images.novusbio.com/fullsize/LRRK2-Antibody-Flow-Cytometry-NB300-268-img0029.jpg)
![Western Blot: LRRK2 Antibody - BSA Free [NB300-268] - Western blotting of LRRK2. A. Recombinant LRRK2 (arrowhead) from transfected (+) HEK 293T & M17 cells was specifically recognized by all four LRRK2 antibodies (Ab1, Ab2, Ab3, & Ab4) used in this study. LRRK2 was not recognized in non-transfected cells (-). B. Recombinant LRRK2 (arrowhead) from transfected M17 cells is detected by anti-LRRK2 Ab4 (lane 1), but not after absorption of the antibody with its peptide antigen (lane 2). Brain LRRK2 was recognized by anti-LRRK2 Ab4 in two controls (lanes 3 & 4) & two PD cases (lanes 5 & 6). Cell lysates (10 μg protein) & brain homogenates (100 μg protein) were prepared & loaded on 6% SDS-PAGE gels for Western blot analysis using anti-LRRK2 antibodies Ab1–Ab4 in (A) & Ab4 in (B). Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/17137507), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb300-268_rabbit-polyclonal-lrrk2-antibody-310202415371926.jpg)
![Flow Cytometry: LRRK2 Antibody - BSA Free [NB300-268] - Deletion of LRRK2 attenuates Mn-induced apoptosis & cell death in RAW 264.7 cells.(A) LRRK2 WT or KO RAW 264.7 cells were treated with Mn (250 μM) for the designated times, followed by flow cytometry analysis to determine Mn-induced apoptosis. Both early & late apoptotic cells (Q2 & Q3) were measured. (B) At the end of Mn exposure, cell viability was determined by MTT assay. @@@, p < 0.001; ###, p < 0.001; ***, p < 0.001 compared to the control (one-way ANOVA followed by Tukey’s post hoc test; n = 3, for apoptosis assay; n = 6, for MTT assay). The data shown are representative of 3 independent experiments. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/30645642), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb300-268_rabbit-polyclonal-lrrk2-antibody-31020241539739.jpg)
![Immunocytochemistry/ Immunofluorescence: LRRK2 Antibody - BSA Free [NB300-268] - LRRK2 accumulates in globules in alpha S tg mice. (a & b) Double immunofluorescence for alpha S with parkin, PINK1, DJ-1, LRRK2, or negative control (the immunopeptide-preabsorbed anti-LRRK2 antibody) in alpha S tg mice (a) & P123H beta S tg mice (b). Note that alpha S-globules were immunopositive for LRRK2 (~79%, n = 22), whereas P123H beta S globules were negative for LRRK2. Representative images are shown for the thalamus ( alpha S) & basal ganglia (P123H beta S). Scale bar = 5 μm for all panels. (c) Triple immunofluorescence for alpha S, LRRK2 & Rab5B for basal ganglia in alpha S tg mice. LRRK2 & Rab5B were colocalized in axon terminal (arrow), but were not colocalized in the alpha S-globule (arrowhead) Scale bar = 10 μm for all panels. Image collected & cropped by CiteAb from the following publication (//molecularbrain.biomedcentral.com/articles/10.1186/1756-6606-5-34), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb300-268_rabbit-polyclonal-lrrk2-antibody-31020241538242.jpg)
![Immunohistochemistry-Paraffin: LRRK2 Antibody - BSA Free [NB300-268] - Specificity of immunostaining for LRRK2. Specificity of the antibodies used for immunocytochemistry was determined by performing adsorptions with the corresponding peptide sequences. Immunochemical localization of LBs (arrows) by Ab4 against LRRK22500–2527 (A) & Ab1 against LRRK2900–100 (C) was blocked using respective peptide antigens (B & D). Adjacent sections with LB within pigmented neurons from the substantia nigra of a case of PD were used. Scale bar: 20 μm. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/17137507), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb300-268_rabbit-polyclonal-lrrk2-antibody-310202415392599.jpg)
