Cholesterol Metabolism reagents: Novus Biologicals

NB400-105

ABCA1 Antibody - BSA Free

(7 Reviews)

(408 Publications)

0.1 ml

NB400-105

Formalin-fixed paraffin-embedded tissue sections of human prostate cancer were probed for ABCA1 mRNA (ACD RNAScope Probe, catalog # 432291; Fast Red chromogen, ACD catalog # 322360). Adjacent tissue section was processed for immunohistochemistry using rabbit polyclonal (Novus Biologicals catalog # NB400-105) at 1.5ug/mL with overnight incubation at 4 degrees Celsius followed by incubation with anti-rabbit IgG VisUCyte HRP Polymer Antibody (Catalog # VC003) and DAB chromogen (yellow-brown). Tissue was counterstained with hematoxylin (blue). Specific staining was localized to glandular cells.

<b>Genetic Strategies Validation and Orthogonal Strategies Validation.</b>HSKMCs were transfected with scrambled siRNA (scr siRNA) or ABCA1 siRNA. The cells were lysed and ABCA1 (A) protein levels were quantified by immunoblotting. Image collected and cropped by CiteAb from the following publication (//www.nature.com/articles/s41598-018-38014-3) licensed under under a CC-BY license.

<b>Biological Strategies Validation. </b>Analysis of ABCA1 in total cell lysates of RAW264.9 cells treated with vehicle (-) or 9-cisretinoic acid and 22Rhydroxycholesterol (+). Samples used for this testing were 40 ug of total cell post-nuclear lysate from each group.

<b>Biological Strategies Validation. </b>HepG2 cells were grown to 60% confluency, serum starved for 24 hours, and then treated with 1uM TO9 for 24 hours prior to being fixed for 10 minutes using 10% formalin and then permeabilized for 5 minutes using 1X TBS + 0.5% Triton-X100. The cells were incubated with anti-ABCA1 at 5.0ug/ml overnight at 4C and detected with an anti-rabbit Dylight 488 (Green) at a 1:500 dilution. Alpha tubulin (DM1A) NB100-690 was used as a co-stain at a 1:1000 dilution and detected with an anti-mouse Dylight 550 (Red) at a 1:500 dilution. Nuclei were counterstained with DAPI (Blue). Cells were imaged using a 40X objective.

Untreated HepG2 cells were grown to 60% confluency, and serum starved for 24 hours prior to being fixed for 10 minutes using 10% formalin and then permeabilized for 5 minutes using 1X TBS + 0.5% Triton-X100. The cells were incubated with anti-ABCA1 at 5.0ug/ml overnight at 4C and detected with an anti-rabbit Dylight 488 (Green) at a 1:500 dilution. Alpha tubulin (DM1A) NB100-690 was used as a co-stain at a 1:1000 dilution and detected with an anti-mouse Dylight 550 (Red) at a 1:500 dilution. Nuclei were counterstained with DAPI (Blue). Cells were imaged using a 40X objective.

ABCA-1 FITC conjugated antibody of human adipose tissue macrophage subsets by flow cytometry. Image from verified customer review.

Association between expression of ABCA1 and survival in ovarian cancer patients. Expression of ABCA1 in 55 ovarian cancer patient samples was determined by IHC in tissue microarray. Representative image of ovarian cancer showing high (left panel) and low (right panel) ABCA1 expression on the cell membrane or cytoplasm (x400). Image collected and cropped by CiteAb from the following publication (//www.clinicalepigeneticsjournal.com/content/7/1/1), licensed under a CC-BY license.

ABCA1 in human primary fibroblasts in culture. 10 ug of total protein. 7.5% TGX gel. Blocking 5% milk in PBST 1h RT. 1:1000 primary ab in BSA 3% PBST O/N at 4C. Secondary 1:5000 HRP 1h RT. Arrow shows around 250 kDa. WB image submitted by a verified customer review.

ABCA1 antibody was tested at 1: 400 in HeLa cells using an Alexa Fluor 488 secondary (shown in purple). M1 is defined by unstained cells.

<b>Biological Strategies Validation. </b>Detection of ABCA1 in mouse peritoneal macrophages using NB 400-105 (Lot L). ECL exposure, 1 min. Lane 4: T09 uninduced lysate Lane 5: T09 induced lysate.

Prostates of LXR mutant mice accumulate cholesterol esters through inappropriate LXR target genes regulation. Total protein lysates of WT and LXR null mice under normal or high cholesterol diet were analyzed by western blotting with antibodies against ABCA1, LDLR and ACTIN as a loading control (left panel), quantification of ABCA1 and LDLR protein accumulation levels (right panel). * p<0.05, *** p<0.001 in Student's t test. Error bars represent the +/- mean SEM. Image collected and cropped by CiteAb from the following publication (//dx.plos.org/10.1371/journal.pgen.1003483), licensed under a CC-BY license.

miR-33b reduces cellular cholesterol efflux and serum HDL-C levels. Western blotting for ABCA1 (using NB400-105) and ABCG1 proteins in peritoneal macrophages from WT and KI+/+ mice. Representative images are shown. beta-actin was used as the loading control. Image collected and cropped by CiteAb from the following publication (//www.nature.com/articles/srep05312), licensed under a CC-BY license.

miR-33b regulates ABCA1 and SREBP-1. Analysis for ABCA1, SREBP-1, CPT1a, and AMPK alpha protein levels in the livers of WT, KI+/-, and KI+/+ mice. Representative images are shown. TF2B and beta-actin were used as loading controls. Image collected and cropped by CiteAb from the following publication (//www.nature.com/articles/srep05312), licensed under a CC-BY license.

Detection of ABCA1 in human prostate epithelium showing luminal and membrane staining.

Liver mRNA & protein expression analysis of chow-fed Osbpl8KO mice.A: qPCR analysis of the quantity of the mRNAs identified at the bottom in chow-fed KO females (open bars) & males (closed bars). The mRNAs were quantified using ribosomal protein 36B4 message as a housekeeping reference. The data are expressed relative to quantity in littermate WT animals of the same gender, & represent mean ± s.e.m. (n = 6; *p<0.05, **p<0.01, T-test). B: Western blot analysis of ABCA1 & SR-B1 proteins in WT & KO mouse liver. The blots were probed with anti-beta -actin as a loading control. Densitometric quantification of the Western blot data is shown on the right. The results were normalized against beta -actin. The data represents mean ± s.e.m. (n = 4). Image collected & cropped by CiteAb from the following publication (//dx.plos.org/10.1371/journal.pone.0058856), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Protein expressions of ABCA1, SR-BI & ABCG1 in liver & macrophage by Western blot. Simvastatin increased the expressions of ABCA1 & ABCG1 in liver & ABCA1 in macrophage, Both L-4F & the combination group improved the expressions of ABCA1, SR-BI & ABCG1 in liver & ABCA1 & ABCG1 in macrophage. 1P < 0.05, 2P < 0.001, vs. AS group; aP < 0.05, bP < 0.001, vs. Simva group;*P < 0.05, **P < 0.001, vs. L-4F group. Image collected & cropped by CiteAb from the following publication (//lipidworld.biomedcentral.com/articles/10.1186/1476-511X-12-180), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