![Immunohistochemistry-Paraffin: LRRK2 Antibody - BSA Free [NB300-268] - Immunocytochemistry of LRRK2 in DLB. Cortical LBs (arrows) in DLB were positive for LRRK2 using both Ab4 against LRRK22500–2527 (A), & Ab1 against LRRK2900–100 (B). Neuronal cytoplasm (C) was also strongly labelled throughout the cortex by Ab4 & with a consistently more granular pattern by Ab1 (inset in C) in cases of DLB. Control cases display similar, though less intense neuronal labeling (D). Biochemically purified cortical LBs were strongly positive for staining by Ab4 (E) as well as by anti-alpha -synuclein (F), while they were unstained when omitting primary antibody (G). Large vessels (H) were also intensely labelled by Ab4. Scale bars: A, B = 25 μm; C, D = 100 μm; E-G = 25 μm; H = 50 μm. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/17137507), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb300-268_rabbit-polyclonal-lrrk2-antibody-310202415304221.jpg)
![Immunohistochemistry-Paraffin: LRRK2 Antibody - BSA Free [NB300-268] - Immunocytochemistry of LRRK2 in DLB. Cortical LBs (arrows) in DLB were positive for LRRK2 using both Ab4 against LRRK22500–2527 (A), & Ab1 against LRRK2900–100 (B). Neuronal cytoplasm (C) was also strongly labelled throughout the cortex by Ab4 & with a consistently more granular pattern by Ab1 (inset in C) in cases of DLB. Control cases display similar, though less intense neuronal labeling (D). Biochemically purified cortical LBs were strongly positive for staining by Ab4 (E) as well as by anti-alpha -synuclein (F), while they were unstained when omitting primary antibody (G). Large vessels (H) were also intensely labelled by Ab4. Scale bars: A, B = 25 μm; C, D = 100 μm; E-G = 25 μm; H = 50 μm. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/17137507), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb300-268_rabbit-polyclonal-lrrk2-antibody-31020241534387.jpg)
![Immunocytochemistry/ Immunofluorescence: LRRK2 Antibody - BSA Free [NB300-268] - LRRK2 accumulates in globules in alpha S tg mice. (a & b) Double immunofluorescence for alpha S with parkin, PINK1, DJ-1, LRRK2, or negative control (the immunopeptide-preabsorbed anti-LRRK2 antibody) in alpha S tg mice (a) & P123H beta S tg mice (b). Note that alpha S-globules were immunopositive for LRRK2 (~79%, n = 22), whereas P123H beta S globules were negative for LRRK2. Representative images are shown for the thalamus ( alpha S) & basal ganglia (P123H beta S). Scale bar = 5 μm for all panels. (c) Triple immunofluorescence for alpha S, LRRK2 & Rab5B for basal ganglia in alpha S tg mice. LRRK2 & Rab5B were colocalized in axon terminal (arrow), but were not colocalized in the alpha S-globule (arrowhead) Scale bar = 10 μm for all panels. Image collected & cropped by CiteAb from the following publication (//molecularbrain.biomedcentral.com/articles/10.1186/1756-6606-5-34), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb300-268_rabbit-polyclonal-lrrk2-antibody-31020241517133.jpg)
![Immunocytochemistry/ Immunofluorescence: LRRK2 Antibody - BSA Free [NB300-268] - LRRK2 accumulates in globules in alpha S tg mice. (a & b) Double immunofluorescence for alpha S with parkin, PINK1, DJ-1, LRRK2, or negative control (the immunopeptide-preabsorbed anti-LRRK2 antibody) in alpha S tg mice (a) & P123H beta S tg mice (b). Note that alpha S-globules were immunopositive for LRRK2 (~79%, n = 22), whereas P123H beta S globules were negative for LRRK2. Representative images are shown for the thalamus ( alpha S) & basal ganglia (P123H beta S). Scale bar = 5 μm for all panels. (c) Triple immunofluorescence for alpha S, LRRK2 & Rab5B for basal ganglia in alpha S tg mice. LRRK2 & Rab5B were colocalized in axon terminal (arrow), but were not colocalized in the alpha S-globule (arrowhead) Scale bar = 10 μm for all panels. Image collected & cropped by CiteAb from the following publication (//molecularbrain.biomedcentral.com/articles/10.1186/1756-6606-5-34), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb300-268_rabbit-polyclonal-lrrk2-antibody-310202415304292.jpg)
![Western Blot: LRRK2 Antibody - BSA Free [NB300-268] - Western blotting of LRRK2. A. Recombinant LRRK2 (arrowhead) from transfected (+) HEK 293T & M17 cells was specifically recognized by all four LRRK2 antibodies (Ab1, Ab2, Ab3, & Ab4) used in this study. LRRK2 was not recognized in non-transfected cells (-). B. Recombinant LRRK2 (arrowhead) from transfected M17 cells is detected by anti-LRRK2 Ab4 (lane 1), but not after absorption of the antibody with its peptide antigen (lane 2). Brain LRRK2 was recognized by anti-LRRK2 Ab4 in two controls (lanes 3 & 4) & two PD cases (lanes 5 & 6). Cell lysates (10 μg protein) & brain homogenates (100 μg protein) were prepared & loaded on 6% SDS-PAGE gels for Western blot analysis using anti-LRRK2 antibodies Ab1–Ab4 in (A) & Ab4 in (B). Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/17137507), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb300-268_rabbit-polyclonal-lrrk2-antibody-31020241536376.jpg)
![Immunohistochemistry-Paraffin: LRRK2 Antibody - BSA Free [NB300-268] - Immunocytochemistry of LRRK2 in DLB. Cortical LBs (arrows) in DLB were positive for LRRK2 using both Ab4 against LRRK22500–2527 (A), & Ab1 against LRRK2900–100 (B). Neuronal cytoplasm (C) was also strongly labelled throughout the cortex by Ab4 & with a consistently more granular pattern by Ab1 (inset in C) in cases of DLB. Control cases display similar, though less intense neuronal labeling (D). Biochemically purified cortical LBs were strongly positive for staining by Ab4 (E) as well as by anti-alpha -synuclein (F), while they were unstained when omitting primary antibody (G). Large vessels (H) were also intensely labelled by Ab4. Scale bars: A, B = 25 μm; C, D = 100 μm; E-G = 25 μm; H = 50 μm. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/17137507), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb300-268_rabbit-polyclonal-lrrk2-antibody-310202415175254.jpg)
![Immunohistochemistry-Paraffin: LRRK2 Antibody - BSA Free [NB300-268] - Immunocytochemistry of LRRK2 in DLB. Cortical LBs (arrows) in DLB were positive for LRRK2 using both Ab4 against LRRK22500–2527 (A), & Ab1 against LRRK2900–100 (B). Neuronal cytoplasm (C) was also strongly labelled throughout the cortex by Ab4 & with a consistently more granular pattern by Ab1 (inset in C) in cases of DLB. Control cases display similar, though less intense neuronal labeling (D). Biochemically purified cortical LBs were strongly positive for staining by Ab4 (E) as well as by anti-alpha -synuclein (F), while they were unstained when omitting primary antibody (G). Large vessels (H) were also intensely labelled by Ab4. Scale bars: A, B = 25 μm; C, D = 100 μm; E-G = 25 μm; H = 50 μm. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/17137507), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb300-268_rabbit-polyclonal-lrrk2-antibody-310202415345320.jpg)
![Immunohistochemistry-Paraffin: LRRK2 Antibody - BSA Free [NB300-268] - Immunocytochemistry of LRRK2 in DLB. Cortical LBs (arrows) in DLB were positive for LRRK2 using both Ab4 against LRRK22500–2527 (A), & Ab1 against LRRK2900–100 (B). Neuronal cytoplasm (C) was also strongly labelled throughout the cortex by Ab4 & with a consistently more granular pattern by Ab1 (inset in C) in cases of DLB. Control cases display similar, though less intense neuronal labeling (D). Biochemically purified cortical LBs were strongly positive for staining by Ab4 (E) as well as by anti-alpha -synuclein (F), while they were unstained when omitting primary antibody (G). Large vessels (H) were also intensely labelled by Ab4. Scale bars: A, B = 25 μm; C, D = 100 μm; E-G = 25 μm; H = 50 μm. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/17137507), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb300-268_rabbit-polyclonal-lrrk2-antibody-310202415384173.jpg)