ABCA1, ABCG1 & SR-BI protein expressions. a & b Hepatic protein expressions of ABCA1, ABCG1 & SR-BI were significantly decreased in COMT−/− mice at GD 18.5, compared to C57BL/6 J mice. Decreased hepatic ABCA1 expression was also observed at 10 days postpartum. ATI-5261 increased ABCA1 & ABCG1 expression in the liver at 10 days postpartum. c Placental protein expressions of ABCA1 & ABCG1 was reduced in COMT−/− mice, compared to C57BL/6 J mice. ATI-5261 treatment significantly increased ABCA1 levels in the placenta of COMT−/− mice. d Representative immunoblots of the corresponding proteins in the placenta with mouse RAW264.7 cell lysate included as positive control. Similar results were obtained when the experiment was repeated with lysates prepared from three batches of tissues. Data are presented as mean ± SEM. Groups (n = 8 in all groups) were compared using one-way ANOVA with post-hoc analysis (Tukey’s procedure). *, p < 0.05 Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/30237900), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Effects of 13-HODE & LA in the presence & absence of PPAR alpha & PPAR gamma selective antagonists on molecular markers of cholesterol homeostasis in RAW264.7 macrophages. RAW264.7 cells were pre-treated without or with the PPAR alpha selective antagonist GW6471 or the PPAR gamma selective antagonist GW9662 & subsequently treated without (vehicle control) or with 2.5 μmol/L 13-HODE or 100 μmol/L LA for 24 h. Afterwards, cells were lysed & subsequently processed for western blotting as described in the materials & methods section. A, Representative immunoblots specific for ABCA1, ABCG1, SR-BI, LXR alpha , & beta -actin which was used for normalization are shown. B, Bars represent data from densitometric analysis & are means ± SD from three independent experiments (n = 3). Data are expressed as percentage of protein concentration of vehicle control cells. Results from statistical analysis are indicated: Significant effects are denoted with superscript letters. Bars marked without a common superscript letter significantly differ (P < 0.05). Image collected & cropped by CiteAb from the following publication (//lipidworld.biomedcentral.com/articles/10.1186/1476-511X-10-222), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: ABCA1 Antibody - BSA Free [NB400-105] - (A) Upregulation of ABCA1 & ABCG1 & (B) enhancement of cholesterol efflux by purple Perilla frutescens extracts (PPE) in 50 μg/ml Cu2+-oxidized low-density lipoproteins (LDL)-exposed J774A.1 murine macrophages. (A) For the measurement of ABCA1 & ABCG1 expression, total cell lysates were subjected to western blot analysis with a primary antibody against ABCA1 or ABCG1. beta -actin was used as an internal control. Bar graphs (means ± SEM, n=3) represent quantitative densitometric results of the upper bands. (B) Cholesterol efflux was expressed as the percentage of fluorescence in the medium relative to the total fluorescence. Bar graphs denoted without a common letter indicate significant difference, P<0.05. Image collected & cropped by CiteAb from the following publication (//www.spandidos-publications.com/10.3892/ijmm.2015.2101), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: ABCA1 Antibody - BSA Free [NB400-105] - 6‐Dihydroparadol increases A) ABCA1 & B) ABCG1, but not C) SR‐BI protein levels in cholesterol‐loaded THP‐1‐derived macrophages. THP‐1 cells were differentiated as described in Figure 2, & then loaded with unlabeled cholesterol for 24 h. Cells were treated with increasing concentrations of 6‐dihydroparadol (1–30 μm) for another 24 h. The protein levels of ABCA1, ABCG1, & SR‐B1 were detected by Western blot analysis. The control was treated with solvent vehicle (0.1% DMSO). As a positive control, TO901317 (5 μm, 24 h) was used. The bar graphs represent mean ± SD from three independent experiments. *p < 0.05, **p < 0.01, & ***p < 0.001 versus control (determined by Student's t‐test or ANOVA with Bonferroni's post hoc test). Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/29802792), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: ABCA1 Antibody - BSA Free [NB400-105] - Akt inhibition suppresses mTORC1 activity.BHK-ABCA1 cells were induced overnight with mifepristone (10 nM) & then incubated with DEBC, LY294002 or rapamycin at indicated concentrations for 2 h. Cells were then lysed & analyzed for ABCA1 & phosphorylated S6K by Western blotting. Actin was also blotted as loading control. Image collected & cropped by CiteAb from the following publication (//dx.plos.org/10.1371/journal.pone.0113789), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: ABCA1 Antibody - BSA Free [NB400-105] - Reversal of hepatic steatosis by reduction of SREBP-1 levels.(a) Western blotting analysis of SREBP-1 & ABCA1 levels in livers of miR-33+/+Srebf1+/+, miR-33+/+Srebf1+/−, miR-33−/−Srebf1+/+ & miR-33−/−Srebf1+/− mice. Representative western blot images are shown (n=4). Image collected & cropped by CiteAb from following publication (//pubmed.ncbi.nlm.nih.gov/24300912), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: ABCA1 Antibody - BSA Free [NB400-105] - 6‐Dihydroparadol increases A) ABCA1 & B) ABCG1 protein stability. THP‐1 cells were differentiated as described in Figure 2. Then cells were loaded with unlabeled cholesterol & treated with 6‐dihydroparadol (10 μm), or solvent vehicle (0.1% DMSO, control) for 24 h. Cells were lysed at different time points (0, 1, 2, 3, 4, & 6 h) after treatment with the protein synthesis inhibitor cycloheximide (CHX, 100 μm). The protein levels of both ABCA1 & ABCG1 were detected by Western blot analysis. The data points represent mean ± SD from three independent experiments. *p < 0.05 & **p < 0.01 versus control at the same time point (determined by Student's t‐test). Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/29802792), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: ABCA1 Antibody - BSA Free [NB400-105] - Ligand activation of LXR inhibits LPS-induced MAP kinase activation through Abca1 induction.(A–D) Bone marrow-derived macrophages from Lxr alpha −/−Lxr beta −/− & control wild-type mice (A, B), or bone marrow-derived macrophages from myeloid-specific Abca1−/− & control wild-type mice (C, D) were pretreated with GW3965 (1 µM) overnight, followed by stimulation with LPS (10 ng/ml) for 20 min or 1 hr. Whole cell lysates were harvested & protein expression was analyzed by immunoblotting with the indicated antibodies (A, C). Protein expression was quantified by Image Quant TL7.0 (B, D). N = 4–6 per group. *p < 0.05, **p < 0.01, NS, not significant. Error bars represent means ± SEM.DOI://dx.doi.org/10.7554/eLife.08009.012 Image collected & cropped by CiteAb from the following publication (//elifesciences.org/articles/08009), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: ABCA1 Antibody - BSA Free [NB400-105] - Western Blotting for ABCA1, as detailed in Supplementary Protocol #5 (Additional file 1). Caco-2 cells cultivated on filter inserts were treated for 48 h with bexarotene (RXR agonist, 5 μM), T0901317 (LXR agonist, 10 μM), GW3965 (LXR agonist, 10 μM) or the vehicle control (DMSO 0.1%). Protein expression was then determined by western blot analysis. Results were normalized for interexperimental variance & then set in relation to the vehicle control. Bar graphs represent mean ± SD from three independent experiments. A representative blot is shown - the bands stem from the same membrane & the vertical line indicates excised irrelevant bands. ns not significant, *P < 0.05, **P < 0.01 versus solvent vehicle (determined by paired t-test) Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/32308567), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: ABCA1 Antibody - BSA Free [NB400-105] - Expression of ABCA1 & CROT in livers & RIP140 in macrophages is elevated in miR-33−/−Apoe−/− mice compared with miR-33+/+Apoe−/− mice. A, Quantitative real-time PCR analysis of Abca1, Crot, Cpt1a, & Prkaa1in livers from miR-33+/+Apoe−/− & miR-33−/−Apoe−/− mice. Values from miR-33+/+Apoe−/− mice were set at 100%. Values are mean±SE (n=9 to 11each); **P<0.01. B, Western analysis of ABCA1, CROT, CPT1a, & AMPK alpha in livers from miR-33+/+Apoe−/− & miR-33−/−Apoe−/− mice. beta -actin was used as a loading control. C, Densitometry of ABCA1, CROT, CPT1a, & AMPK alpha in livers from miR-33+/+Apoe−/− & miR-33−/−Apoe−/− mice. Values from miR-33+/+Apoe−/− mice were set at 100%. Values are mean±SE (n=4 each); *P<0.05. D, Total cholesterol, free cholesterol, cholesterol ester, & triglyceride levels in livers of miR-33+/+Apoe−/− & miR-33−/−Apoe−/− mice. Values are mean±SE (n=9 to 11 each). E, HE staining of livers of miR-33+/+Apoe−/− & miR-33−/−Apoe−/− mice at age 20 weeks fed NC. Scale bar: 100 μm. F, Quantitative real-time PCR analysis of Nrip1 (RIP140) in peritoneal macrophages from miR-33+/+Apoe−/− & miR-33−/−Apoe−/− mice. Values from miR-33+/+Apoe−/− mice were set at 100%. Values are mean±SE (n=7 each). G, Western analysis of NRIP1 (RIP140) in peritoneal macrophages from miR-33+/+Apoe−/− & miR-33−/−Apoe−/− mice. GAPDH was used as a loading control. H, Densitometry of NRIP1 (RIP140) in peritoneal macrophages from miR-33+/+Apoe−/− & miR-33−/−Apoe−/− mice. Values from miR-33+/+Apoe−/− mice were set at 100%. Values are mean±SE (n=4 each); *P<0.05. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/23316322), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: ABCA1 Antibody - BSA Free [NB400-105] - Basal ABCA1 expression & function in patient-derived iRPEs. (A) Representation of patient-derived iPSC lines & genotypes harboring polymorphisms in ABCA1 that are associated with decreased or increased risk for AMD development. (B) Relative expression of ABCA1 mRNA in patient-derived iRPEs under basal conditions normalized to RPL28 & decreased risk group. (C) Western blot analysis of ABCA1 levels in patient-derived iRPEs under basal conditions. Actin was detected as loading control. ABCA1 expression was quantified & normalized to actin. (D,E) Relative expression of ABCG1 (D) & NR1H3 (E) mRNA in patient-derived iRPEs under basal conditions normalized to RPL28 & decreased risk group. (F) Cholesterol efflux in patient-derived iRPEs after direct cell labeling & in the presence of ApoAI. (G) Cholesterol efflux in patient-derived iRPEs after phagocytosis of BODIPY-cholesterol-loaded POSs & in the presence of ApoAI. (H) Quantification of phagocytosed POSs per nuclei in patient-derived iRPEs. Values shown are means ± SD (n = 3). * p < 0.05; *** p < 0.001. Unpaired Student’s t-test. (I) Representative fluorescence microscopy images of phagocytosed FITC-labeled POSs (green) & staining for ZO-1 (red) & DAPI (blue) of increased risk cell line IPS19-00096. Scale bar = 100 μm. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/35328615), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: ABCA1 Antibody - BSA Free [NB400-105] - A–C) Effects of 6‐dihydroparadol & specific proteasomal, lysosomal, & calpain inhibitors on the ABCA1 protein levels. THP‐1 cells were differentiated as described in Figure 2, & then loaded with unlabeled cholesterol for 24 h. Cells were treated with or without 6‐dihydroparadol (6‐DP, 30 μm) for 24 h & incubated for another 3 h with or without the proteasome inhibitor lactacystin (10 μm), the lysosomal inhibitor chloroquine (100 μm), or the calpain inhibitor calpeptin (30 μg mL−1). The ABCA1 protein levels were detected by Western blot analysis. The bar graphs represent mean ± SD from three independent experiments. *p < 0.05, **p < 0.01, & ***p < 0.001 versus control; n.s., not significant versus control (determined by Student's t‐test or ANOVA with Bonferroni's post hoc test). Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/29802792), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: ABCA1 Antibody - BSA Free [NB400-105] - Suppressive effects of Ucn1 on foam cell formation & related protein expression in human monocyte-derived macrophages.Human monocytes were incubated for 7 days with RPMI-1640 supplemented with 10% human serum & the indicated concentrations of Ucn1, followed by a 19 h-incubation with 50 µg/ml oxLDL in the presence of 0.1 mmol/l [3H]oleate. Intracellular CE accumulation was determined from the radioactivity of cholesterol-[3H]oleate. Otherwise, before the addition of oxLDL, cells were harvested & subjected to immunoblotting analyses for CD36, ACAT1, or ABCA1. beta -Actin served as a loading control. Data are expressed as means ± SEM from 4–6 independent experiments with monocytes from 4–6 different donors. Baseline (1 fold) = 8.4±2.2 nmol/mg cell protein. *P<0.05, †P<0.001 vs. 0 nmol/l of Ucn1. Image collected & cropped by CiteAb from the following publication (//dx.plos.org/10.1371/journal.pone.0110866), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: ABCA1 Antibody - BSA Free [NB400-105] - Effect of evodiamine on ABCA1 transcription & the degradation rate of ABCA1 protein. (a) Differentiated THP-1 macrophages were incubated with 10 μM evodiamine or 10 μM pioglitazone as positive control for 24 h. Total RNA was extracted & ABCA1 mRNA expression levels were quantified by qRT-PCR. (b) 293 T cells were transfected with a luciferase reporter construct driven by the human ABCA1 promoter as described in the Materials & Methods section. After transfection, cells were treated with 10 μM Evodiamine or 1 μM T0901317 as positive control for 24 h. (c) Differentiated THP-1 macrophages were incubated for 24 h with (black circle) or without (Veh; white circle) evodiamine (10 μM) & lysed after addition of cycloheximide (CHX; 140 μM) at different time points (0, 10, 20, 40 min). Western blot analysis shows the decline of ABCA1 protein level with cycloheximide in the presence & absence of evodiamine. All data are means ± S.D. (n = 3) vs. solvent vehicle control (DMSO), *p < 0.05, **p < 0.01, n.s. no significance (ANOVA/Bonferroni). Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/30038271), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: ABCA1 Antibody - BSA Free [NB400-105] - miR-33 deficiency improved cholesterol efflux in macrophages. A, Quantitative real-time PCR analysis of Abca1 & Abcg1 in macrophages from miR-33+/+Apoe−/− & miR-33−/−Apoe−/− mice. Values from miR-33+/+Apoe−/− were set at 100%. Values are mean±SE (n=7 each); ***P<0.001. B, Western blotting analysis of ABCA1 & ABCG1 in thioglycollate-elicited peritoneal macrophages from miR-33+/+Apoe−/− & miR-33−/−Apoe−/− mice. GAPDH was used as a loading control. C, Cholesterol efflux from thioglycollate-elicited peritoneal macrophages in the presence or absence of apoA-I (5 or 10 μg/mL). Values are mean±SE (n=6 each); **P<0.01. D, Cholesterol efflux from thioglycollate-elicited peritoneal macrophages in the presence or absence of HDL-C (50 or 100 μg/mL). Values are mean±SE (n=6 each); **P<0.01. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/23316322), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: ABCA1 Antibody - BSA Free [NB400-105] - Srebf1 is a miR-33 target gene.(a) Relative changes in lipid metabolism-related genes in the livers of miR-33−/− mice compared with miR-33+/+ mice fed NC at 16 weeks of age. (n=5–8 each,*P<0.05 in Student’s t-test). (b) Conservation of miR-33 target regions in the 3′UTR of Srebf1. Underlined sequences are the potential binding site of miR-33 seed sequences. * indicates the conservation among spieces. (c) 3′UTR reporter assay used to verify the target. Luciferase reporter activity of human & mouse SREBP-1 gene 3′UTR constructs in 293T cells overexpressing miR-control (miR-Con) & miR-33 (n=4 each, *P<0.05 & ***P<0.001 in Student’s t-test). (d) miR-33 dose-dependent changes in luciferase reporter activity of mouse Srebf1 3′UTR construct in 293T cells. miR-Con & miR-146a is used as a negative control (n=4 each, *P<0.05 & ***P<0.001 in one-way analysis of valiance test). (e) Luciferase reporter activity of the WT or mutant Srebf1 3′UTR at the potential miR-33 binding site in 293T cells (n=4 each, **P<0.01 in Student’s t-test). (f,g) Luciferase reporter activity of SRE-promoter (f) or FAS-promoter (g) in 293T cells. 293T cells were co-transfected with mouse Srebf1 with the full-length 3′UTR or without the 3′UTR, along with expression plasmids for miR-negative control, or miR-33. Values are the mean±s.e. (n=4 each, **P<0.01 versus miR-Con. ***P<0.001 versus miR-Con in one-way analysis of valiance test). (h) Western blotting analysis of SREBP-1, ABCA1, & IRS-2 in miR-33 transduced HepG2 cells & primary hepatocytes & hepatocytes prepared from miR-33+/+ & miR-33−/− mice. Representative western blot images are shown (n=4). Values are the means±s.e.m. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/24300912), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: ABCA1 Antibody - BSA Free [NB400-105] - (A) Chemical structure, (B) cytotoxicity of alpha -asarone, (C) enhancement of cholesterol efflux by alpha -asarone, (D & E) upregulation of ABCA1 & ABCG1 by alpha -asarone & beta -asarone, & (F) elevation of retinoid X receptor (RXR) alpha transcription. J774A.1 murine macrophages were exposed to 50 μg/ml oxidized low-density lipoprotein (LDL) & treated with 1–10 μM purple Perilla frutescens extracts (PPE)-alpha -asarone & 5–10 μM beta -asarone. (B) MTT assay was performed for the measurement of alpha -asarone toxicity. Graph data represent 1 of 4 independent experiments with multiple estimations. Values are expressed as the percentage cell survival relative to the untreated control cells (cell viability, 100%). (C) Cholesterol efflux was expressed as the percentage fluorescence in the medium relative to total fluorescence. (D & E) For the measurement of ABCA1 & ABCG1 expression, total cell lysates were subjected to western blot analysis with a primary antibody against ABCG1 or ABCG1. beta -actin was used as an internal control. Bar graphs (means ± SEM, n=3) represent quantitative densitometric results of the upper bands. Bar graphs denoted without a common letter indicate significant difference, P<0.05. (F) RXR alpha mRNA expression was measured by RT-PCR. GAPDH was used as a housekeeping gene for the co-amplification with RXR alpha . Image collected & cropped by CiteAb from the following publication (//www.spandidos-publications.com/10.3892/ijmm.2015.2101), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: ABCA1 Antibody - BSA Free [NB400-105] - Bilirubin significantly decreases expression of ATP‐binding cassette transporter A1 (ABCA1) protein in THP‐1 macrophages treated with LXR agonist (TO901317) to upregulate ABCA1 protein. THP‐1 cells were differentiated for 72 hours with 200 nmol/L phorbol‐12‐myristate‐13‐acetate & then loaded with unlabeled cholesterol for another 24 hours. Cells were treated with TO901317 (5 μmol/L) or solvent vehicle (0.1% dimethyl sulfoxide [DMSO]) for 24 hours. Afterward, cells were treated with bilirubin (17.1 μmol/L) or solvent vehicle (0.1% DMSO) for 16 hours. The protein levels of ABCA1 were detected by western blot analysis. The bar graphs present mean±SD from 3 independent experiments. ***P<0.001 vs control (determined by ANOVA with Bonferroni post hoc test). Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/28455345), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: ABCA1 Antibody - BSA Free [NB400-105] - Induction of cholesterol efflux attenuates the enhancement in HIV-1infectivity in NPCD55 cells. (A) Normal & NPCD55 cells were treated with 5 μM TO-901317 at 24 h post-infection & cultured for 72 h in the presence of the compound. At 96 h post-infection the cells were harvested & ABCA1, Gag, & beta -actin expression was detected by Western blotting analysis. All samples were loaded on the same gel. (B) AmplexRed assay was performed to measure free cholesterol content of untreated (filled) & TO-901317-treated (slashed) cells. Cholesterol content was normalized to protein concentration. (C) AmplexRed assay was performed to measure virion-associated cholesterol from purified virus produced in untreated (filled) & TO-901317-treated (slashed) infected cells. Virion-associated cholesterol content was normalized to p24 concentration. (D) TZM-bl reporter assay was performed to measure virus infectivity when cholesterol efflux was induced via TO-901317 stimulation. The ρ values were calculated by performing student T-test (*denotes < 0.05). Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/22273177), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: ABCA1 Antibody - BSA Free [NB400-105] - Effects of apabetalone on ABCA1 expression & carboplatin response in ovarian cancer cells. (A) Apabetalone treatment reduced expression of ABCA1 in OVCAR-5 & OVCAR-5 CBPR cell lines. Cells were treated for 72 h with control medium (DMSO) or apabetalone (80 µM). Protein extracts from OVCAR-5 (~30 µg) were electrophoresed & immunoblotted with rabbit polyclonal ABCA1 antibody (1/1000, NB400-105, Novus Biological) & beta -actin (1/2000, Abcam) was used as a loading control. (B) Quantification of Western blot. OVCAR-5 (C), CaOV3 (D), OVCAR-5 CBPR (E) & CaOV3 CBPR (F) cell survival following treatment with carboplatin (CBP) alone (0-200 µM, black line) & in combination with apabetalone (Apa, 80 µM, purple line). (G) Carboplatin IC50 for OVCAR-5 & OVCAR-5 CBPR cells ± apabetalone. Data are mean ± SEM from three independent experiments. *P < 0.05, Student’s t-test. (H) Carboplatin IC50 for CaOV3 & CaOV3 CBPR cells ± apabetalone. Data are mean ± SEM from three independent experiments. P < 0.05, Student’s t-test. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/35582032), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: ABCA1 Antibody - BSA Free [NB400-105] - Expression of ATP‐binding cassette transporter A1 (ABCA1) protein in THP‐1 macrophages treated with bilirubin & in peripheral blood mononuclear cells (PBMCs) from Gilbert syndrome (GS) patients. A, Bilirubin suppresses the expression of ABCA1 protein in THP‐1‐derived macrophages time‐dependently. THP‐1 cells were differentiated as described in Figure 1 & then loaded with unlabeled cholesterol for another 24 hours. Cells were treated with bilirubin (17.1 μmol/L) for 4, 8, 16, & 24 hours. The protein levels of ABCA1 were detected by western blotting. Control was treated with solvent vehicle (0.1% dimethyl sulfoxide). The bar graph presents mean±SD from 3 independent experiments. B, Expression of ABCA1 protein is decreased in PBMCs from participants with high bilirubin blood levels (GS) compared with healthy controls. The protein levels of ABCA1 were detected by western blotting. The bar graph presents mean±SEM (n=28 per group). *P<0.05, **P<0.01 & ***P<0.001 vs control. ns indicates not significant (determined by Student t test). Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/28455345), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: ABCA1 Antibody - BSA Free [NB400-105] - (A) Time course response of ABCA1 induction by pioglitazone, & (B) enhancement of ABCA1 & (C) peroxisome proliferator-activated receptor gamma (PPAR gamma ) by purple Perilla frutescens extracts (PPE). J774A.1 murine macrophages were incubated with 10 μM pioglitazone & 50 μg/ml oxidized low-density lipoprotein (LDL) in the absence or presence of 1–10 μg/ml PPE. For the measurement of expression of (A & B) ABCA1 & (C) PPAR gamma , total cell lysates were subjected to western blot analysis with a primary antibody against ABCA1 or PPAR gamma . beta -actin was used as an internal control. Bar graphs (means ± SEM, n=3) represent quantitative densitometric results of the upper bands. Bar graphs denoted without a common letter indicate significant difference, P<0.05. Image collected & cropped by CiteAb from the following publication (//www.spandidos-publications.com/10.3892/ijmm.2015.2101), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: ABCA1 Antibody - BSA Free [NB400-105] - LXR agonist-stimulated ABCA1 expression & function in patient-derived iRPEs. Patient-derived iRPE lines were stimulated for 16 h with LXR agonist & are relative to unstimulated cells shown in Figure 2. (A) Expression of ABCA1 mRNA normalized to RPL28 & relative to unstimulated cells shown in Figure 2B. (B) Western blot analysis of ABCA1 protein levels. Actin was detected as loading control. ABCA1 expression was quantified & normalized to actin. (C) Cholesterol efflux assay after direct cell labeling & in the presence of ApoAI. (D) Cholesterol efflux assay after phagocytosis of BODIPY-cholesterol-loaded POSs & in the presence of ApoAI. Data are relative to unstimulated cells shown in Figure 2F,G, respectively. Data are presented as means ± SD (n = 3). Unpaired Student’s t-test. * p < 0.05. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/35328615), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: ABCA1 Antibody - BSA Free [NB400-105] - Akt inhibition by LY294002 or Akt1/2 also enhances cholesterol efflux to apoA-I from ABCA1-expressing BHK cells.A) BHK cells were induced as in Fig. 1 & then incubated with LY294002 (200 µM) for 2 h. Cells were then lysed & analysed for ABCA1, phosphorylated Akt (p-Akt) & total Akt by Western-blotting. Hsp70 was also blotted as loading control. B & C) BHK cells were labeled with [3H] cholesterol & induced with 10 nM mifepristone overnight. Cholesterol efflux was measured after 2 h incubation with BSA (1 mg/ml) or BSA plus apoA-I (5 µg/ml). Some of cells were also incubated with indicated doses of LY294002 (B) or Akt1/2 (C), in addition to apoA-I, during 2 h efflux period. Results are presented as the average of triplicate wells with standard deviation & representative of more than three independent experiments. *** P<0.0001, **P<0.001 & *P<0.05 vs apoA-I only. Image collected & cropped by CiteAb from the following publication (//dx.plos.org/10.1371/journal.pone.0113789), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: ABCA1 Antibody - BSA Free [NB400-105] - Generation, differentiation & analysis of ABCA1-deficient iRPEs. (A) Immunofluorescence staining for ZO-1 (red) in 4-week cultured iRPEs. Nuclei were stained with DAPI (blue). Scale bar = 100 μm. (B) Bright-field microscopy of iRPEs. (C) Ct values of RPE marker genes BEST1, OTX2, RLBP1 & RPE65 in iRPEs & parental iPSCs obtained by qPCR. Values shown are means ± SD (n = 3). Unpaired Student’s t-test. **** p < 0.0001. (D) Sequence alignment of parts of exon 14 (top) & exon 46 (bottom) of ABCA1-deficient iRPE cell clones & parental line. (E) Western blot of ABCA1 protein levels in ABCA1-deficient iRPE cell lines & parental cell line after 16 h of stimulation with 1 μM LXR agonist. Actin was detected as loading control. (F) Relative expression of ABCA1 mRNA in ABCA1-deficient iRPE cell lines & parental cell line normalized to ACTB. Values shown are means ± SD (n = 3). One-way ANOVA with Tukey’s post hoc test. **** p < 0.0001. (G) Relative expression of ABCG1 mRNA in ABCA1-deficient iRPE cell lines & parental cell line normalized to ACTB. Values shown are means ± SD (n = 3). One-way ANOVA with Tukey’s post hoc test. ** p < 0.01; *** p < 0.001. (H) Cholesterol efflux assay in iRPEs in the presence of ApoAI and/or LXR agonist (LXR ag). Values shown are means ± SD (n = 3). Two-way ANOVA with Bonferroni post hoc test vs. DMSO + BSA control. **** p < 0.0001. (I) Bright-field (BF) microscopy & Nile Red fluorescence microscopy (overview & close-up view marked with white squares) of 4-week cultured ABCA1-deficient iRPE cell lines & parental cell line. Relative fluorescence was quantified & is shown as mean ± SD (n = 8). One-way ANOVA with Tukey’s post hoc test. * p < 0.05, **** p < 0.0001. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/35328615), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: ABCA1 Antibody - BSA Free [NB400-105] - Akt inhibition enhances cholesterol efflux to apoA-I from wt MEFs, but not from TSC2-/- MEFs where mTORC1 is constitutively activated.A) Mouse embryonic fibroblasts (MEFs), wt & TSC2-/-, were induced overnight with T0901317 (10 µM). Cell lysates were collected for Western blotting for phosphorylated S6K & total S6K. B) wt & TSC2-/- MEFs were incubated with or without T0901317 (10 µM) overnight. Some of cells were then incubated with apoA-I (10 µg/ml) or apoA-I plus DEBC (25 µM) for 2 h. The expression of ABCA1, phosphorylated Akt, total Akt & loading control hsp70 were analyzed by Western blotting. C) wt & TSC2-/- were labeled with [3H] cholesterol for 1 day & then incubated with or without T0901317 (10 µM) overnight. Some of cells were then incubated with apoA-I (10 µg/ml) or apoA-I plus DEBC (25 µM) for 2 h to analyze cholesterol efflux. Data presented as the average of triplicate wells with standard deviation & representative of at least three independent experiments. *** P<0.0001 vs apoA-I only. Image collected & cropped by CiteAb from the following publication (//dx.plos.org/10.1371/journal.pone.0113789), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: ABCA1 Antibody - BSA Free [NB400-105] - Akt inhibition by DEBC enhances cholesterol efflux to apoA-I specifically from ABCA1-expressing BHK cells.A) BHK-ABCA1 cells were induced with mifepristone (10 nM) overnight & then incubated with indicated doses of DEBC for 2 h. Cells were then lysed & Western-blotted for ABCA1, phosphorylated Akt (p-Akt) & total Akt. Hsp70 was also blotted as loading control. B) BHK-ABCA1 cells were labeled with [3H] cholesterol & induced overnight as above. After 2 h incubation with BSA (1 mg/ml) or BSA plus apoA-I (5 µg/ml), cholesterol efflux was measured as described in the Methods section. Some of the cells were also incubated with indicated doses of DEBC, in addition to apoA-I, during 2 h efflux period. C) BHK-ABCA1 & BHK-A937V cells were induced with mifepristone (10 nM) overnight. 2 h Cholesterol efflux was measured as above either with or without DEBC (25 µM). Results are presented as the average of triplicate wells with standard deviation & representative of more than three independent experiments. *** P<0.0001 & **P<0.001 vs apoA-I only. Image collected & cropped by CiteAb from the following publication (//dx.plos.org/10.1371/journal.pone.0113789), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: ABCA1 Antibody - BSA Free [NB400-105] - LXRs control expression of genes involved in cholesterol homeostasis & fatty acid synthesis in MPECs.(A) qPCR analysis of Abca1, Abcg1 & Idol levels in WT (+/+) & Lxr alpha beta −/− (lxr−/−) MPECs after DMSO (vehicle) or T0901317 stimulation (B) Effect of 9-cis retinoic acid and/or T0901317 stimulation on Abca1 accumulation levels in WT (+/+) & Lxr alpha beta −/− (lxr−/−) MPECs (C) qPCR analysis of Srebp1, Acc, & Fas levels in WT (+/+) & Lxr alpha beta −/− (lxr−/−) MPECs after DMSO (vehicle) or T0901317 stimulation. (qPCR analysis results from 4 independant experiments & was normalized using 36b4 gene). *p<0.05, **p<0.01, ***p<0.001 in Student’s t test. Error bars represent mean ± SEM. (D) Western blot analysis was performed on WT (+/+) or Lxr alpha beta −/− MPECs using Srebp1c, Abca1 & beta -Actin antibodies. (E) Oil-Red O staining (ORO) & Normarski/Dapi of WT (+/+) & Lxr alpha beta −/− MPECs, or WT MEFs, treated for 48h with DMSO (vehicle) or T0901317 (1 µM). Head arrows indicate lipid droplets. Scale bars 100 µm. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/23554947), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: ABCA1 Antibody - BSA Free [NB400-105] - Anti-ApoA-1 IgGs upregulate ABCA1. ABCA1 was increased after 16 & 24 h of anti-ApoA-1 IgG exposure to HMDM at the mRNA level as revealed by RT-PCR (a) as well as at the protein level after 24 h anti-apoA-1 IgG stimulation, as revealed by Western blot analysis (b). In panel a, data are expressed as fold change expression of the mean ± SD of ABCA1 calculated by delta delta CT method of six independent experiments (n = 6) & values were normalized to untreated condition. p-values were calculated using the Student’s t-test: * p < 0.05, ** p < 0.01, **** p < 0.0001. (b) One of four representative Western blots is shown. Data are the mean ± SD of band intensity volume/actin intensity volume of four independent experiments (n = 4). p-values were calculated using the Student’s t-test: * p = 0.02, ** p = 0.005. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31766415), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: ABCA1 Antibody - BSA Free [NB400-105] - ABCA1 protein expression is upregulated in ovarian cancer cells with acquired carboplatin resistance. ABCA1 expression in OVCAR-5 (A) & CaOV3 (C) & carboplatin resistant OVCAR-5 CBPR (B) & CaOV3 CBPR (D) by immunocytochemistry using rabbit polyclonal ABCA1 antibody (1/100, NB400-105, Novus Biological). (E) OVCAR-5 cells with Rabbit IgG & (F) CaOV3 cells with Rabbit IgG. (G) Protein extracts from OVCAR-5 (~30 µg) & CaOV3 cell lines (~60 µg) were electrophoresed & immunoblotted with rabbit polyclonal ABCA1 antibody (1/1000, NB400-105, Novus Biological), & beta -actin (1/2000, Abcam) was used as a loading control. A major band was detected at ~250 kDa, which is the predicted size for ABCA1. (H) Quantitation of ABCA1 Western blots. Data are from 2-4 independent experiments. Statistical significance was determined using the Student’s t-test, *P < 0.05. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/35582032), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: ABCA1 Antibody - BSA Free [NB400-105] - Evodiamine enhances apo A1-mediated ChE from THP-1 macrophages & increases ABCA1 protein level. (a) Differentiated THP-1 cells were loaded with [3H]-cholesterol together with the indicated treatments for 24 h. On the next day, the cells were washed twice with PBS & incubated with the same compounds [solvent vehicle control (Veh; ≤0.1% DMSO), evodiamine (1–20 μM), & the PPAR gamma agonist pioglitazone (10 μM) as positive control] with or without 10 µg/mL apo A1. Extracellular as well as intracellular radioactivities were quantified with scintillation counter. Differentiated THP-1-derived macrophages were treated with solvent vehicle control (Veh; ≤0.1% DMSO), evodiamine (10 μM), & the PPAR gamma agonist pioglitazone (10 μM) as positive control. After 24 h incubation, the cells were lysed & 20 μg protein was resolved via SDS-PAGE. Immunodetection was performed with antibodies against the indicated proteins, ABCA1 (b), ABCG1 (c), & SR-B1 (d), & visualized by chemiluminescence detection. All experiments were performed at least three times & data are presented as means ± S.D. vs. solvent vehicle control, *p < 0.05, **p < 0.01, ***p < 0.001, n.s. no significance (ANOVA/Bonferroni). Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/30038271), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: ABCA1 Antibody - BSA Free [NB400-105] - Functional miR-33 responsive elements in the 3′UTR of ATP8B1 & ABCB11A,B. Conserved sequences in the 3′UTR of ATP8B1 & ABCB11 are partially complementary to miR-33. The element in human ATP8B1 is located 1877–1897 nt after the stop codon. The element in ABCB11 overlaps the stop codon in primates, while rodents show a conserved sequence 732–751 nt after the stop codon.C,D. Luciferase assays in HEK293 cells using the whole 3′UTR of human or murine ATP8B1 & ABCB11, or a single copy of the responsive elements (RE) identified above, or mutant responsive elements (RE*; where AATGCA was mutated to GGGTTG to prevent complementarity to the seed sequence of the miRNA), co-transfected with (closed bars) or without (open bars) a vector to overexpress miR-33. In grey, data from empty (negative control) & R33 (positive control containing a 100% match to miR-33) reporter vectors.E,F. Relative mRNA expression of canalicular transporters in primary murine hepatocytes (n = 4 dishes/condition) & human HuH-7 hepatoma cells (n = 3 dishes/condition) transduced 48 h with empty or miR-33 adenovirus.G. Relative protein levels in HuH7 cells transduced with empty or miR-33 adenovirus. Some cells were incubated for 16 h in the presence of FXR:RXR agonists (2 µmol/L GW4064 : 1 µmol/L 9-cis-retinoic acid) to induce ABCB11. Asterisk indicates a non-specific band. Data shown as mean ± SD; **p < 0.01. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/22767443), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: ABCA1 Antibody - BSA Free [NB400-105] - Gas6 treatment enhances expression of LXR alpha & LXR beta & their target genes in BMDM.Mouse BMDM were stimulated with 400 ng/ml Gas6, 1 μM T0901317, 10 ng/ml interferon (IFN)-gamma , 10 ng/ml IL-4, or 100 ng/ml LPS for 4 h (a,b) or 400 ng/ml Gas6 for the indicated times (c–g). (a,b,e) The amounts of the LXR alpha , LXR beta , ABCA1, ABCG1, ApoE, AIM, Arg2, VEGF, YM1, & Arg1 mRNAs were analyzed by real-time PCR & normalized to that of Hprt mRNA. (c,d,f,g) The relative abundances of LXR alpha , LXR beta , ABCA1, ABCG1, ApoE, Aim, Arg2, & VEGF proteins were determined by Western blotting analysis. The relative densitometric intensity was determined for each band & normalized to beta -actin. Data in all bar graphs are means ± SEM of three independent experiments. *P < 0.05 compared with control. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/27406916), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: ABCA1 Antibody - BSA Free [NB400-105] - (A) Time course response of ABCA1 induction by TO-091317 & (B) upregulation of ABCA1 by purple Perilla frutescens extracts (PPE), & (C) enhancement of liver X receptor (LXR) alpha induction by PPE. J774A.1 murine macrophages were cultured with 1 μM TO-091317 or 50 μg/ml Cu2+-oxidized low-density lipoprotein (LDL) in the absence or presence of 1–10 μg/ml PPE. For the measurement of expression of (A & B) ABCA1 & (C) LXR alpha , total cell lysates were subjected to western blot analysis with a primary antibody against ABCA1 or LXR alpha . beta -actin was used as an internal control. Bar graphs (means ± SEM, n=3) represent quantitative densitometric results of the upper bands. Bar graphs denoted without a common letter indicate significant difference, P<0.05. Image collected & cropped by CiteAb from the following publication (//www.spandidos-publications.com/10.3892/ijmm.2015.2101), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Reactivity:

Hu, Mu, Rt, Po, Ca, Ch, ChHa, Eq, Ha, Md, Pm, Rb

Species Glossary

Reactivity: Hu, Mu, Rt, Po, Ca, Ch, ChHa, Eq, Ha, Md, Pm, Rb

Applications:

, , , , , , , , , , , , , , , ,

Applications: , , , , , , , , , , , , , , , ,

Host:

Rabbit Polyclonal

Host: Rabbit Polyclonal

Sizes:

Sample Size Available

Sizes: Sample Size Available

Conjugate:

Unconjugated

Available Conjugates:

Validated by:

Validated by:

Conjugate	Catalog #	Availability	Size	Price
Alexa Fluor 350	NB400-105AF350
Alexa Fluor 405	NB400-105AF405
Alexa Fluor 488	NB400-105AF488
Alexa Fluor 532	NB400-105AF532
Alexa Fluor 594	NB400-105AF594
Alexa Fluor 647	NB400-105AF647
Alexa Fluor 700	NB400-105AF700
Alexa Fluor 750	NB400-105AF750
Allophycocyanin	NB400-105APC
Allophycocyanin/Cy7	NB400-105APCCY7
Biotin	NB400-105B
CoraFluor 1	NB400-105CL1
DyLight 350	NB400-105UV
DyLight 405	NB400-105V
DyLight 488	NB400-105G
DyLight 550	NB400-105R
DyLight 594	NB400-105DL594
DyLight 650	NB400-105C
DyLight 680	NB400-105FR
DyLight 755	NB400-105IR
FITC	NB400-105F
HRP	NB400-105H
Janelia Fluor 525	NB400-105JF525
Janelia Fluor 549	NB400-105JF549
Janelia Fluor 646	NB400-105JF646
Janelia Fluor 669	NB400-105JF669
PE	NB400-105PE
PE/Atto594	NB400-105PEATT594
PE/Cy5.5	NB400-105PECY55
PE/Cy7	NB400-105PECY7
PerCP	NB400-105PCP
mFluor Violet 450 SE	NB400-105MFV450
mFluor Violet 500 SE	NB400-105MFV500
mFluor Violet 610 SE	NB400-105MFV610

Available Formulations

Formulation	Catalog #	Availability	Price
BSA Free	NB400-105SS

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NBP1-04676

PGC1 alpha Antibody - BSA Free

(11 Reviews)

(278 Publications)

0.1 ml

NBP1-04676

Mitochondrial content and biogenesis. Immunoblot analysis of PGC1 alpha in MEFs (n = 7; t = 5.764; df = 6). Image collected and cropped by CiteAb from the following publication (//www.nature.com/articles/s41598-017-12662-3), licensed under a CC-BY license.

HeLa cells were fixed in 4% paraformaldehyde for 10 minutes and permeabilized in 0.5% Triton X-100 in PBS for 5 minutes. The cells were incubated with anti-PGC1 alpha Antibody NBP1-04676 at 2 ug/ml overnight at 4C and detected with an anti-rabbit 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.

Analysis of a FFPE section of mouse prostate using rabbit polyclonal PGC1 alpha Antibody at 1:200 dilution. The antibody generated an expected strong nuclear (punctate in some cells) and a weak cytoplasmic staining in the glandular cells lining of tubule-alveolar gland.

An intracellular stain was performed on A431 cells with PGC1 alpha Antibody NBP1-04676 (blue) and matched isotype control NBP2-24891 (orange). Cells were fixed with 4% PFA and then permeabilized with 0.1% saponin. Cells were incubated in an antibody dilution of 1.0 ug/mL for 30 minutes at room temperature, followed by Rabbit IgG (H+L) Cross-Adsorbed Secondary Antibody, Dylight 550 (SA5-10033, Thermo Fisher).

<b>Biological Strategies Validation. </b>Vehicle or RU 486 (5 mg/kg) injected mice were presented with/without corticosterone (10 mg/kg) for 3 days. The expressions of peroxisome proliferator-activated receptor gamma coactivator 1-alpha (PGC1 alpha NBP1-04676) and NIX (BNIP3L NBP1-88558) were visualized via western blotting. Loading control is beta-actin. n = 5. Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/33473105/) licensed under a CC-BY license.

Total protein from human adipose and skeletal muscle tissue, HeLa and A431 cells lines 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 PGC1 alpha Antibody (Molecular weight: 91 KDa) in 1% non-fat milk in TBST and detected with an anti-rabbit HRP secondary antibody using chemiluminescence

Western Blot of total protein from murine skeletal muscle tissue using PGC1 alpha Antibody. Image from verified customer review.

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 PGC1 alpha Antibody [NBP1-04676] at a 1:200 dilution overnight at 4C and detected with an anti-rabbit DyLight 488 (Green) at a 1:500 dilution. Alpha tubulin (DM1A) [NB100-690] was used as a co-stain at a 1:1000 dilution and detected with an anti-mouse DyLight 550 (Red) at a 1:500 dilution. Nuclei were counterstained with DAPI (Blue). Cells were imaged using a 40X objective.

Analysis of PGC1 alpha Antibody in mouse prostate using DAB with hematoxylin counterstain.

An intracellular stain was performed on HeLa cells with NBP1-04676AF647 (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.

An intracellular stain was performed on HepG2 cells with PGC1 alpha Antibody 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.

<b>Genetic Strategies Validation. </b>Western blot shows lysates of A431 human squamous carcinoma parental cell line and PGC1 alpha knockout (KO) A431 cell line. PVDF membrane was probed with 1:1000 of Rabbit Polyclonal PGC1 alpha Antibody (Catalog # NBP1-04676) followed by HRP-conjugated Anti-Rabbit IgG Secondary Antibody (Catalog #HAF008). Specific band was detected for PGC1 alpha at approximately 105 kDa (as indicated) in the parental A431 cell line, but is not detectable in the knockout A431 cell line. This experiment was conducted under reducing conditions.

DM1-derived fibroblasts have no changes in mitochondria biogenesis. (A, B) Representative images of immunofluorescence of TOMM20, and PGC1-alpha in DM1 and control fibroblasts (n=3). (C) Medium fluorescence intensity of MitoTracker Red FM in control (n=3) and DM1 cells (n=5) and (D) of Rhodamine 123 in DM1 and control fibroblasts (n=3). (E) mRNA levels of TFAM transcription factor (n=3). (F) mRNA levels of OPA1, MFN1, MFN2, DRP1 and PARKIN in DM1 and control fibroblasts (n≥2).

A431 human skin carcinoma cell line was stained with Rabbit anti-PGC1 alpha Affinity-purified Polyclonal Antibody conjugated to Phycoerythrin (Catalog # NBP1-04676PE, blue histogram) or matched control antibody (Catalog # NBP2-24983, orange histogram).