![Western Blot: LRRK2 Antibody - BSA Free [NB300-268] - LRRK2 deletion attenuates Mn-induced pro-apoptotic protein levels.(A) After cells (LRRK2 WT & LRRK2 KO) were exposed to Mn (250 μM) for up to 24 h, total protein was extracted & followed by western blot analysis to determine protein levels of Bax & Daxx. beta -actin was used as a loading control. (B) The expression levels of Bax & Daxx modulated by Mn were quantified relative to its control levels in LRRK2 WT & KO cells. **, p < 0.01; ***, p < 0.001 (one-way ANOVA followed by Tukey’s post hoc test; n = 3). The data shown are representative of 3 independent experiments. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/30645642), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb300-268_rabbit-polyclonal-lrrk2-antibody-31020241535611.jpg)
![Immunocytochemistry/ Immunofluorescence: LRRK2 Antibody - BSA Free [NB300-268] - The interaction & phosphorylation of LRRK2 & LC1. (A) Cellular co-localisation of endogenous LRRK2 & MAP1B (LC1). SKNSH cells were labelled with LRRK2 (green) & LC1 (red) antibodies & signals were detected by immunofluorescence. Detailed figure in Additional file 1. (B) LRRK2 kinase assay. The LRRK2 wild-typed (WT) kinase interacted & phosphorylated the LC1 domain unlike the LRRK2 kinase-dead protein. (C) Western blotting of LRRK2 & LC1 proteins after a kinase assay. Both LRRK2 & LC1 proteins were probed for phospho-threonine & phospho-serine signals respectively. Image collected & cropped by CiteAb from the following publication (//molecularbrain.biomedcentral.com/articles/10.1186/1756-6606-7-29), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb300-268_rabbit-polyclonal-lrrk2-antibody-310202415382414.jpg)
![Western Blot: LRRK2 Antibody - BSA Free [NB300-268] - Mn increases LRRK2 kinase activity & expression in RAW 264.7 & HMC3 cells.(A) Two-hundred (200) μg of protein were collected from cell lysates, followed by western blot analysis to determine the presence of LRRK2 in LRRK2 WT, KO RAW 264.7 & HMC3 cells. beta -actin was used as a loading control. (B,C) LRRK2 WT or HMC3 cells were treated with Mn (250 μM) for the designated times, followed by protein extraction & western blot analysis as described in the Methods section. Protein levels of LRRK2 & phosphorylated LRRK2 (S1292) in LRRK2 WT RAW 264.7 (B) & HMC3 (C) cells were quantified. (D,E) Effect of Mn on LRRK2 mRNA levels in LRRK2 WT RAW 264.7 (D) & HMC3 (E) cells were assessed as described in the Methods section. GAPDH was used as a loading control. (F) After pre-treatment with LRRK2 inhibitors GSK (1 μM) & MLi-2 (50 nM) for 90 min, RAW 264.7 cells were exposed to Mn (250 μM) for 20 min, followed by western blot analysis to detect phosphorylation of LRRK2 (S1292). ###, p < 0.001; *, p < 0.05; **, p < 0.01; ***, p < 0.001 compared to the control (one-way ANOVA followed by Tukey’s post hoc test; n = 3). The data shown are representative of 3 independent experiments. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/30645642), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb300-268_rabbit-polyclonal-lrrk2-antibody-31020241621814.jpg)
![Immunohistochemistry-Paraffin: LRRK2 Antibody - BSA Free [NB300-268] - Immunocytochemistry of LRRK2 in PD. Four antibodies raised against sequences corresponding to various regions shown on the schematic diagram of LRRK2 (red bars) were used on brainstem sections of PD (A-H) & age-matched controls (I-L). Intense immunolabeling of brainstem LBs in cases of PD was seen with Ab1 against LRRK2900–100 (A) & Ab4 against LRRK22500–2527(D). Both rim (A & D) & core (inset in D) of LBs were recognized. In contrast, LBs were not labelled in any case using antibodies directed against LRRK21246–1265 (Ab2, B) or LRRK21838–2133 (Ab3, C), for which the antigenic sites are located within the folded domains. The cell bodies of both pigmented & no-pigmented neurons (arrows) as well as axons (arrowheads) contain LRRK2, seen only using antibodies against sites outside the folded domains (Ab1, E & Ab4, H). In contrast, Ab4 staining was much less intense in control tissue (L). The muscle layer of both large & small vessels was consistently found to contain high levels of LRRK2 in almost all PD cases (seen in E, G, & H) & strikingly the vessels are the only structure immunolabeled with Ab3 recognizing LRRK21838–2133 in all cases studied (G & K). Ab2 to LRRK21246–1265 did not recognize LBs, cell bodies or vessels in any case (B, F, & J). Scale bars: A-D & inset = 10 μm; E-L = 100 μm. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/17137507), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb300-268_rabbit-polyclonal-lrrk2-antibody-310202416205168.jpg)
![Immunohistochemistry-Paraffin: LRRK2 Antibody - BSA Free [NB300-268] - Immunocytochemistry of LRRK2 in PD. Four antibodies raised against sequences corresponding to various regions shown on the schematic diagram of LRRK2 (red bars) were used on brainstem sections of PD (A-H) & age-matched controls (I-L). Intense immunolabeling of brainstem LBs in cases of PD was seen with Ab1 against LRRK2900–100 (A) & Ab4 against LRRK22500–2527(D). Both rim (A & D) & core (inset in D) of LBs were recognized. In contrast, LBs were not labelled in any case using antibodies directed against LRRK21246–1265 (Ab2, B) or LRRK21838–2133 (Ab3, C), for which the antigenic sites are located within the folded domains. The cell bodies of both pigmented & no-pigmented neurons (arrows) as well as axons (arrowheads) contain LRRK2, seen only using antibodies against sites outside the folded domains (Ab1, E & Ab4, H). In contrast, Ab4 staining was much less intense in control tissue (L). The muscle layer of both large & small vessels was consistently found to contain high levels of LRRK2 in almost all PD cases (seen in E, G, & H) & strikingly the vessels are the only structure immunolabeled with Ab3 recognizing LRRK21838–2133 in all cases studied (G & K). Ab2 to LRRK21246–1265 did not recognize LBs, cell bodies or vessels in any case (B, F, & J). Scale bars: A-D & inset = 10 μm; E-L = 100 μm. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/17137507), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb300-268_rabbit-polyclonal-lrrk2-antibody-310202416205158.jpg)
![Western Blot: LRRK2 Antibody - BSA Free [NB300-268] - Mn increases LRRK2 kinase activity & expression in RAW 264.7 & HMC3 cells.(A) Two-hundred (200) μg of protein were collected from cell lysates, followed by western blot analysis to determine the presence of LRRK2 in LRRK2 WT, KO RAW 264.7 & HMC3 cells. beta -actin was used as a loading control. (B,C) LRRK2 WT or HMC3 cells were treated with Mn (250 μM) for the designated times, followed by protein extraction & western blot analysis as described in the Methods section. Protein levels of LRRK2 & phosphorylated LRRK2 (S1292) in LRRK2 WT RAW 264.7 (B) & HMC3 (C) cells were quantified. (D,E) Effect of Mn on LRRK2 mRNA levels in LRRK2 WT RAW 264.7 (D) & HMC3 (E) cells were assessed as described in the Methods section. GAPDH was used as a loading control. (F) After pre-treatment with LRRK2 inhibitors GSK (1 μM) & MLi-2 (50 nM) for 90 min, RAW 264.7 cells were exposed to Mn (250 μM) for 20 min, followed by western blot analysis to detect phosphorylation of LRRK2 (S1292). ###, p < 0.001; *, p < 0.05; **, p < 0.01; ***, p < 0.001 compared to the control (one-way ANOVA followed by Tukey’s post hoc test; n = 3). The data shown are representative of 3 independent experiments. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/30645642), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb300-268_rabbit-polyclonal-lrrk2-antibody-310202416205187.jpg)
![<b>Genetic Strategies Validation. </b>Western Blot: LRRK2 Antibody - BSA Free [NB300-268] - Mn increases LRRK2 kinase activity & expression in RAW 264.7 & HMC3 cells.(A) Two-hundred (200) μg of protein were collected from cell lysates, followed by western blot analysis to determine the presence of LRRK2 in LRRK2 WT, KO RAW 264.7 & HMC3 cells. beta -actin was used as a loading control. (B,C) LRRK2 WT or HMC3 cells were treated with Mn (250 μM) for the designated times, followed by protein extraction & western blot analysis as described in the Methods section. Protein levels of LRRK2 & phosphorylated LRRK2 (S1292) in LRRK2 WT RAW 264.7 (B) & HMC3 (C) cells were quantified. (D,E) Effect of Mn on LRRK2 mRNA levels in LRRK2 WT RAW 264.7 (D) & HMC3 (E) cells were assessed as described in the Methods section. GAPDH was used as a loading control. (F) After pre-treatment with LRRK2 inhibitors GSK (1 μM) & MLi-2 (50 nM) for 90 min, RAW 264.7 cells were exposed to Mn (250 μM) for 20 min, followed by western blot analysis to detect phosphorylation of LRRK2 (S1292). ###, p < 0.001; *, p < 0.05; **, p < 0.01; ***, p < 0.001 compared to the control (one-way ANOVA followed by Tukey’s post hoc test; n = 3). The data shown are representative of 3 independent experiments. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/30645642), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb300-268_rabbit-polyclonal-lrrk2-antibody-31020241621239.jpg)
![Western Blot: LRRK2 Antibody - BSA Free [NB300-268] - Mn increases LRRK2 kinase activity & expression in RAW 264.7 & HMC3 cells.(A) Two-hundred (200) μg of protein were collected from cell lysates, followed by western blot analysis to determine the presence of LRRK2 in LRRK2 WT, KO RAW 264.7 & HMC3 cells. beta -actin was used as a loading control. (B,C) LRRK2 WT or HMC3 cells were treated with Mn (250 μM) for the designated times, followed by protein extraction & western blot analysis as described in the Methods section. Protein levels of LRRK2 & phosphorylated LRRK2 (S1292) in LRRK2 WT RAW 264.7 (B) & HMC3 (C) cells were quantified. (D,E) Effect of Mn on LRRK2 mRNA levels in LRRK2 WT RAW 264.7 (D) & HMC3 (E) cells were assessed as described in the Methods section. GAPDH was used as a loading control. (F) After pre-treatment with LRRK2 inhibitors GSK (1 μM) & MLi-2 (50 nM) for 90 min, RAW 264.7 cells were exposed to Mn (250 μM) for 20 min, followed by western blot analysis to detect phosphorylation of LRRK2 (S1292). ###, p < 0.001; *, p < 0.05; **, p < 0.01; ***, p < 0.001 compared to the control (one-way ANOVA followed by Tukey’s post hoc test; n = 3). The data shown are representative of 3 independent experiments. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/30645642), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb300-268_rabbit-polyclonal-lrrk2-antibody-31020241621810.jpg)