Western Blot: PGC1 alpha Antibody - BSA Free [NBP1-04676] - Effect of butein T on SC adipose tissue browning in the ThermoMouse. SC fat was obtained from ThermoMouse exposed for 4 days to butein (10 or 20 mg/kg; n = 4) or vehicle (n = 2). A BAT lysate of a ThermoMouse was used as a positive control for UCP-1 protein levels. Tissues were homogenized & protein lysates (50 µg for SC fat & 10 µg for BAT) were used in western blotting for PGC1-alpha (a) & UCP-1 (c). Panels (b) & (d) illustrate the densitometric quantitation of the PGC1-alpha & UCP-1 western blot, respectively, normalized for the levels of the loading control alpha -tubulin. Abbreviations: subcutaneous (SC); brown adipose tissue (BAT); peroxisome proliferator-activated receptor-gamma coactivator 1-alpha (PGC1-alpha ) & uncoupling protein-1 (UCP-1). Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31094273), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: PGC1 alpha Antibody - BSA Free [NBP1-04676] - Expression of the mitochondrial biogenesis proteins: SIRT1, PGC1 alpha , TFAM & SIRT3 in H1299, H1299r, P31 & P31r cell lysates as determined by immunoblot analysisWhole cell lysates were prepared from confluent cultures of H1299, H1299r, P31 & P31r cells. Proteins (90 μg) were resolved in 10% SDS-PAGE gels & transferred to a PVDF membrane. Blots were probed for SIRT1, PGC1 alpha , TFAM & SIRT3 or the loading control gamma -tubulin. Figure shows representative blots of (A) of SIRT1, (B) PGC1 alpha , (C) SIRT3, (D) TFAM protein expression; each from three independent experiments. Image collected & cropped by CiteAb from the following publication (//www.oncotarget.com/lookup/doi/10.18632/oncotarget.21885), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: PGC1 alpha Antibody - BSA Free [NBP1-04676] - Maternal exercise during pregnancy on mitochondrial biogenesis in the fetal hearts. (A) Levels of relative mRNA expression measured by qRT‐PCR. n = 9–12/group. Maternal exercise during pregnancy did not alter levels of mRNA in Ppargc1a & Tfam, while it significantly upregulated the levels of mRNA in Nrf1 & Nrf2. (B–D) Densitometric analyses of protein expression levels relative to the sedentary group with representative images of western blots were shown. No significant differences in PGC‐1 alpha , NRF1, & NRF2 (P > 0.05). n = 5–6/group. * P < 0.05, significantly different from the sedentary group. Black bar: fetal hearts from sedentary dams; gray bar: fetal hearts from exercised dams. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/28292876), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Immunocytochemistry/ Immunofluorescence: PGC1 alpha Antibody - BSA Free [NBP1-04676] - DM1-derived fibroblasts have no changes in mitochondria biogenesis. (A, B) Representative images of immunofluorescence of TOMM20, & PGC1-alpha in DM1 & control fibroblasts (n=3). (C) Medium fluorescence intensity of MitoTracker Red FM in control (n=3) & DM1 cells (n=5) & (D) of Rhodamine 123 in DM1 & control fibroblasts (n=3). (E) mRNA levels of TFAM transcription factor (n=3). (F) mRNA levels of OPA1, MFN1, MFN2, DRP1 & PARKIN in DM1 & control fibroblasts (n≥2). Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/32310829), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: PGC1 alpha Antibody - BSA Free [NBP1-04676] - Effect of BGP-15 treatment on the regulation of mitochondrial biogenesis in NRCM cells. Western blot analysis of PGC-1-alpha , CREB, & VDAC proteins as well as densitometric evaluation is shown. GAPDH was used as a loading control. Control group: cells without any treatment; BGP-15 group: cells with only 50 μM BGP-15 for 0.5 hours; H2O2 group: cells with 150 μM H2O2 for 0.5 hours; H2O2+BGP-15 group: cells with 150 μM H2O2 & 50 μM BGP-15 for 0.5 hours. Values are mean ± SEM (n = 4). ∗p < 0.05 vs. Control, ∗∗p < 0.01 vs. Control, §§p < 0.01 vs H2O2 group. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/33728024), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: PGC1 alpha Antibody - BSA Free [NBP1-04676] - Feeding the diabetes mellitus (DM) mice with the RSV‐enriched diet improved mitochondrial biogenesis in the quadriceps muscle. A) Representative western blots using antibodies against nuclear respiratory factor (NRF‐1), ATP synthase, H+ transporting, mitochondrial F1 complex, beta polypeptide (ATP5B), cytochrome c oxidase subunit IV (Cox IV), peroxisome proliferator‐activated receptor‐ gamma coactivator 1‐ alpha (PGC‐1 alpha ), & GAPDH. After quantification, the B) NRF‐1/GAPDH, C) ATP5B/GAPDH, D) Cox IV/GAPDH, & E) PGC‐1 alpha /GAPDH ratios were calculated in mice fed either the control (CTL) or RSV‐enriched diet. GAPDH was used as a loading control. F) Representative western blots using antibodies against mitochondrial transcription factor A (mtTFA) & voltage‐dependent anion channel (VDAC), & the mtTFA/VDAC ratio was determined. The mitochondrial protein VDAC was used as a loading control. Data are expressed as fold change versus CTL & reported as mean ± SD, n = 4–6 per group; *p < 0.05; **p < 0.01 between CTL & DM groups. #p < 0.05 between DM & DM+RSV groups; ††p < 0.05 between CTL+RSV & DM+RSV groups. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/29578301), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: PGC1 alpha Antibody - BSA Free [NBP1-04676] - Effects of SRTAW04 on expression of markers of mitochondrial & anti-oxidant function. (a) Western blot of protein extracts from optic nerve & retina of control (lanes 1–4), MHV-A59 infected (lanes 5–8), & MHV-A59 infected + SRTAW04-treated (lanes 9–12) mice. Average levels of SDHb measured by Western blotting (n = 4/group) showed a significant (*p < 0.05) decrease in protein extracts from optic nerves (a,b) & retinas (a,d) of MHV-A59 infected mice 7 days post-inoculation, compared to control mice. MHV-A59 infected mice treated with SRTAW04 (100 mg/kg/day) showed a significant increase (@p < 0.05) of SDHb protein expression compared to untreated MHV-A59 infected mice. There is a significant decrease (*p < 0.05) in expression of SOD2 (n = 4/group) in optic nerves (a,c) & retinas (a,e) of MHV-A59 infected mice compared to control mice, & treatment with SRTAW04 significantly (@p < 0.05) attenuates that change. PGC1-alpha expression shows a significant (*p < 0.05) decrease in retinas (a,f) (n = 4/group) during MHV-A59 infection & treatment with SRTAW04 for 7 days significantly (@p < 0.05) increases the PGC1-alpha protein levels. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/24383546), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: PGC1 alpha Antibody - BSA Free [NBP1-04676] - RSV treatment increases markers of mitochondrial function in stressed RGC-5 cells. Staurosporine-differentiated RGC-5 cells were cultured with or without 500 μM H2O2, & with or without 0.25 μM RSV for 24 h. (A) Western blot analysis shows a significant decrease in SDH expression (**p < 0.01) during H2O2 treatment which is attenuated by treatment with RSV (*p < 0.05). (B) Western blot analysis shows similar effects on SOD2 expression. The significant decrease (**p < 0.01) during H2O2 treatment, compared to controls, is not found in cells treated with RSV (*p < 0.05). (C) Protein extracts were immunoprecipitated with anti-PGC-1 alpha antibodies, blotted, & hybridized with anti-PGC-1 alpha & anti-acetylated lysine antibodies to assess the acetylation state of PGC-1 alpha . H2O2 treatment significantly increases the proportion of acetylated PGC-1 alpha (*p < 0.05) compared to controls, & RSV & SRTAW04 treatment each prevent this acetylation (*p < 0.05). Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/23293585), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: PGC1 alpha Antibody - BSA Free [NBP1-04676] - Pequi extract increases expression of antioxidant enzymes in HCAEC. Cells were cultured, pre-treated with pequi extract (25 μg/mL) for 24 h under normoxia conditions, & total protein content was extracted for Western blots analysis for Superoxide dismutase (SOD)-1 (A), SOD-2 (B), catalase (C), glutathione peroxidase—GPx (D), sirtuin 1—SIRT-1 (E), peroxisome-proliferator-activated receptor gamma coactivator 1-alpha (PCG1-alpha ) (F), glycogen synthase kinase 3 beta (GSK3 beta ) (G), & microtubule-associated protein 1A/1B-light chain 3 (LC3) (H). Western blots were normalized using alpha -tubulin or glyceraldehyde 3-phosphate dehydrogenase (GAPDH) as loading control. Five independent Western blot experiments were carried for each condition. Representative images are shown here. Statistical analysis was performed using Student’s t-test (p < 0.05). OD: Optical Density. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/35326129), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

$Immunocytochemistry/ Immunofluorescence: PGC1 alpha Antibody - BSA Free [NBP1-04676] - Role of PGC1 alpha in NIX-dependent mitophagy.a–e Nontargeting (NT) or GR siRNA was transfected to hippocampal neurons & SH-SY5Y cells for 24 h prior to corticosterone & cortisol for 12 h, respectively. a, b Peroxisome proliferator-activated receptor gamma coactivator 1-alpha (PGC1 alpha ) expression was detected in western blot where beta -actin was used as a loading control in both cell types. n = 5. c Colocalization of PGC1 alpha (red) & DAPI (blue) in hippocampal neurons was visualized with SRRF imaging system. Scale bars, 20 μm (magnification, ×1000). n = 5. d Colocalization of PGC1 alpha (green) & DAPI (blue) in SH-SY5Y was visualized with SRRF imaging system. Scale bars, 20 μm (magnification, ×1000). n = 5. e PGC1 alpha protein expressions in subcellular fraction samples were detected by western blotting. Lamin A/C & alpha -tubulin were used as a nuclear & cytosolic loading control, respectively. n = 5. f, g SH-SY5Y cells were transfected with pcDNA3.1/c-eGFP or pcDNA3.1/PPARGC1A-c-eGFP vector for 24 h prior to cortisol treatment for 24 h. f NIX expression was detected in western blot where beta -actin was used as a loading control. n = 5. g TOMM20 levels were detected by western blot. Loading control for western blot is beta -actin. n = 5. All blots & immunofluorescence images are representative. n = 5 from independent experiments with two technical replicates each. Quantitative data are presented as a mean ± S.E.M. Two-sided two-way ANOVA was conducted. ** indicates p < 0.01 versus control. #, ## indicates p < 0.05, p < 0.01 versus corticosterone in hippocampal neurons & cortisol in SH-SY5Y, respectively. Data are provided as a Source data file. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/33473105), licensed under a CC-BY license. Not internally tested by Novus Biologicals.$

$Western Blot: PGC1 alpha Antibody - BSA Free [NBP1-04676] - Role of PGC1 alpha in NIX-dependent mitophagy.a–e Nontargeting (NT) or GR siRNA was transfected to hippocampal neurons & SH-SY5Y cells for 24 h prior to corticosterone & cortisol for 12 h, respectively. a, b Peroxisome proliferator-activated receptor gamma coactivator 1-alpha (PGC1 alpha ) expression was detected in western blot where beta -actin was used as a loading control in both cell types. n = 5. c Colocalization of PGC1 alpha (red) & DAPI (blue) in hippocampal neurons was visualized with SRRF imaging system. Scale bars, 20 μm (magnification, ×1000). n = 5. d Colocalization of PGC1 alpha (green) & DAPI (blue) in SH-SY5Y was visualized with SRRF imaging system. Scale bars, 20 μm (magnification, ×1000). n = 5. e PGC1 alpha protein expressions in subcellular fraction samples were detected by western blotting. Lamin A/C & alpha -tubulin were used as a nuclear & cytosolic loading control, respectively. n = 5. f, g SH-SY5Y cells were transfected with pcDNA3.1/c-eGFP or pcDNA3.1/PPARGC1A-c-eGFP vector for 24 h prior to cortisol treatment for 24 h. f NIX expression was detected in western blot where beta -actin was used as a loading control. n = 5. g TOMM20 levels were detected by western blot. Loading control for western blot is beta -actin. n = 5. All blots & immunofluorescence images are representative. n = 5 from independent experiments with two technical replicates each. Quantitative data are presented as a mean ± S.E.M. Two-sided two-way ANOVA was conducted. ** indicates p < 0.01 versus control. #, ## indicates p < 0.05, p < 0.01 versus corticosterone in hippocampal neurons & cortisol in SH-SY5Y, respectively. Data are provided as a Source data file. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/33473105), licensed under a CC-BY license. Not internally tested by Novus Biologicals.$

Western Blot: PGC1 alpha Antibody - BSA Free [NBP1-04676] - EMPA treatment increased mitochondrial biogenesis. (A) Left, Transmission electron microscopy showing the morphology of mitochondria in sham, sham + EMPA, TAC & TAC + EMPA groups & Right, quantitative analysis of mitochondrial size & counts. Results are expressed as mean ± SEM, n = 3–5, *p < 0.05 vs. corresponding sham, †p < 0.05 vs. corresponding TAC. (B) Left, Representative blots of mitochondrial biogenesis-related proteins & Right, quantitative results. (C) Relative mRNA levels of PGC1 alpha , NRF1, TFAM & COX1. Results are expressed as mean ± SEM, n = 5–7, *p < 0.05 vs. corresponding sham group, †p < 0.05 vs. corresponding TAC vehicle group. One-way ANOVA & Tukey post hoc test. EMPA, empagliflozin; SEM, standard error of the mean; TAC, transverse aortic constriction; PGC1-alpha , peroxisome proliferator-activated receptor gamma coactivator 1-alpha; NRF-1, nuclear respiratory factor 1; TFAM, mitochondrial transcription factor A; COX1, cyclooxygenase1; GAPDH, glyceraldehyde 3-phosphate dehydrogenase. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/35647080), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

$Immunocytochemistry/ Immunofluorescence: PGC1 alpha Antibody - BSA Free [NBP1-04676] - Role of PGC1 alpha in NIX-dependent mitophagy.a–e Nontargeting (NT) or GR siRNA was transfected to hippocampal neurons & SH-SY5Y cells for 24 h prior to corticosterone & cortisol for 12 h, respectively. a, b Peroxisome proliferator-activated receptor gamma coactivator 1-alpha (PGC1 alpha ) expression was detected in western blot where beta -actin was used as a loading control in both cell types. n = 5. c Colocalization of PGC1 alpha (red) & DAPI (blue) in hippocampal neurons was visualized with SRRF imaging system. Scale bars, 20 μm (magnification, ×1000). n = 5. d Colocalization of PGC1 alpha (green) & DAPI (blue) in SH-SY5Y was visualized with SRRF imaging system. Scale bars, 20 μm (magnification, ×1000). n = 5. e PGC1 alpha protein expressions in subcellular fraction samples were detected by western blotting. Lamin A/C & alpha -tubulin were used as a nuclear & cytosolic loading control, respectively. n = 5. f, g SH-SY5Y cells were transfected with pcDNA3.1/c-eGFP or pcDNA3.1/PPARGC1A-c-eGFP vector for 24 h prior to cortisol treatment for 24 h. f NIX expression was detected in western blot where beta -actin was used as a loading control. n = 5. g TOMM20 levels were detected by western blot. Loading control for western blot is beta -actin. n = 5. All blots & immunofluorescence images are representative. n = 5 from independent experiments with two technical replicates each. Quantitative data are presented as a mean ± S.E.M. Two-sided two-way ANOVA was conducted. ** indicates p < 0.01 versus control. #, ## indicates p < 0.05, p < 0.01 versus corticosterone in hippocampal neurons & cortisol in SH-SY5Y, respectively. Data are provided as a Source data file. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/33473105), licensed under a CC-BY license. Not internally tested by Novus Biologicals.$

$Western Blot: PGC1 alpha Antibody - BSA Free [NBP1-04676] - Role of PGC1 alpha in NIX-dependent mitophagy.a–e Nontargeting (NT) or GR siRNA was transfected to hippocampal neurons & SH-SY5Y cells for 24 h prior to corticosterone & cortisol for 12 h, respectively. a, b Peroxisome proliferator-activated receptor gamma coactivator 1-alpha (PGC1 alpha ) expression was detected in western blot where beta -actin was used as a loading control in both cell types. n = 5. c Colocalization of PGC1 alpha (red) & DAPI (blue) in hippocampal neurons was visualized with SRRF imaging system. Scale bars, 20 μm (magnification, ×1000). n = 5. d Colocalization of PGC1 alpha (green) & DAPI (blue) in SH-SY5Y was visualized with SRRF imaging system. Scale bars, 20 μm (magnification, ×1000). n = 5. e PGC1 alpha protein expressions in subcellular fraction samples were detected by western blotting. Lamin A/C & alpha -tubulin were used as a nuclear & cytosolic loading control, respectively. n = 5. f, g SH-SY5Y cells were transfected with pcDNA3.1/c-eGFP or pcDNA3.1/PPARGC1A-c-eGFP vector for 24 h prior to cortisol treatment for 24 h. f NIX expression was detected in western blot where beta -actin was used as a loading control. n = 5. g TOMM20 levels were detected by western blot. Loading control for western blot is beta -actin. n = 5. All blots & immunofluorescence images are representative. n = 5 from independent experiments with two technical replicates each. Quantitative data are presented as a mean ± S.E.M. Two-sided two-way ANOVA was conducted. ** indicates p < 0.01 versus control. #, ## indicates p < 0.05, p < 0.01 versus corticosterone in hippocampal neurons & cortisol in SH-SY5Y, respectively. Data are provided as a Source data file. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/33473105), licensed under a CC-BY license. Not internally tested by Novus Biologicals.$

$Western Blot: PGC1 alpha Antibody - BSA Free [NBP1-04676] - Mitochondrial content & PGC‐1 alpha levels are increased in cells with greater TFEB protein expression. (a) Mitochondrial content was measured in SH‐SY5Y cells & TFEB‐DDK cells under basal conditions by assaying citrate synthase (CS) activity. **p < 0.01 versus SH‐SY5Y; n = 6. (b) Western blotting for the mitochondrial proteins prohibitin 1 & cytochrome oxidase (COX) subunit IV also indicated that mitochondrial content was increased in TFEB‐DDK cells. (c) PGC‐1 alpha mRNA levels were measured in SH‐SY5Y cells & TFEB‐DDK cells under basal conditions by qPCR. Data normalised against beta ‐actin mRNA levels. **p < 0.01 versus SH‐SY5Y cells; n = 3. (d) SH‐SY5Y cells were treated with scrambled (scram) or TFEB siRNA for 72 h & PGC‐1 alpha mRNA levels measured. *p < 0.05 versus scram; n = 4. (e) PGC‐1 alpha protein levels were detected by western blotting in total cell lysates of SH‐SY5Y cells, TFEB‐DDK cells & a SH‐SY5Y cell line over‐expressing human PGC‐1 alpha . The fold increase in PGC‐1 alpha protein density for this blot & PGC‐1 alpha mRNA levels of the respective cell lines are reported underneath the blot. (f) TFEB‐DDK cells were treated with 10 μM carbonyl cyanide m‐chlorophenylhydrazone (CCCP) for 18 h & cytosolic & nuclear fractions prepared. PGC‐1 alpha protein was detected in cytosolic (3.5% of total volume) & nuclear fractions (35% of total volume) by western blotting. The purity of the nuclear & cytosolic fractions was assessed by western blotting using lamin A & beta ‐actin antibodies respectively. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/26509433), licensed under a CC-BY license. Not internally tested by Novus Biologicals.$

Western Blot: PGC1 alpha Antibody - BSA Free [NBP1-04676] - PGC1 alpha & HNF4 alpha interacts & binds to Vnn1 promoter in IUGR asthmatic mice. Asthma was induced with OVA in IUGR mice. PBS induction was used as the control. Nuclear protein was extracted from lung tissues. (A) Immunoblot assay was performed for expressions of PGC1 alpha & HNF4 alpha . (B) IP was performed using mouse anti-HNF4 alpha antibody & Protein G-coupled agarose beads, followed by immunoblot with rabbit-anti-PGC1 alpha antibody. The normal mouse IgG was used as the IP control. (C) In primary cultured bronchial epithelia cells isolated from IUGR mice injected with OVA or PBS, ChIP assay was performed using mouse anti-HNF4 alpha or rabbit anti-PGC1 alpha antibodies. The normal mouse or rabbit IgG was used as the control. Graphics show the percentage of total DNA immunoprecipitated by each indicated antibody. Data are shown as mean±s.d. n=4. *P<0.01 OVA versus PBS. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/32139393), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

$Western Blot: PGC1 alpha Antibody - BSA Free [NBP1-04676] - Role of PGC1 alpha in NIX-dependent mitophagy.a–e Nontargeting (NT) or GR siRNA was transfected to hippocampal neurons & SH-SY5Y cells for 24 h prior to corticosterone & cortisol for 12 h, respectively. a, b Peroxisome proliferator-activated receptor gamma coactivator 1-alpha (PGC1 alpha ) expression was detected in western blot where beta -actin was used as a loading control in both cell types. n = 5. c Colocalization of PGC1 alpha (red) & DAPI (blue) in hippocampal neurons was visualized with SRRF imaging system. Scale bars, 20 μm (magnification, ×1000). n = 5. d Colocalization of PGC1 alpha (green) & DAPI (blue) in SH-SY5Y was visualized with SRRF imaging system. Scale bars, 20 μm (magnification, ×1000). n = 5. e PGC1 alpha protein expressions in subcellular fraction samples were detected by western blotting. Lamin A/C & alpha -tubulin were used as a nuclear & cytosolic loading control, respectively. n = 5. f, g SH-SY5Y cells were transfected with pcDNA3.1/c-eGFP or pcDNA3.1/PPARGC1A-c-eGFP vector for 24 h prior to cortisol treatment for 24 h. f NIX expression was detected in western blot where beta -actin was used as a loading control. n = 5. g TOMM20 levels were detected by western blot. Loading control for western blot is beta -actin. n = 5. All blots & immunofluorescence images are representative. n = 5 from independent experiments with two technical replicates each. Quantitative data are presented as a mean ± S.E.M. Two-sided two-way ANOVA was conducted. ** indicates p < 0.01 versus control. #, ## indicates p < 0.05, p < 0.01 versus corticosterone in hippocampal neurons & cortisol in SH-SY5Y, respectively. Data are provided as a Source data file. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/33473105), licensed under a CC-BY license. Not internally tested by Novus Biologicals.$