![Western Blot: LRRK2 Antibody - BSA Free [NB300-268] - LRRK2 kinase inhibition blocks Tat-induced S935 phosphorylation & inflammatory cytokine expression in BV-2 cells. (A) Western blot depicting pS935-LRRK2 & total LRRK2 protein levels 12 hours after saline or Tat-treatment ± LRRK2 kinase inhibition (LRRK2i). (B) Tat treatment significantly increased pS935-LRRK2, which was attenuated by LRRK2i. (C) We measured TNF-alpha , IL-6, MCP-1 & IL-10 mRNA levels by qRT-PCR 12 hours post saline or Tat treatment ± LRRK2i. LRRK2i attenuated Tat-induced TNF-alpha , IL-6, MCP-1 & IL-10 expression for all groups (*P <0.05, ***P <0.001, one way ANOVA, Newman-Keuls post-test). ANOVA, analysis of variance; LRRK2, leucine-rich repeat kinase2; pS935, phosphorylation of serine 935; Tat, trans activator of transcription. Image collected & cropped by CiteAb from the following publication (//jneuroinflammation.biomedcentral.com/articles/10.1186/1742-2094-9-261), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb300-268_rabbit-polyclonal-lrrk2-antibody-310202416212357.jpg)
![Immunohistochemistry-Paraffin: LRRK2 Antibody - BSA Free [NB300-268] - Immunocytochemistry of LRRK2 in PD. Four antibodies raised against sequences corresponding to various regions shown on the schematic diagram of LRRK2 (red bars) were used on brainstem sections of PD (A-H) & age-matched controls (I-L). Intense immunolabeling of brainstem LBs in cases of PD was seen with Ab1 against LRRK2900–100 (A) & Ab4 against LRRK22500–2527(D). Both rim (A & D) & core (inset in D) of LBs were recognized. In contrast, LBs were not labelled in any case using antibodies directed against LRRK21246–1265 (Ab2, B) or LRRK21838–2133 (Ab3, C), for which the antigenic sites are located within the folded domains. The cell bodies of both pigmented & no-pigmented neurons (arrows) as well as axons (arrowheads) contain LRRK2, seen only using antibodies against sites outside the folded domains (Ab1, E & Ab4, H). In contrast, Ab4 staining was much less intense in control tissue (L). The muscle layer of both large & small vessels was consistently found to contain high levels of LRRK2 in almost all PD cases (seen in E, G, & H) & strikingly the vessels are the only structure immunolabeled with Ab3 recognizing LRRK21838–2133 in all cases studied (G & K). Ab2 to LRRK21246–1265 did not recognize LBs, cell bodies or vessels in any case (B, F, & J). Scale bars: A-D & inset = 10 μm; E-L = 100 μm. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/17137507), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb300-268_rabbit-polyclonal-lrrk2-antibody-31020241621837.jpg)
![Flow Cytometry: LRRK2 Antibody - BSA Free [NB300-268] - Inhibition of LRRK2 kinase activity attenuates Mn-induced apoptosis.(A) After pre-treatment with GSK (1 μM) for 90 min, cells (HMC3) were exposed to Mn (250 μM) for the designated time periods, followed by annexin V & PI staining & flow cytometry analysis to determine apoptosis. Early & late apoptotic cells (Q2 & Q3) were analyzed. (B,C) After pre-treatment with GSK (1 μM) for 90 min, cells (LRRK2 WT RAW 264.7 & HMC3) were exposed to Mn for designated time periods, followed by the MTT assay to determine cell viability, as described in the Methods section, (@@@, p < 0.001; *, p < 0.05; ***, p < 0.001 compared to the control (one-way ANOVA followed by Tukey’s post hoc test; n = 3, apoptosis assay; n = 6, MTT assay). The data shown are representative of 3 independent experiments. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/30645642), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb300-268_rabbit-polyclonal-lrrk2-antibody-31020241621844.jpg)
![Western Blot: GADD153/CHOP Antibody (9C8) [NB600-1335] - Ethanol feeding increases CHOP expression. Image from verified customer review.](http://images.novusbio.com/fullsize/GADD153-CHOP-Antibody-9C8-Western-Blot-NB600-1335-img0011.jpg "Western Blot: GADD153/CHOP Antibody (9C8) [NB600-1335] - Ethanol feeding increases CHOP expression. Image from verified customer review.")