Reactivity:

Hu, Mu, Rt, Po, Gt, Ha, Sh, Sq, Ca, Eq, Pm

Species Glossary

Reactivity: Hu, Mu, Rt, Po, Gt, Ha, Sh, Sq, Ca, Eq, Pm

Applications:

, , , , , , , ,

Applications: , , , , , , , ,

Host:

Rabbit Polyclonal

Host: Rabbit Polyclonal

Sizes:

Sample Size Available

Sizes: Sample Size Available

Conjugate:

Unconjugated

Available Conjugates:

Validated by:

Validated by:

Conjugate	Catalog #	Availability	Size	Price
Alexa Fluor 350	NBP1-04676AF350
Alexa Fluor 405	NBP1-04676AF405
Alexa Fluor 488	NBP1-04676AF488
Alexa Fluor 532	NBP1-04676AF532
Alexa Fluor 594	NBP1-04676AF594
Alexa Fluor 647	NBP1-04676AF647
Alexa Fluor 700	NBP1-04676AF700
Alexa Fluor 750	NBP1-04676AF750
Allophycocyanin	NBP1-04676APC
Biotin	NBP1-04676B
CoraFluor 1	NBP1-04676CL1
DyLight 350	NBP1-04676UV
DyLight 405	NBP1-04676V
DyLight 488	NBP1-04676G
DyLight 550	NBP1-04676R
DyLight 594	NBP1-04676DL594
DyLight 650	NBP1-04676C
DyLight 680	NBP1-04676FR
DyLight 755	NBP1-04676IR
FITC	NBP1-04676F
HRP	NBP1-04676H
Janelia Fluor 525	NBP1-04676JF525
Janelia Fluor 549	NBP1-04676JF549
Janelia Fluor 646	NBP1-04676JF646
Janelia Fluor 669	NBP1-04676JF669
PE	NBP1-04676PE
PerCP	NBP1-04676PCP
mFluor Violet 450 SE	NBP1-04676MFV450
mFluor Violet 500 SE	NBP1-04676MFV500
mFluor Violet 610 SE	NBP1-04676MFV610

Available Formulations

Formulation	Catalog #	Availability	Price
BSA Free	NBP1-04676SS

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NB400-104

SR-BI Antibody - BSA Free

(5 Reviews)

(234 Publications)

0.1 ml

NB400-104

Immunocytochemistry/Immunofluorescence: SR-BI Antibody [NB400-104] - SR-BI antibody was tested in human fibroblast samples fixed in 4% PFA and permeabilized in PBS (0.2% Tween). Primary incubation overnight at 4C using a 1:100 dilution in PBS (0.1% Tween) with 1% BSA. Secondary antibody is anti-rabbit conjugate to Alexa Fluor 488. SR-BI is shown in green and nucleus in blue (Hoescht 33342 stain).

Flow Cytometry: SR-BI Antibody [NB400-104] - An intracellular stain was performed on HeLa cells with SR-BI antibody NB400-104AF488 (blue) and a matched isotype control NBP2-24893AF488 (orange). Cells were fixed with 4% PFA and then permeablized with 0.1% saponin. Cells were incubated in an antibody dilution of 5 ug/mL for 30 minutes at room temperature. Both antibodies were conjugated to Alexa Fluor 488.

Western Blot: SR-BI Antibody [NB400-104] - Detection of SR-BI in rat H4IIE total cell lysates and plasma membrane proteins. Photo courtesy of product review by verified customer.

Immunohistochemistry: SR-BI Antibody [NB400-104] - Immunolocalization of SR-BI in adult mink testis using NB400-104. SR-BI labeling is visible at the surface and along the outline of the large vacuole. Photo courtesy of R.M. Pelletier, University of Montreal.

Immunohistochemistry-Paraffin: SR-BI Antibody [NB400-104] - FFPE tissue section of mouse liver using SR-BI antibody (Lot 8310) at 1:300 dilution with HRP-DAB detection and hematoxylin counterstaining. The antibody generated a specific membrane signal of SR-BI protein in the murine hepatocytes.

<b>Genetic Strategies Validation. </b>Knockdown Validated: SR-BI Antibody [NB400-104] - HCV replication was increased by CD36. Silence of CD36 decreased HCV infection and replication (n = 3). Huh7.5 cells were transfected with 0.2 u g CD36-HA plasmid or with 150 pmol siRNA for CD36 (B) for 48 hrs, and then were washed and infected with HCV (150 IU/cell) for 2 hrs, followed by washing and continuously incubating. Intracellular HCV RNA and proteins were detected in 96 hrs, and the cytotoxicity of siRNAs was measured in 96-wells plate with a MTT assay in B. Image collected and cropped by CiteAb from the following publication (//www.nature.com/articles/srep21808) licensed under a CC-BY license.

Immunohistochemistry-Paraffin: SR-BI Antibody [NB400-104] - Staining of human adrenal cortex.

Immunocytochemistry/Immunofluorescence: SR-BI Antibody [NB400-104] - HeLa cells were fixed and permeabilized for 10 minutes using -20C MeOH. The cells were incubated with anti-SR-BI at 2 ug/ml overnight at 4C and detected with an anti-rabbit Dylight 488 (Green) at a 1:500 dilution. Alpha tubulin (DM1A) NB100-690 was used as a co-stain at a 1:1000 dilution and detected with an anti-mouse Dylight 550 (Red) at a 1:500 dilution. Nuclei were counterstained with DAPI (Blue). Cells were imaged using a 40X objective.

Immunohistochemistry-Paraffin: SR-BI Antibody [NB400-104] - FFPE tissue section of mouse liver using SR-BI antibody (Lot R-4) at 1:300 dilution with HRP-DAB detection and hematoxylin counterstaining. The antibody generated mainly a membranous signal of SR-BI protein in the murine hepatocytes.

Flow Cytometry: SR-BI Antibody [NB400-104] - Analysis of Huh7 and HepG2 cells using SR-B1 antibody NB400-104. Courtesy of Bruno Sainz, Jr., PhD, University of Illinois at Chicago.

Western Blot: SR-BI Antibody - BSA Free [NB400-104] - Effects of 13-HODE & LA in the presence & absence of PPAR alpha & PPAR gamma selective antagonists on molecular markers of cholesterol homeostasis in RAW264.7 macrophages. RAW264.7 cells were pre-treated without or with the PPAR alpha selective antagonist GW6471 or the PPAR gamma selective antagonist GW9662 & subsequently treated without (vehicle control) or with 2.5 μmol/L 13-HODE or 100 μmol/L LA for 24 h. Afterwards, cells were lysed & subsequently processed for western blotting as described in the materials & methods section. A, Representative immunoblots specific for ABCA1, ABCG1, SR-BI, LXR alpha , & beta -actin which was used for normalization are shown. B, Bars represent data from densitometric analysis & are means ± SD from three independent experiments (n = 3). Data are expressed as percentage of protein concentration of vehicle control cells. Results from statistical analysis are indicated: Significant effects are denoted with superscript letters. Bars marked without a common superscript letter significantly differ (P 2000) (g, h, i, respectively). Bar graph shows the mean percentage of positively stained cells. Error bars depict standard deviations. ****p 0.3) by one-way ANOVA. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/29523748), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: SR-BI Antibody - BSA Free [NB400-104] - Differentiation & characteristics of iHLCs. (a) Cell morphology & culture conditions at different stages of differentiation from iPSCs into iHLCs. Bright-field images were taken at the indicated time points (scale bar 100 µm). (b) Sequential expression & repression of transcription factors marking successful differentiation. Cells were immunostained with antibodies against Oct 3/4 (pluripotency marker), the endodermal transcription factor GATA-4, & the hepatic marker HNF4 alpha at day 0, 5, & 10 of differentiation (scale bars 20 µm). Shown are representative fluorescence & DIC images. (c) mRNA expression levels of different hepatocyte-specific factors in iHLCs, Huh7.5 cells, & primary human hepatocytes (PHHs) were analysed via qRT-PCR. Expression levels are displayed as fold over iPSCs normalised to GAPDH & 18S rRNA (mean ± SEM, n = 3–4, *p 0.9) by one-way ANOVA. §P < 0.02 by unpaired Student's t-test, relative to 0 h time point. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/29523748), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Reactivity:

Hu, Mu, Rt, Po, ChHa, Ha, Md, Pm, Rb, SyHa

Species Glossary

Reactivity: Hu, Mu, Rt, Po, ChHa, Ha, Md, Pm, Rb, SyHa

Applications:

, , , , , , , , ,

Applications: , , , , , , , , ,

Host:

Rabbit Polyclonal

Host: Rabbit Polyclonal

Sizes:

Sample Size Available

Sizes: Sample Size Available

Conjugate:

Unconjugated

Available Conjugates:

Validated by:

Validated by:

Conjugate	Catalog #	Availability	Size	Price
Alexa Fluor 350	NB400-104AF350
Alexa Fluor 405	NB400-104AF405
Alexa Fluor 488	NB400-104AF488
Alexa Fluor 532	NB400-104AF532
Alexa Fluor 594	NB400-104AF594
Alexa Fluor 647	NB400-104AF647
Alexa Fluor 700	NB400-104AF700
Alexa Fluor 750	NB400-104AF750
Allophycocyanin	NB400-104APC
Biotin	NB400-104B
CoraFluor 1	NB400-104CL1
DyLight 350	NB400-104UV
DyLight 405	NB400-104V
DyLight 488	NB400-104G
DyLight 550	NB400-104R
DyLight 594	NB400-104DL594
DyLight 650	NB400-104C
DyLight 680	NB400-104FR
DyLight 755	NB400-104IR
FITC	NB400-104F
HRP	NB400-104H
Janelia Fluor 525	NB400-104JF525
Janelia Fluor 549	NB400-104JF549
Janelia Fluor 646	NB400-104JF646
Janelia Fluor 669	NB400-104JF669
PE	NB400-104PE
PerCP	NB400-104PCP
mFluor Violet 450 SE	NB400-104MFV450
mFluor Violet 500 SE	NB400-104MFV500
mFluor Violet 610 SE	NB400-104MFV610

Available Formulations

Formulation	Catalog #	Availability	Price
BSA Free	NB400-104SS

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NB400-132

ABCG1 Antibody - BSA Free

(2 Reviews)

(182 Publications)

0.1 ml

NB400-132

Flow (Intracellular): ABCG1 Antibody - BSA Free [NB400-132] - RAW 246.7 cells were either untreated (A) or serum starved for 24 hours, and then treated with 1uM TO9 for 24 hours (B). An intracellular stain was performed with NB400-132 (blue) and a matched isotype control NB810-56910 (orange). Cells were fixed with 4% paraformaldehyde, following fixation, cells were permeabilized with 0.1% saponin. Cells were incubated in an antibody dilution of 5 ug/mL for 30 minutes at room temperature, followed by Goat Anti-Rabbit Dylight 550-conjugated antibody.

<b>Biological Strategies Validation. </b>Western Blot: ABCG1 Antibody - BSA Free [NB400-132] - Cells were pretreated with 5 uM F12511 or 5 uM MG132 for 30 min and then exposed to 5 or 50 uM 24S-OHC for 6 h. Whole-cell lysates were immunoblotted with antibodies specific for ABCG1 or beta-actin. Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31285856/) licensed under a CC-BY license.

Western Blot: ABCG1 Antibody - BSA Free [NB400-132] - Detection of ABCG1 in J774 mouse macrophages. Image provided by Dr. Angeliki Chroni of the National Centre for Scientific Research Demokritos.

Western Blot: ABCG1 Antibody - BSA Free [NB400-132] - Raw 264.7 (A), and Raw 264.7 + 10uM T09 18 hr (B) cell lysate using ABCG1 antibody at 2 ug/mL.

Western Blot: ABCG1 Antibody - BSA Free [NB400-132] - Detection of ABCG1 in mouse peritoneal macrophages. Lane 1: untreated mouse peritoneal macrophages, Lane 2: 22-(R)-hydrocholesterol treated macrophages, Lane 3: T0901713 treated macrophages, Lane 4: T091713 treated macrophages.

Western Blot: ABCG1 Antibody - BSA Free [NB400-132] - SAA has little impact on the impairment in biliary and fecal excretion of macrophage-derived 3H-cholesterol during endotoxemia. WT and SAAKO mice were injected subcutaneously with PBS or 0.8 ug/g LPS as indicated, followed 4 hr later by intraperitoneal injection of 3H-cholesterol-labeled J774 macrophages. ABCG1 in liver lysates (40 ug protein) was identified by immunoblotting and quantified by densitometry. Results from each of the 3 experiments (n = 4-5 per group per experiment) were expressed relative to PBS-injected WT mice after normalization to beta-actin. A representative western blot is shown. Image collected and cropped by CiteAb from the following publication (//www.hindawi.com/journals/jl/2013/283486/), licensed under a CC-BY license.

miR-33 deficiency improved cholesterol efflux in macrophages. A, Quantitative real-time PCR analysis of Abca1 & Abcg1 in macrophages from miR-33+/+Apoe−/− & miR-33−/−Apoe−/− mice. Values from miR-33+/+Apoe−/− were set at 100%. Values are mean±SE (n=7 each); ***P<0.001. B, Western blotting analysis of ABCA1 & ABCG1 in thioglycollate-elicited peritoneal macrophages from miR-33+/+Apoe−/− & miR-33−/−Apoe−/− mice. GAPDH was used as a loading control. C, Cholesterol efflux from thioglycollate-elicited peritoneal macrophages in the presence or absence of apoA-I (5 or 10 μg/mL). Values are mean±SE (n=6 each); **P<0.01. D, Cholesterol efflux from thioglycollate-elicited peritoneal macrophages in the presence or absence of HDL-C (50 or 100 μg/mL). Values are mean±SE (n=6 each); **P<0.01. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/23316322), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

6‐Dihydroparadol increases A) ABCA1 & B) ABCG1, but not C) SR‐BI protein levels in cholesterol‐loaded THP‐1‐derived macrophages. THP‐1 cells were differentiated as described in Figure 2, & then loaded with unlabeled cholesterol for 24 h. Cells were treated with increasing concentrations of 6‐dihydroparadol (1–30 μm) for another 24 h. The protein levels of ABCA1, ABCG1, & SR‐B1 were detected by Western blot analysis. The control was treated with solvent vehicle (0.1% DMSO). As a positive control, TO901317 (5 μm, 24 h) was used. The bar graphs represent mean ± SD from three independent experiments. *p < 0.05, **p < 0.01, & ***p < 0.001 versus control (determined by Student's t‐test or ANOVA with Bonferroni's post hoc test). Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/29802792), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

(A) Chemical structure, (B) cytotoxicity of alpha -asarone, (C) enhancement of cholesterol efflux by alpha -asarone, (D & E) upregulation of ABCA1 & ABCG1 by alpha -asarone & beta -asarone, & (F) elevation of retinoid X receptor (RXR) alpha transcription. J774A.1 murine macrophages were exposed to 50 μg/ml oxidized low-density lipoprotein (LDL) & treated with 1–10 μM purple Perilla frutescens extracts (PPE)-alpha -asarone & 5–10 μM beta -asarone. (B) MTT assay was performed for the measurement of alpha -asarone toxicity. Graph data represent 1 of 4 independent experiments with multiple estimations. Values are expressed as the percentage cell survival relative to the untreated control cells (cell viability, 100%). (C) Cholesterol efflux was expressed as the percentage fluorescence in the medium relative to total fluorescence. (D & E) For the measurement of ABCA1 & ABCG1 expression, total cell lysates were subjected to western blot analysis with a primary antibody against ABCG1 or ABCG1. beta -actin was used as an internal control. Bar graphs (means ± SEM, n=3) represent quantitative densitometric results of the upper bands. Bar graphs denoted without a common letter indicate significant difference, P<0.05. (F) RXR alpha mRNA expression was measured by RT-PCR. GAPDH was used as a housekeeping gene for the co-amplification with RXR alpha . Image collected & cropped by CiteAb from the following publication (//www.spandidos-publications.com/10.3892/ijmm.2015.2101), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

6‐Dihydroparadol increases A) ABCA1 & B) ABCG1 protein stability. THP‐1 cells were differentiated as described in Figure 2. Then cells were loaded with unlabeled cholesterol & treated with 6‐dihydroparadol (10 μm), or solvent vehicle (0.1% DMSO, control) for 24 h. Cells were lysed at different time points (0, 1, 2, 3, 4, & 6 h) after treatment with the protein synthesis inhibitor cycloheximide (CHX, 100 μm). The protein levels of both ABCA1 & ABCG1 were detected by Western blot analysis. The data points represent mean ± SD from three independent experiments. *p < 0.05 & **p < 0.01 versus control at the same time point (determined by Student's t‐test). Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/29802792), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