![Immunohistochemistry-Paraffin: GADD153/CHOP Antibody (9C8) [NB600-1335] - FFPE tissue section of mouse brain using 1:100 dilution of GADD153/CHOP antibody. The signal was developed using HRP-DAB based detection method which followed counterstaining of the nuclei with hematoxylin. The antibody generated a cytoplasmic and nuclear staining of CHOP in various cell types in the tested section.](http://images.novusbio.com/fullsize/GADD153-CHOP-Antibody-9C8-Immunohistochemistry-Paraffin-NB600-1335-img0010.jpg)
![Flow Cytometry: GADD153/CHOP Antibody (9C8) [NB600-1335] - An intracellular stain was performed on SK-MEL-28 cells with GADD153/CHOP Antibody (9C8) NB600-1335 (blue) and a matched isotype control MAB004 (orange). Cells were fixed with 4% PFA and then permeabilized with 0.1% saponin. Cells were incubated in an antibody dilution of 2.5 ug/mL for 30 minutes at room temperature, followed by Mouse IgG (H+L) Cross-Adsorbed Secondary Antibody, Dylight 550 (84540, Thermo Fisher).](http://images.novusbio.com/fullsize/GADD153-CHOP-Antibody-9C8-Flow-Cytometry-NB600-1335-img0012.jpg)
![<b>Biological Strategies Validation. </b>Western Blot: GADD153/CHOP Antibody (9C8) [NB600-1335] - GADD153/CHOP expression in HeLa cells treated with 2.5 ug/mL tunicamycin for 4 hours (Lane 1) and untreated (Lane 2).](http://images.novusbio.com/fullsize/GADD153-CHOP-Antibody-9C8-Western-Blot-NB600-1335-img0001.jpg)
![<b>Biological Strategies Validation. </b>Western Blot: GADD153/CHOP Antibody (9C8) [NB600-1335] - Analysis of endogenous CHOP/GADD153 from primary human fibroblasts using NB600-1335. Lane 1: Untreated cells, Lane 2: Cells treated with tunicamycin for 10 hours.](http://images.novusbio.com/fullsize/GADD153-CHOP-Antibody-9C8-Western-Blot-NB600-1335-img0004.jpg)
![Western Blot: GADD153/CHOP Antibody (9C8) [NB600-1335] - Analysis of CHOP in rat heart tissue lysate. Image courtesy of product review submitted by Lee Hsiao-Wei.](http://images.novusbio.com/fullsize/GADD153-CHOP-Antibody-9C8-Western-Blot-NB600-1335-img0005.jpg)
![Immunohistochemistry-Paraffin: GADD153/CHOP Antibody (9C8) [NB600-1335] - FFPE tissue section of mouse brain using 1:100 dilution of GADD153/CHOP antibody. The signal was developed using HRP-DAB based detection method which followed counterstaining of the nuclei with hematoxylin. The antibody generated a cytoplasmic and nuclear staining of CHOP in various cell types in the tested section.](http://images.novusbio.com/fullsize/GADD153-CHOP-Antibody-9C8-Immunohistochemistry-Paraffin-NB600-1335-img0008.jpg)
![Simple Western: GADD153/CHOP Antibody (9C8) [NB600-1335] - Image shows a specific band for CHOP/GADD153 in 1.0 mg/mL of HeLa lysate. This experiment was performed under reducing conditions using the 12-230 kDa separation system.](http://images.novusbio.com/fullsize/GADD153-CHOP-Antibody-9C8-Simple-Western-NB600-1335-img0007.jpg)