(A) Upregulation of ABCA1 & ABCG1 & (B) enhancement of cholesterol efflux by purple Perilla frutescens extracts (PPE) in 50 μg/ml Cu2+-oxidized low-density lipoproteins (LDL)-exposed J774A.1 murine macrophages. (A) For the measurement of ABCA1 & ABCG1 expression, total cell lysates were subjected to western blot analysis with a primary antibody against ABCA1 or ABCG1. beta -actin was used as an internal control. Bar graphs (means ± SEM, n=3) represent quantitative densitometric results of the upper bands. (B) Cholesterol efflux was expressed as the percentage of fluorescence in the medium relative to the total fluorescence. Bar graphs denoted without a common letter indicate significant difference, P<0.05. Image collected & cropped by CiteAb from the following publication (//www.spandidos-publications.com/10.3892/ijmm.2015.2101), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: ABCG1 Antibody - BSA Free [NB400-132] - 6‐Dihydroparadol increases A) ABCA1 & B) ABCG1 protein stability. THP‐1 cells were differentiated as described in Figure 2. Then cells were loaded with unlabeled cholesterol & treated with 6‐dihydroparadol (10 μm), or solvent vehicle (0.1% DMSO, control) for 24 h. Cells were lysed at different time points (0, 1, 2, 3, 4, & 6 h) after treatment with the protein synthesis inhibitor cycloheximide (CHX, 100 μm). The protein levels of both ABCA1 & ABCG1 were detected by Western blot analysis. The data points represent mean ± SD from three independent experiments. *p < 0.05 & **p < 0.01 versus control at the same time point (determined by Student's t‐test). Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/29802792), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: ABCG1 Antibody - BSA Free [NB400-132] - Evodiamine enhances apo A1-mediated ChE from THP-1 macrophages & increases ABCA1 protein level. (a) Differentiated THP-1 cells were loaded with [3H]-cholesterol together with the indicated treatments for 24 h. On the next day, the cells were washed twice with PBS & incubated with the same compounds [solvent vehicle control (Veh; ≤0.1% DMSO), evodiamine (1–20 μM), & the PPAR gamma agonist pioglitazone (10 μM) as positive control] with or without 10 µg/mL apo A1. Extracellular as well as intracellular radioactivities were quantified with scintillation counter. Differentiated THP-1-derived macrophages were treated with solvent vehicle control (Veh; ≤0.1% DMSO), evodiamine (10 μM), & the PPAR gamma agonist pioglitazone (10 μM) as positive control. After 24 h incubation, the cells were lysed & 20 μg protein was resolved via SDS-PAGE. Immunodetection was performed with antibodies against the indicated proteins, ABCA1 (b), ABCG1 (c), & SR-B1 (d), & visualized by chemiluminescence detection. All experiments were performed at least three times & data are presented as means ± S.D. vs. solvent vehicle control, *p < 0.05, **p < 0.01, ***p < 0.001, n.s. no significance (ANOVA/Bonferroni). Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/30038271), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Reactivity:

Hu, Mu, Rt, ChHa, Ha, Pm, Rb

Species Glossary

Reactivity: Hu, Mu, Rt, ChHa, Ha, Pm, Rb

Applications:

, , , , , ,

Applications: , , , , , ,

Host:

Rabbit Polyclonal

Host: Rabbit Polyclonal

Sizes:

Sample Size Available

Sizes: Sample Size Available

Conjugate:

Unconjugated

Available Conjugates:

Validated by:

Validated by:

Conjugate	Catalog #	Availability	Size	Price
Alexa Fluor 350	NB400-132AF350
Alexa Fluor 405	NB400-132AF405
Alexa Fluor 488	NB400-132AF488
Alexa Fluor 532	NB400-132AF532
Alexa Fluor 594	NB400-132AF594
Alexa Fluor 647	NB400-132AF647
Alexa Fluor 700	NB400-132AF700
Alexa Fluor 750	NB400-132AF750
Allophycocyanin	NB400-132APC
Allophycocyanin/Cy7	NB400-132APCCY7
Biotin	NB400-132B
CoraFluor 1	NB400-132CL1
DyLight 350	NB400-132UV
DyLight 405	NB400-132V
DyLight 488	NB400-132G
DyLight 550	NB400-132R
DyLight 594	NB400-132DL594
DyLight 650	NB400-132C
DyLight 680	NB400-132FR
DyLight 755	NB400-132IR
FITC	NB400-132F
HRP	NB400-132H
Janelia Fluor 525	NB400-132JF525
Janelia Fluor 549	NB400-132JF549
Janelia Fluor 646	NB400-132JF646
Janelia Fluor 669	NB400-132JF669
PE	NB400-132PE
PE/Atto594	NB400-132PEATT594
PE/Cy5.5	NB400-132PECY55
PE/Cy7	NB400-132PECY7
PerCP	NB400-132PCP
mFluor Violet 450 SE	NB400-132MFV450
mFluor Violet 500 SE	NB400-132MFV500
mFluor Violet 610 SE	NB400-132MFV610

Available Formulations

Formulation	Catalog #	Availability	Price
BSA Free	NB400-132SS

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NB400-101

SR-BI Antibody - BSA Free

(1 Review)

(111 Publications)

0.1 ml

NB400-101

<b>Genetic Strategies Validation. </b>Knockout Validated: SR-BI Antibody [NB400-101] - Immunofluorescent analysis of SR-BI localization in liver of normal, Tie2-Scarb1 x Scarb1-KO, and Scarb1-KO mice. Liver sections from normal (b) and Tie2-Scarb1 x Scarb1-KO mice (c) were stained for SR-BI (red) and cytokeratin 8-18 (green).Merge image for normal mouse (b) demonstrates strong presence of SR-BI in hepatocytes (b, yellow signal) and absence of detectable level of SR-BI protein in liver of Tie2-Scarb1 x Scarb1-KO mice (c). In Scarb1-KO mice there was no detectable level of SR-BI protein (d, staining for SR-BI). Blue = DAPI. Image collected and cropped by CiteAb from the following publication (//www.hindawi.com/journals/bmri/2015/607120/) licensed under a CC-BY license.

Western Blot: SR-BI Antibody [NB400-101] - Detection of SR-BI in mouse liver lysate (20 ug) using NB 400-101. ECL detection 5 seconds.

Flow (Intracellular): SR-BI Antibody [NB400-101] - An intracellular stain was performed on HeLa cells with NB400-101AF647 (blue) and a matched isotype control (orange). Cells were fixed with 4% PFA and then permeablized with 0.1% saponin. Cells were incubated in an antibody dilution of 2.5 ug/mL for 30 minutes at room temperature. Both antibodies were conjugated to Alexa Fluor 647.

$<b>Genetic Strategies Validation. </b>Knockout Validated: SR-BI Antibody [NB400-101] - Western blot and Coomassie stain of membrane fractions isolated from livers of normal C57Bl/6N (lane 1), Scarb1-KO (lane 2), and LIV11-SCARB1 x Scarb1-KO (lane 3) mice. 20 ug of membrane protein was loaded into each lane. (a)Western blot (anti-SR-BI antibody). (b) Coomassie stain (loading control for Western blot) encompassing the same MW region as SR-BI. Aliquots from the same tube were loaded for the Western blot and for the Coomassie-stained gel, which shows comparable loading between the three samples. Image collected and cropped by CiteAb from the following publication (//www.hindawi.com/journals/bmri/2015/607120/) licensed under a CC-BY license.$

Western Blot: SR-BI Antibody [NB400-101] - Western blot analysis of ABCA1 and SR-B1 proteins from WT and Osbpl8KO mouse liver. The blots were probed with anti-beta-actin as a loading control. Densitometric quantification of the Western blot data is shown on the right. The results were normalized against beta-actin. The data represents mean +/- s.e.m. (n = 4). Image collected and cropped by CiteAb from the following publication (//dx.plos.org/10.1371/journal.pone.0058856), licensed under a CC-BY license.

Immunocytochemistry/Immunofluorescence: SR-BI Antibody [NB400-101] - HeLa cells were fixed and permeabilized for 10 minutes using -20C MeOH. The cells were incubated with anti-SR-BI at 2 ug/ml overnight at 4C and detected with an anti-rabbit DyLight 488 (Green) at a 1:500 dilution. Alpha tubulin (DM1A) NB100-690 was used as a co-stain at a 1:1000 dilution and detected with an anti-mouse DyLight 550 (Red) at a 1:500 dilution. Nuclei were counterstained with DAPI (Blue). Cells were imaged using a 40X objective.

Immunocytochemistry/ Immunofluorescence: SR-BI Antibody - BSA Free [NB400-101] - SR-BI distribution in polarized EC SVEC4-10 cells. SR-BI localization is presented in (a) as x-y image & orthogonal (x-z & y-z) views. (b) & (c) represent rendering of SR-BI staining (red) throughout the cells. Nuclei: blue. In (b) & (c) basolateral surface is on the top & the bottom, respectively. These results demonstrate the presence of SR-BI on both the apical & the basolateral sides of EC. The size of scale bar on (a) is 5 μm & on (b) & (c) 10 μm. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/26504816), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Immunocytochemistry/ Immunofluorescence: SR-BI Antibody - BSA Free [NB400-101] - Immunofluorescent analysis of SR-BI localization in aorta of Tie2-Scarb1 × Scarb1-KO & Scarb1-KO mice. Mouse aorta sections were stained for SR-BI (a & d, red) & CD31 (b & e, green). Colocalization of SR-BI & CD31 was presented on (c) & (f). Blue = DAPI. (a, b, & c) Immunohistological analysis of SR-BI localization in aortic sections of Tie2-Scarb1 × Scarb1-KO mice. Colocalization of SR-BI & CD31 was found in aortic endothelial cells. In several EC stained for SR-B1 red color was present on both apical & basolateral sides (a). (d, e, & f) Immunohistological analysis of SR-BI localization in aortic sections of Scarb1-KO mice. There is no red signal in aorta from Scarb1-KO mice. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/26504816), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Immunocytochemistry/ Immunofluorescence: SR-BI Antibody - BSA Free [NB400-101] - Immunofluorescent analysis of SR-BI localization in liver of normal, Tie2-Scarb1 × Scarb1-KO, & Scarb1-KO mice. Liver sections from normal (a, b) & Tie2-Scarb1 × Scarb1-KO mice (c) were stained for SR-BI (red) & cytokeratin 8–18 (green). Merge image for normal mouse (b) demonstrates strong presence of SR-BI in hepatocytes (b, yellow signal) & absence of detectable level of SR-BI protein in liver of Tie2-Scarb1 × Scarb1-KO mice (c). In Scarb1-KO mice there was no detectable level of SR-BI protein (d, staining for SR-BI). Blue = DAPI. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/26504816), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

$Western Blot: SR-BI Antibody - BSA Free [NB400-101] - Western blot & Coomassie stain of membrane fractions isolated from livers of normal C57Bl/6N (lane 1), Scarb1-KO (lane 2), & LIV11-SCARB1 × Scarb1-KO (lane 3) mice. 20 μg of membrane protein was loaded into each lane. (a) Western blot (anti-SR-BI antibody). (b) Coomassie stain (loading control for Western blot) encompassing the same MW region as SR-BI. Aliquots from the same tube were loaded for the Western blot & for the Coomassie-stained gel, which shows comparable loading between the three samples. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/26504816), licensed under a CC-BY license. Not internally tested by Novus Biologicals.$

Western Blot: SR-BI Antibody - BSA Free [NB400-101] - Liver mRNA & protein expression analysis of chow-fed Osbpl8KO mice.A: qPCR analysis of the quantity of the mRNAs identified at the bottom in chow-fed KO females (open bars) & males (closed bars). The mRNAs were quantified using ribosomal protein 36B4 message as a housekeeping reference. The data are expressed relative to quantity in littermate WT animals of the same gender, & represent mean ± s.e.m. (n = 6; *p<0.05, **p<0.01, T-test). B: Western blot analysis of ABCA1 & SR-B1 proteins in WT & KO mouse liver. The blots were probed with anti-beta -actin as a loading control. Densitometric quantification of the Western blot data is shown on the right. The results were normalized against beta -actin. The data represents mean ± s.e.m. (n = 4). Image collected & cropped by CiteAb from the following publication (//dx.plos.org/10.1371/journal.pone.0058856), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

$Western Blot: SR-BI Antibody - BSA Free [NB400-101] - Western blot & Coomassie stain of membrane fractions isolated from livers of normal C57Bl/6N (lane 1), Scarb1-KO (lane 2), & LIV11-SCARB1 × Scarb1-KO (lane 3) mice. 20 μg of membrane protein was loaded into each lane. (a) Western blot (anti-SR-BI antibody). (b) Coomassie stain (loading control for Western blot) encompassing the same MW region as SR-BI. Aliquots from the same tube were loaded for the Western blot & for the Coomassie-stained gel, which shows comparable loading between the three samples. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/26504816), licensed under a CC-BY license. Not internally tested by Novus Biologicals.$

Reactivity:

Hu, Mu, Rt, Bv, ChHa, Md, Pm, Sj

Species Glossary

Reactivity: Hu, Mu, Rt, Bv, ChHa, Md, Pm, Sj

Applications:

, , , , , , , ,

Applications: , , , , , , , ,

Host:

Rabbit Polyclonal

Host: Rabbit Polyclonal

Sizes:

Sample Size Available

Sizes: Sample Size Available

Conjugate:

Unconjugated

Available Conjugates:

Validated by:

Validated by:

Conjugate	Catalog #	Availability	Size	Price
Alexa Fluor 350	NB400-101AF350
Alexa Fluor 405	NB400-101AF405
Alexa Fluor 488	NB400-101AF488
Alexa Fluor 532	NB400-101AF532
Alexa Fluor 594	NB400-101AF594
Alexa Fluor 647	NB400-101AF647
Alexa Fluor 700	NB400-101AF700
Alexa Fluor 750	NB400-101AF750
Allophycocyanin	NB400-101APC
Biotin	NB400-101B
CoraFluor 1	NB400-101CL1
DyLight 350	NB400-101UV
DyLight 405	NB400-101V
DyLight 488	NB400-101G
DyLight 550	NB400-101R
DyLight 594	NB400-101DL594
DyLight 650	NB400-101C
DyLight 680	NB400-101FR
DyLight 755	NB400-101IR
FITC	NB400-101F
HRP	NB400-101H
Janelia Fluor 525	NB400-101JF525
Janelia Fluor 549	NB400-101JF549
Janelia Fluor 646	NB400-101JF646
Janelia Fluor 669	NB400-101JF669
PE	NB400-101PE
PerCP	NB400-101PCP
mFluor Violet 450 SE	NB400-101MFV450
mFluor Violet 500 SE	NB400-101MFV500
mFluor Violet 610 SE	NB400-101MFV610

Available Formulations

Formulation	Catalog #	Availability	Price
BSA Free	NB400-101SS

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NB100-2288

BMAL1 Antibody

(1 Review)

(71 Publications)

0.1 ml

NB100-2288

<b>Biological Strategies Validation. </b>Immunohistochemistry: BMAL1 Antibody [NB100-2288] - Inhibition of mTOR signaling with Rapamycin rescues PTEN-driven accumulation of BMAL1A. Tissue samples and graphic show BMAL1 in K14cre PtenF/F mice and control (arrows). Note a significant amount of BMAL1 expression in PTEN mutant mice. K14cre PtenF/F mice and control littermates received Rapamycin or vehicle every other day for 15 days. Rapamycin treatment reduces the expression of nuclear BMAL1 in K14cre PtenF/F mice (arrowhead) (*** p0.05). Scale bars -30um. Image collected and cropped by CiteAb from the following publication (//www.ncbi.nlm.nih.gov/pmc/articles/PMC5173143/) licensed under a CC-BY license.

Western Blot: BMAL1 Antibody [NB100-2288] - Oxidation causes accumulation of BMAL1. Western blot assay demonstrates time-dependent accumulation of BMAL1 upon oxidative stress in HNSCC cells (*p0.05). Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/27285754), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: BMAL1 Antibody [NB100-2288] - Small interference RNA targeting Raptor & Rictor disrupts BMAL1 accumulation in HNSCCTargeted disruption of Raptor (A-B) & Rictor (C-D) using siRNA results in a dose-dependent downregulation of BMAL1 in HNSCC cells. E. Disruption of PTEN by protein oxidation causes activation of mTOR signaling, resulting in accumulation of BMAL1. Notably, inhibition of mTOR signaling, particularly mTORC1 & mTORC2, results in restoration of normal BMAL1 levels in the epidermis of mice & head & neck cancer cells. These results demonstrate a novel role for mTOR in regulating nuclear levels of the core clock gene BMAL1. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/27285754), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: BMAL1 Antibody [NB100-2288] - Targeted disruption of PTEN in vitro & in vivo induces activation of pS6 & BMAL1A. & B. Targeted inhibition of PTEN using siRNA results in concentration-dependent inhibition of PTEN protein in HNSCC cells. HNSCC cells show accumulation of BMAL1 & pS6 in response to PTEN inhibition. C. Immunofluorescence assay to detect BMAL1 in PTEN conditional knockout mice (K14cre PtenF/F) & control littermates. Immunofluorescences & graphic show high accumulation of nuclear BMAL1 in K14cre PtenF/F mice compared to control mice (K14cre). Scale bars represent 50 μm. Black & white images depict cells positive for BMAL1 in K14cre PtenF/F mice (arrows) compared to few BMAL-positive cells in control mice (arrowhead). Scale bars represent 10 μm. (**p<0.01). Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/27285754), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: BMAL1 Antibody [NB100-2288] - Oxidation causes accumulation of BMAL1A. Head & neck cancer cells have different expression levels of the core clock protein BMAL1. B. Immunofluorescence assay depicts accumulation of ROS (green channel) & BMAL1 (red channel) upon oxidation. C. & D. Western blot assay demonstrates time-dependent accumulation of BMAL1 upon oxidative stress in HNSCC cells (*p<0.05, **p<0.01). Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/27285754), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Immunocytochemistry/ Immunofluorescence: BMAL1 Antibody [NB100-2288] - Targeted disruption of PTEN in vitro & in vivo induces activation of pS6 & BMAL1A. & B. Targeted inhibition of PTEN using siRNA results in concentration-dependent inhibition of PTEN protein in HNSCC cells. HNSCC cells show accumulation of BMAL1 & pS6 in response to PTEN inhibition. C. Immunofluorescence assay to detect BMAL1 in PTEN conditional knockout mice (K14cre PtenF/F) & control littermates. Immunofluorescences & graphic show high accumulation of nuclear BMAL1 in K14cre PtenF/F mice compared to control mice (K14cre). Scale bars represent 50 μm. Black & white images depict cells positive for BMAL1 in K14cre PtenF/F mice (arrows) compared to few BMAL-positive cells in control mice (arrowhead). Scale bars represent 10 μm. (**p<0.01). Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/27285754), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Immunohistochemistry: BMAL1 Antibody [NB100-2288] - Astrocyte Bmal1 regulates genes with conflicting effects on A beta deposition. (A) Topro, GFAP, & BMAL1 staining in CA1 hippocampus of 4-month-old BMAL1 aKO; APP/PS1-21 mice & Cre- controls (scale bar = 100 µm). Arrows indicate astrocyte nuclei quantified as indicated by Topro nuclei surrounded by GFAP positivity. Blue circles indicate nuclei quantified as BMAL1 negative. Quantification of astrocytes counted as BMAL1- or BMAL1+ is shown on the right. n = 5 mice per group, **** = p < 0.0001 by two-way ANOVA with Sidak multiple comparisons test. (B) Heatmap of Fluidigm qPCR analysis of 20 genes involved in the circadian clock, glial activation, & Alzheimer’s Disease in cortex from Aldh1l1-CreERT2; Bmal1fl/fl mice & Cre- controls with or without APP/PS1-21 or APPNL-G-F/wt (n = 6–8 mice per group). Two-way ANOVA analysis: c = significant main effect of Cre genotype, m = main effect of A beta model, c*m = interaction effect of cre & A beta model, - = no significance (all p < 0.05). (C) Individually plotted genes from A. * = p < 0.05, ** = p < 0.005, *** = p < 0.0005 by two-way ANOVA with Sidak multiple comparisons test. Panel B was made using GraphPad Prism version 9.2 (//www.graphpad.com). Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/35110643), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Reactivity:

Hu, Mu, Rt, Am, Pm

Species Glossary

Reactivity: Hu, Mu, Rt, Am, Pm

Applications:

, , , , ,

Applications: , , , , ,

Host:

Rabbit Polyclonal

Host: Rabbit Polyclonal

Sizes:

Sample Size Available

Sizes: Sample Size Available

Conjugate:

Unconjugated

Available Conjugates:

Validated by:

Validated by:

Conjugate	Catalog #	Availability	Size	Price
Alexa Fluor 350	NB100-2288AF350
Alexa Fluor 405	NB100-2288AF405
Alexa Fluor 488	NB100-2288AF488
Alexa Fluor 532	NB100-2288AF532
Alexa Fluor 594	NB100-2288AF594
Alexa Fluor 647	NB100-2288AF647
Alexa Fluor 700	NB100-2288AF700
Alexa Fluor 750	NB100-2288AF750
Allophycocyanin	NB100-2288APC
Biotin	NB100-2288B
CoraFluor 1	NB100-2288CL1
DyLight 350	NB100-2288UV
DyLight 405	NB100-2288V
DyLight 488	NB100-2288G
DyLight 550	NB100-2288R
DyLight 594	NB100-2288DL594
DyLight 650	NB100-2288C
DyLight 680	NB100-2288FR
DyLight 755	NB100-2288IR
FITC	NB100-2288F
HRP	NB100-2288H
Janelia Fluor 525	NB100-2288JF525
Janelia Fluor 549	NB100-2288JF549
Janelia Fluor 646	NB100-2288JF646
Janelia Fluor 669	NB100-2288JF669
PE	NB100-2288PE
PerCP	NB100-2288PCP
mFluor Violet 450 SE	NB100-2288MFV450
mFluor Violet 500 SE	NB100-2288MFV500
mFluor Violet 610 SE	NB100-2288MFV610

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NB600-582

SREBP1 Antibody (2A4) - BSA Free

(66 Publications)

0.1 ml

NB600-582

Simple Western: SREBP1 Antibody (2A4) [NB600-582] - Lane view shows a specific band for SREBP1 in 1.0 mg/ml of HeLa lysate. This experiment was performed under reducing conditions using the 12-230 kDa separation system.

<b>Genetic Strategies Validation. </b>Knockout Validated: SREBP1 Antibody (2A4) [NB600-582] - KO and OE of SREBP1 influenced lipid metabolism in Bel-7402 cells. The protein level of lipid-associated genes in SREBP1-KO, SREBP1-OE, and WT Bel-7402 cells. Data were expressed as mean -/+ standard error of the mean. *P < 0.05, **P < 0.01, and ***P < 0.001 vs. WT group, respectively.

Western Blot: SREBP1 Antibody (2A4) - BSA Free [NB600-582] - Effect of GEN on the expression of Nrf2‐related signalling proteins in OA (660 μmol/L) & PA (330 μmol/L)‐induced HepG2 cells. GEN was added into HepG2 cells prior 1 h to stimulation of OA & PA for 18 h. A‐C, Protein expression of Nrf2, PPAR alpha , PPAR gamma in nucleus & HO‐1 in cytoplasm was detected by Western blot. (D & E) Protein expression of P‐ACC, ACC, P‐AKT, AKT, P‐AMPK alpha , AMPK alpha , P‐AMPK beta & AMPK beta was detected by Western blot. F‐H, Protein expression of PI3K, P‐mTORC, mTORC, P‐S6K, S6K, P‐S6, S6, SREBP‐1c & HMGB1 was detected by Western blot. The similar results were collected from three dependent experiments. All data were expressed by mean ± SEM (n = 5 in each group). ##P < .01 vs Control Group; *P < .05 & **P < .01 vs OA & PA Group Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/32293113), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: SREBP1 Antibody (2A4) - BSA Free [NB600-582] - KO & OE of SREBP1 influenced lipid metabolism in Bel-7402 cells. (A) Total cellular TG content of SREBP1-KO, SREBP1-OE, & WT Bel-7402 cells. (B) HPLC-MS determination of the SFAs to MUFAs ratios (palmitic acid to palmitoleic acid, 16:0 to 16:1) (stearic acid to oleic acid, 18:0 to 18:1) as well as the content of 16:0, 16:1, 18:0, & 18:1 in SREBP1-KO, SREBP1-OE, & WT Bel-7402 cells. (C) The transcript level of lipid-associated genes in SREBP1-KO, SREBP1-OE, & WT Bel-7402 cells. (D & E) The protein level of lipid-associated genes in SREBP1-KO, SREBP1-OE, & WT Bel-7402 cells. Data were expressed as mean ± standard error of the mean. *P < 0.05, **P < 0.01, & ***P < 0.001 vs. WT group, respectively. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31297058), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: SREBP1 Antibody (2A4) - BSA Free [NB600-582] - Construction of knockout (KO) & overexpression (OE) cell lines. (A) The sequencing results of KO positive clone cells; (B) The messenger RNA (mRNA) level of SREBP1 in wild type (WT) & OE Bel-7402 cells. Data were expressed as mean ± standard error of the mean. ***P < 0.001 vs. WT group; (C & D) The protein level of SREBP1 in WT, OE, & KO Bel-7402 cells. Data were expressed as mean ± standard error of the mean. ***P < 0.001 vs. WT group. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31297058), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: SREBP1 Antibody (2A4) - BSA Free [NB600-582] - p75NTR stimulation activated SREBP1 & SREBP2 in Huh7 hepatocyte cells.Human Huh7 cells were stimulated with 10 ng/ml pro-NGF or 50 ng/ml NGF for 16 h followed by immunoblotting using antibodies to detect the presence of cleaved/activated SREBP1 & SREBP2. a SREBP1, immunoblots & b quantification. Values are mean ± SD, n = 3. **P < 0.01 & *p < 0.05 for treated vs. control cells. c, d SREBP2. Cells were treated with 10 ng/ml pro-NGF in the absence or presence of 0.5 μM PF429242 (PF), which is a selective inhibitor of the Site 1 protease (S1P). c Immunoblots & d quantification. PF decreased the amount of processed SREBP2 in these cells; however, addition of pro-NGF increased the relative level of cleaved SREBP2. Values are mean ± SD, n = 3. *p < 0.05 for treated vs. the corresponding control Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31296846), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: SREBP1 Antibody (2A4) - BSA Free [NB600-582] - Effect of GEN on the protein expression of Nrf2, ACC & mTORC signalling pathways in tyloxapol‐induced mice. GEN (50, 75, 100 mg/kg) was administered to WT or Nrf2−/− mice prior 1 h to stimulation of tyloxapol (500 mg/kg) for 18 h. A‐C, Protein expression of Nrf2, PPAR alpha , PPAR gamma in nucleus & HO‐1 in cytoplasm of WT mice was detected by Western blot. (D & E) Protein expression of Nrf2, PPAR alpha & PPAR gamma in Nrf2−/− mice was detected by Western blot. F‐H, Protein expression of P‐ACC, ACC, P‐AKT, AKT, P‐AMPK alpha , AMPK alpha , P‐AMPK beta , AMPK beta in WT & Nrf2−/− mice was detected by Western blot. I‐M, Protein expression of PI3K, P‐mTORC, mTORC, P‐S6K, S6K, P‐S6, S6, SREBP‐1c & HMGB1 WT & Nrf2−/− mice was detected by Western blot. The similar results were collected from three dependent experiments. All data were expressed by mean ± SEM (n = 5 in each group). ##P < .01 vs Control group; *P < .05 & **P < .01 vs Tyloxapol group Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/32293113), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Reactivity:

Hu, Mu, Rt, Ca, Ch, Ha, Pm, SyHa

Species Glossary

Reactivity: Hu, Mu, Rt, Ca, Ch, Ha, Pm, SyHa

Applications:

, , ,

Applications: , , ,

Host:

Mouse Monoclonal

Host: Mouse Monoclonal

Sizes:

Sample Size Available

Sizes: Sample Size Available

Conjugate:

Unconjugated

Available Conjugates:

Validated by:

Validated by:

Conjugate	Catalog #	Availability	Size	Price
Alexa Fluor 350	NB600-582AF350
Alexa Fluor 405	NB600-582AF405
Alexa Fluor 488	NB600-582AF488
Alexa Fluor 532	NB600-582AF532
Alexa Fluor 594	NB600-582AF594
Alexa Fluor 647	NB600-582AF647
Alexa Fluor 700	NB600-582AF700
Alexa Fluor 750	NB600-582AF750
Allophycocyanin	NB600-582APC
Biotin	NB600-582B
CoraFluor 1	NB600-582CL1
DyLight 350	NB600-582UV
DyLight 405	NB600-582V
DyLight 488	NB600-582G
DyLight 550	NB600-582R
DyLight 594	NB600-582DL594
DyLight 650	NB600-582C
DyLight 680	NB600-582FR
DyLight 755	NB600-582IR
HRP	NB600-582H
Janelia Fluor 525	NB600-582JF525
Janelia Fluor 549	NB600-582JF549
Janelia Fluor 646	NB600-582JF646
Janelia Fluor 669	NB600-582JF669
PE	NB600-582PE
PerCP	NB600-582PCP
mFluor Violet 450 SE	NB600-582MFV450
mFluor Violet 500 SE	NB600-582MFV500
mFluor Violet 610 SE	NB600-582MFV610

Available Formulations

Formulation	Catalog #	Availability	Price
BSA Free	NB600-582SS
Azide and BSA Free	NBP2-80959

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NB100-2215

SREBP1 Antibody - BSA Free

(3 Reviews)

(57 Publications)

0.1 ml

NB100-2215

Western Blot: SREBP1 Antibody [NB100-2215] - MiR-181a overexpression impairs and miR-181a inhibition improves glucose and lipid homeostasis in HepG2 cellsHepG2 cells were divided into 4 groups as follows: a control group, mimics group (HepG2 cells transfected with 10 nM mimics), NEFA group (treated with 1. 2 mM NEFA), and miR-181a + NEFA group (transfected with 50 nM miR-181a inhibitors and then treated with 1. 2 mM NEFA). It was followed with or without 100 nM insulin. Immunoblot analysis (left) and quantification (right) of SREBP-1c and PPARI+- in HepG2 cells. Image collected and cropped by Citeab from the following publication (Upregulation of miR-181a impairs hepatic glucose and lipid homeostasis. Oncotarget (2017)) licensed under a CC-BY license.

Immunocytochemistry/Immunofluorescence: SREBP1 Antibody [NB100-2215] - SREBP1 antibody was tested in HeLa cells with DyLight488 (green). Nuclei and alpha-tubulin were counterstained with DAPI (blue) and DyLight 550 (red). Nuclear and punctate vesicle staining was observed.

Immunohistochemistry-Paraffin: SREBP1 Antibody [NB100-2215] - nalysis of FFPE tissue section of mouse liver with SREBP1 antibody at 1:200. The antibody generated an expected cytoplasmic-nuclear immunostaining of SREBP1 protein in the hepatocytes.

Western Blot: SREBP1 Antibody [NB100-2215] - Detection of SREBP1. Lane 1: human liver. Lane 2: mouse liver.

Western Blot: SREBP1 Antibody - BSA Free [NB100-2215] - MiR-181a overexpression impairs & miR-181a inhibition improves glucose & lipid homeostasis in HepG2 cellsHepG2 cells were divided into 4 groups as follows: a control group, mimics group (HepG2 cells transfected with 10 nM mimics), NEFA group (treated with 1.2 mM NEFA), & miR-181a + NEFA group (transfected with 50 nM miR-181a inhibitors & then treated with 1.2 mM NEFA). B was followed with or without 100 nM insulin. (A) Immunoblot analysis (top) & quantification (bottom) of SIRT1, PGC-1 alpha & acetylated PGC-1 alpha in HepG2 cells. (B) Immunoblotting analysis (top) & quantification (bottom) of insulin-stimulated phosphorylation of AKT in HepG2 cells. (C) Glucose concentration in medium. (D) The glycogen content in HepG2 cells. (E) The mRNA expression levels of G6Pase & PEPCK. (F) Immunoblot analysis (left) & quantification (right) of SREBP-1c & PPAR alpha in HepG2 cells. (G) TG content in HepG2 cells. *P < 0.05, **P < 0.01. All experiments were repeated at least three times & representative results are shown. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/29207650), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: SREBP1 Antibody - BSA Free [NB100-2215] - Effect of restoration of macrophage A2bAR on liver.Liver was collected from WT, A2bAR KO, & CD68-Tg mice after 16 weeks of HFD as described in the methods. Relative mRNA expression was determined using the delta delta CT method with normalization to 18s rRNA. A. mRNA expression of TNF-alpha in liver. A2bAR KO (n = 5) vs WT (n = 7) p-value = 0.0271; A2bAR KO vs CD68-Tg (n = 6) p-value = 0.0210. B. mRNA expression of IL-6 in liver. A2bAR KO (n = 8) vs WT (n = 7) p-value = 0.0159; A2bAR KO vs CD68-Tg (n = 8) p-value = 0.0080. C. mRNA expression of IRS-2 in liver. CD68-Tg (n = 7) vs A2bAR KO (n = 8) p-value = 0.0300. D. Western blot analysis of liver; one representative (of 3 sets) WT, CD68-Tg & A2bAR KO group shown at 15 minutes post-insulin injection, following 16 weeks of HFD. Levels of mature SREBP-1 (68 kDa), & IRS-2 (185 kDa), were probed by Western blot analysis, using beta -actin (43 kDa) as loading control. Quantification of Western Blot results was performed with Image J software (//rsb.info.nih.gov/ij/) with normalization to beta -actin. WT to A2bAR KO: IRS-2 p-value = 0.0092, SREBP-1 p-value = 0.0154; CD68-Tg to A2bAR KO: IRS-2 p-value = 0.0247, SREBP-1 p-value = 0.0170. Data are averages ± SD. *Student two-tail t-test assuming equal variance was found significant only when p-value <0.05. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/24892847), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: SREBP1 Antibody - BSA Free [NB100-2215] - MiR-181a overexpression or SIRT1 knockdown impairs glucose & lipid metabolism in vivo(Aa & Ab) Immunoblotting analysis (left) & quantification (right) of SIRT1, PGC-1 alpha & acetylated PGC-1 alpha in the liver of mice injected with Ago-181a or Ago-NC or Ad-shRNA NC or Ad-shRNA SIRT1. (B) Glucose tolerance test of mice injected with Ago-181a (n = 7) or Ago-NC (n = 7) or Ad-shRNA NC (n = 6) or Ad-shRNA SIRT1 (n = 6). (C) Insulin tolerance test of mice injected with Ago-181a (n = 7) or Ago-NC (n = 7) or Ad-shRNA NC (n = 6) or Ad-shRNA SIRT1 (n = 6). (D) Representative images of PAS staining (original magnification × 20) of liver sections from mice injected with Ago-181a or Ago-NC or Ad-shRNA NC or Ad-shRNA SIRT1. (Ea & Eb) Immunoblotting analysis (top) & quantification (bottom) of insulin-stimulated phosphorylation of IR, AKT & GSK3 beta in liver of mice injected with Ago-181a or Ago-NC or Ad-shRNA NC or Ad-shRNA SIRT1. (F) Representative images of H&E staining (left, original magnification × 20) & Oil-red staining (right, original magnification × 20) of liver sections from mice injected with Ago-181a or Ago-NC or Ad-shRNA NC or Ad-shRNA SIRT1. (Ga & Gb) Immunoblotting analysis (top) & quantification (bottom) of SREBP-1c & PPAR alpha in the liver of mice injected with Ago-181a or Ago-NC or Ad-shRNA NC or Ad-shRNA SIRT1. *P < 0.05, **P < 0.01. All experiments were repeated at least three times & representative results are shown. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/29207650), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: SREBP1 Antibody - BSA Free [NB100-2215] - MiR-181a overexpression impairs & miR-181a inhibition improves glucose & lipid metabolism in vitro(A, B, C, D & E) Hepatocytes were transfected with 10 nM miR-181a mimics or negative controls in the absence or presence of 100 nM insulin. (A) Immunoblot analysis (left) & quantification (right) of insulin-stimulated phosphorylation of IR, Akt & GSK3 beta in hepatocytes. (B) The mRNA expression levels of G6Pase & PEPCK in hepatocytes. (C) Glucose concentration in medium. (D) Immunoblot analysis (left) & quantification (right) of SREBP-1c & PPAR alpha expression in hepatocytes. (E) TG content in hepatocytes. (F, G, H, I & J) Hepatocytes were transfected with 50 nM miR-181a inhibitors or negative controls in the absence or presence of 100 nM insulin. (F) Immunoblot analysis (left) & quantification (right) of insulin-stimulated phosphorylation of IR, Akt & GSK3 beta in hepatocytes. (G) The expression levels of G6Pase & PEPCK in hepatocytes. (H) Glucose concentration in medium. (I) Immunoblot analysis (left) & quantification (right) of SREBP-1c & PPAR alpha expression in hepatocytes. (J) TG content in hepatocytes. *P < 0.05, **P < 0.01. All experiments were repeated at least three times & representative results are shown. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/29207650), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: SREBP1 Antibody - BSA Free [NB100-2215] - Effect of restoration of macrophage A2bAR on adipose tissue.Visceral (epididymal) adipose tissue was collected from WT, A2bAR KO, & CD68-Tg mice after 16 weeks of HFD as described in the methods. A-C,E. Relative mRNA expression was determined using the delta delta CT method with normalization to 18s rRNA. A. mRNA expression of TNF-alpha in visceral fat. A2bAR KO (n = 7) vs CD68-Tg (n = 9) p-value = 0.0345. B. mRNA expression of IL-6 in visceral fat. A2bAR KO (n = 7) vs WT (n = 7) p-value = 0.0073; A2bAR KO vs CD68-Tg (n = 7) p-value = 0.0141. C. mRNA expression of MCP1 in visceral fat. A2bAR KO (n = 7) vs CD68-Tg (n = 9) p-value = 0.0232. D. Visceral adipose tissue from WT, A2bAR KO, & CD68-Tg mice after 16 weeks of HFD was fixed in 4% paraformaldehyde & paraffin-embedded. Sections immunostained with the macrophage marker F4/80. Representative sections for each genotype at a magnification of 200x & 400x. Arrows point to crown-like structures. E. mRNA expression of IRS-2 in visceral fat. CD68-Tg (n = 8) vs A2bAR KO (n = 8) p-value = 0.0115, WT (n = 6) vs A2bAR KO p-value = 0.0358. F. Western blot analysis of visceral fat; one representative (of 3 sets) WT, CD68-Tg & A2bAR KO group shown at 15 minutes post-insulin injection, following 16 weeks of HFD. WT to A2bAR KO: IRS-2 p-value = 0.0411, SREBP-1 p-value = 0.0103. CD68-Tg to A2bAR KO: IRS-2 p-value = 0.0305, SREBP-1 p-value = 0.0459. Data are averages ± SD. *Student two-tail t-test assuming equal variance was found significant only when p-value <0.05. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/24892847), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: SREBP1 Antibody - BSA Free [NB100-2215] - SIRT1 knockdown impairs & SIRT1 overexpression improves glucose & lipid metabolism in hepatocytes(A) Immunoblot analysis (left) & quantification (right) of insulin-stimulated phosphorylation of IR, Akt & GSK3 beta protein levels in hepatocytes. Hepatocytes were transfected with SIRT1 siRNA with or without 100 nM insulin. (B) Immunoblot analysis (left) & quantification (right) of SREBP-1c & PPAR alpha protein levels in hepatocytes. Hepatocytes were transfected with SIRT1 siRNA. (C) Immunoblot analysis (left) & quantification (right) of SIRT1, PGC-1 alpha & acetylated PGC-1 alpha in hepatocytes. Hepatocytes were infected with Ad-SIRT1. (D) Immunoblotting analysis (left) & quantification (right) of insulin-stimulated phosphorylation of IR, AKT & GSK3 beta in hepatocytes. Hepatocytes were treated with 1.2 mM NEFA or 1.2 mM NEFA & Ad-SIRT1 with or without 100 nM insulin. (E, F & G) Hepatocytes were treated with 1.2 mM NEFA or 1.2 mM NEFA & Ad-SIRT1. (E) Glucose concentration in medium. (F) Immunoblot analysis (top) & quantification (bottom) of SREBP-1c & PPAR alpha in hepatocytes. (G) TG contents in hepatocytes. *P < 0.05, **P < 0.01. All experiments were repeated at least three times & representative results are shown. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/29207650), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Reactivity:

Hu, Mu, Rt, Po, Bv, Ha, Pl, ChHa

Species Glossary

Reactivity: Hu, Mu, Rt, Po, Bv, Ha, Pl, ChHa

Applications:

, , , ,

Applications: , , , ,

Host:

Rabbit Polyclonal

Host: Rabbit Polyclonal

Sizes:

Sample Size Available

Sizes: Sample Size Available

Conjugate:

Unconjugated

Available Conjugates:

Conjugate	Catalog #	Availability	Size	Price
Alexa Fluor 350	NB100-2215AF350
Alexa Fluor 405	NB100-2215AF405
Alexa Fluor 488	NB100-2215AF488
Alexa Fluor 532	NB100-2215AF532
Alexa Fluor 594	NB100-2215AF594
Alexa Fluor 647	NB100-2215AF647
Alexa Fluor 700	NB100-2215AF700
Alexa Fluor 750	NB100-2215AF750
Allophycocyanin	NB100-2215APC
Biotin	NB100-2215B
CoraFluor 1	NB100-2215CL1
DyLight 350	NB100-2215UV
DyLight 405	NB100-2215V
DyLight 488	NB100-2215G
DyLight 550	NB100-2215R
DyLight 594	NB100-2215DL594
DyLight 650	NB100-2215C
DyLight 680	NB100-2215FR
DyLight 755	NB100-2215IR
FITC	NB100-2215F
HRP	NB100-2215H
Janelia Fluor 525	NB100-2215JF525
Janelia Fluor 549	NB100-2215JF549
Janelia Fluor 646	NB100-2215JF646
Janelia Fluor 669	NB100-2215JF669
PE	NB100-2215PE
PerCP	NB100-2215PCP
mFluor Violet 450 SE	NB100-2215MFV450
mFluor Violet 500 SE	NB100-2215MFV500
mFluor Violet 610 SE	NB100-2215MFV610

Available Formulations

Formulation	Catalog #	Availability	Price
BSA Free	NB100-2215SS

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NB400-148

Niemann-Pick C1 Antibody - BSA Free

(6 Reviews)

(54 Publications)

0.1 ml

NB400-148

Immunohistochemistry-Paraffin: Niemann-Pick C1 Antibody - BSA Free [NB400-148] - Staining of human brain, cortex, neurons and astrocytes.

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.

<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.

<b>Genetic Strategies Validation. </b>Knockout Validated: 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.

<b>Genetic Strategies Validation. </b>Knockdown Validated: Niemann-Pick C1 Antibody - BSA Free [NB400-148] - HeLa lysate, BHK lysate, A431 lysate tested at 1:1000. Image from verified customer review.

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 µg protein/lane.

$Immunocytochemistry/ Immunofluorescence: Niemann-Pick C1 Antibody - BSA Free [NB400-148] - ESCRT complex recruited to LLOMe-damaged lysosomes promotes cell survival.Human fibroblasts were exposed to 1 mM LLOMe & when indicated, the cell permeable calcium chelator BAPTA-AM (1 µM) was added 10 min prior to LLOMe exposure. Immunocytochemical staining with corresponding colocalization analysis of a CHMP4B (green) & LAMP2 (red), b ALIX (green) & NPC-1 (red), & c CHMP4B (green) & LAMP2 (red) in fibroblasts exposed to LLOMe for 15 min. Nuclei are stained with DAPI (blue) & merged images show colocalization in yellow (n = 5). d Caspase-3 like activity in cells exposed to LLOMe for 8 h (n = 3). e Quantification of apoptotic & necrotic cells using Annexin V/PI staining in fibroblasts exposed to LLOMe for 6 h (n = 3). f Immunoblot of LAMP2 in digitonin-extracted cytosolic fractions from cells exposed to LLOMe for 2 h (n = 8) with corresponding quantitative analysis. *p < 0.05, **p < 0.01 & ***p < 0.001 compared to control (a–b) or LLOMe only (c–f). Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/32409651), licensed under a CC-BY license. Not internally tested by Novus Biologicals.$

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.

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.

Reactivity:

Hu, Mu, Rt, Po, ChHa, Ha, Pm

Species Glossary

Reactivity: Hu, Mu, Rt, Po, ChHa, Ha, Pm

Applications:

, , , , , ,

Applications: , , , , , ,

Host:

Rabbit Polyclonal

Host: Rabbit Polyclonal

Sizes:

Sample Size Available

Sizes: Sample Size Available

Conjugate:

Unconjugated

Available Conjugates:

Validated by:

Validated by:

Conjugate	Catalog #	Availability	Size	Price
Alexa Fluor 350	NB400-148AF350
Alexa Fluor 405	NB400-148AF405
Alexa Fluor 488	NB400-148AF488
Alexa Fluor 532	NB400-148AF532
Alexa Fluor 594	NB400-148AF594
Alexa Fluor 647	NB400-148AF647
Alexa Fluor 700	NB400-148AF700
Alexa Fluor 750	NB400-148AF750
Allophycocyanin	NB400-148APC
Biotin	NB400-148B
CoraFluor 1	NB400-148CL1
DyLight 350	NB400-148UV
DyLight 405	NB400-148V
DyLight 488	NB400-148G
DyLight 550	NB400-148R
DyLight 594	NB400-148DL594
DyLight 650	NB400-148C
DyLight 680	NB400-148FR
DyLight 755	NB400-148IR
FITC	NB400-148F
HRP	NB400-148H
Janelia Fluor 525	NB400-148JF525
Janelia Fluor 549	NB400-148JF549
Janelia Fluor 646	NB400-148JF646
Janelia Fluor 669	NB400-148JF669
PE	NB400-148PE
PerCP	NB400-148PCP
mFluor Violet 450 SE	NB400-148MFV450
mFluor Violet 500 SE	NB400-148MFV500
mFluor Violet 610 SE	NB400-148MFV610

Available Formulations

Formulation	Catalog #	Availability	Price
BSA Free	NB400-148SS

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NB400-113

SR-BI Antibody

(1 Review)

(46 Publications)

0.1 ml

NB400-113

Immunohistochemistry-Paraffin: SR-BI Antibody [NB400-113] - Analysis of a FFPE section of human adrenal gland tissue using 1:100 dilution of SR-BI antibody. The staining was developed using HRP-DAB based detection method and the nuclei of the cells were counterstained with hematoxylin. This antibody generated a specific staining of SR-BI/SCARB1 in the glandular cells. The staining was membrane-cytoplasmic in the zona glomerulosa cells while the signal was primarily localized to the membranes of the cells in the zona fasciculata and zona reticularis layers of the adrenal cortex.

Western Blot: SR-BI Antibody [NB400-113] - Cell surface expression of SR-BI in renal carcinoma cells. Western blot analysis of SR-BI in total cell lysates (left) and on the cell surface (right) in 786-O and 786-O-VHL cells. The Western blots were probed with anti-SR-BI (82 kDa), anti-TBP (40 kDa, used as a control for intracellular protein expression), and anti-Na+/K+-ATPase (110 kDa, used as a control for cell surface protein expression). Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/30173145/) licensed under a CC-BY license.

Reactivity:

Hu, Mu, Rt

Species Glossary

Reactivity: Hu, Mu, Rt

Applications:

, , , , ,

Applications: , , , , ,

Host:

Rabbit Polyclonal

Host: Rabbit Polyclonal

Sizes:

Sample Size Available

Sizes: Sample Size Available

Conjugate:

Unconjugated

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NB100-615

Caveolin-1 Antibody (7C8)

(3 Reviews)

(37 Publications)

0.1 ml

NB100-615

Immunohistochemistry-Frozen: Caveolin-1 Antibody (7C8) [NB100-615] - Immunofluorescence of human adipose tissue. Primary antibody at 1:250. IHC-Fr image submitted by a verified customer review.

Flow Cytometry: Caveolin-1 Antibody (7C8) [NB100-615] - An intracellular stain was performed on HeLa cells with Caveolin-1 Antibody (7C8) NB100-615APC (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 1 ug/mL for 30 minutes at room temperature. Both antibodies were conjugated to allophycocyanin.

Immunocytochemistry/Immunofluorescence: Caveolin-1 Antibody (7C8) [NB100-615] - Antibody at 1:200 dilution (ON incubation) on EaHy926 endothelial cell line showing a clear localization in lipid raft/membrane. Photo courtesy of Alberto Davalos, Yale School of Medicine.

Immunocytochemistry/Immunofluorescence: Caveolin-1 Antibody (7C8) [NB100-615] - HeLa cells were fixed for 10 minutes using 10% formalin and then permeabilized for 5 minutes using 1X PBS + 0.05% Triton X-100. The cells were incubated with anti-Caveolin-1 [7C8] conjugated to Alexa Fluor 488 (NB100-615AF488) at 20 ug/mL for 1 hour at room temperature. Nuclei were counterstained with DAPI (Blue). Cells were imaged using a 40X objective.

Flow Cytometry: Caveolin-1 Antibody (7C8) [NB100-615] - Intracellular flow cytometric staining of 1 x 10^6 CHO (A) and HEK-293 (B) cells using Caveolin 1 antibody (dark blue). Isotype control shown in orange. An antibody concentration of 1 ug/1x10^6 cells was used.

Flow Cytometry: Caveolin-1 Antibody (7C8) [NB100-615] - An intracellular stain was performed on HeLa cells with Caveolin-1 Antibody (7C8) NB100-615 (blue) and a matched isotype control (orange). Cells were fixed with 4% PFA and then permeablized with 0.1% saponin. Cells were incubated in an antibody dilution of 5 ug/mL for 30 minutes at room temperature, followed by mouse F(ab)2 IgG (H+L) APC-conjugated secondary antibody (F0101B, R&D Systems).

Reactivity:

Hu, Mu, Rt, Sh

Species Glossary

Reactivity: Hu, Mu, Rt, Sh

Applications:

, , , , ,

Applications: , , , , ,

Host:

Mouse Monoclonal

Host: Mouse Monoclonal

Sizes:

Sample Size Available

Sizes: Sample Size Available

Conjugate:

Unconjugated

Available Conjugates:

Conjugate	Catalog #	Availability	Size	Price
Alexa Fluor 350	NB100-615AF350
Alexa Fluor 405	NB100-615AF405
Alexa Fluor 488	NB100-615AF488
Alexa Fluor 532	NB100-615AF532
Alexa Fluor 594	NB100-615AF594
Alexa Fluor 647	NB100-615AF647
Alexa Fluor 700	NB100-615AF700
Alexa Fluor 750	NB100-615AF750
Allophycocyanin	NB100-615APC
Biotin	NB100-615B
DyLight 350	NB100-615UV
DyLight 405	NB100-615V
DyLight 488	NB100-615G
DyLight 550	NB100-615R
DyLight 594	NB100-615DL594
DyLight 650	NB100-615C
DyLight 680	NB100-615FR
DyLight 755	NB100-615IR
FITC	NB100-615F
HRP	NB100-615H
Janelia Fluor 549	NB100-615JF549
Janelia Fluor 646	NB100-615JF646
mFluor Violet 450 SE	NB100-615MFV450
mFluor Violet 500 SE	NB100-615MFV500
mFluor Violet 610 SE	NB100-615MFV610

Available Formulations

Formulation	Catalog #	Availability	Price
Azide and BSA Free	NBP2-80617

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NB120-19294

LAMP-1/CD107a Antibody

(2 Reviews)

(36 Publications)

100 μg

NB120-19294

Immunocytochemistry/Immunofluorescence: LAMP-1/CD107a Antibody [NB120-19294] - Lamp1 (red) in HeLa cells.

Immunocytochemistry/Immunofluorescence: LAMP-1/CD107a Antibody [NB120-19294] - Cathepsin B (CathB) expression and localization in primary neurons. Colocalization of transfected CathB with LAMP-1/CD107a. CathB transfected neurons were examined by co-immunostaining of LAMP-1/CD107a and CathB. Yellow colored cytoplasmic spots are indicative of co-localization of transfected cathepsins and LAMP-1/CD107a. Scale bar = 10 micron. Image collected and cropped by CiteAb from the following publication (//molecularneurodegeneration.biomedcentral.com/articles/10.1186/1750-1326-6-37), licensed under a CC-BY license.

Autophagy associated protein immunoreactivity in HIV-infected brain tissue. (A) Representative images from five randomly selected fields of cells each examined in duplicate frontal lobe white matter sections for the indicated subject groups. The indicated proteins were labeled red & microglia with the cell-type-specific marker Iba1 (green). Blue staining indicates cell nuclei. Arrow heads indicate examples of higher Iba1 immunoreactivity whereas arrows indicate more focal (punctal) vs. diffuse (filamentous) patterns of autophagy associated protein expression. Scale bar = 10 μm. (B) Quantification of relative Iba1 immunoreactivity from (A). F(3,20) = 6.450, p = 0.0031; ∗p < 0.05 when compared to all other subject groups. Error bars show the SEM for the average values of 2–6 regions from each subject group across the six autophagy associated proteins examined. (C) Quantification of the indicated autophagy associated protein relative immunoreactivity from (A). Beclin 1: F(3,12) = 11.29, p = 0.0008; LC3B: F(3,12) = 1.994, p = 0.1687; APG7/ATG7: F(3,12) = 84.20, p = < 0.0001; ATG5: F(3,12) = 6.218, p = 0.0086; p62/SQSTM1: F(3,12) = 87.04, p = < 0.0001; LAMP1: F(3,12) = 8.317, p = 0.0029. ∗p < 0.05 when compared to HIV-negative; #p < 0.05 when compared to HIV-positive; & Ωp < 0.05 when compared to HIV-positive/NCI subjects. Error bars show the SEM for four regions from each subject group. Image collected & cropped by CiteAb from the following publication (//journal.frontiersin.org/Article/10.3389/fmicb.2015.00653/abstract), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Differences in neuronal autophagy & dendrite varicosity following HIV-1 Tat protein & morphine treatment. (A) Representative images of neurons transfected with a fluorescent reporter plasmid to monitor autophagic flux at 8 h following the indicated treatments. GFP (green) & GFP + mRFP (yellow) fluorescence are observed prior to the fusion of autophagosomes with lysosomes whereas only mRFP (red) fluorescence is present in post-fusion autolysosomes. DIC, differential interference contrast microscopy image. DAPI (blue) staining indicates cell nuclei. (B) Quantification of autolysosomes (red puncta) from (A). F(3,13) = 8.756, p = 0.0019; ∗p < 0.05 when compared to all other groups. (C) Western blotting analysis of the indicated autophagy associated protein levels at 24 h following the indicated treatments. GAPDH was used as a loading control. Blots are representative of three independent experiments. (D) Quantification of dendrite beading from (A). F(3,77) = 6.429, p = 0.0006; ∗p < 0.05 when compared to control cells. Error bars show the SEM. Image collected & cropped by CiteAb from the following publication (//journal.frontiersin.org/Article/10.3389/fmicb.2015.00653/abstract), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Immunocytochemistry/ Immunofluorescence: LAMP-1/CD107a Antibody [NB120-19294] - EsxG-EsxH alters phagosomal GAL3, ubiquitin, & LAMP1. (A, C, & E) IF images of GAL3 (A), ubiquitin (FK2 antibody) (C), & LAMP1 (E) in BMDMs that were infected with DsRed-expressing H37Rv (WT) or the delta esxH mutant for 3 h. Images are maximum-intensity projections. Scale bar, 10 μm. Boxed areas in the merged image are shown in higher magnification in the rightmost panel. Mtb, M. tuberculosis. (B, D, & F) Automated image analysis was used to quantify the MFI of GAL3 (B), ubiquitin (D), & LAMP1 (F) colocalized with individual bacilli from 5 fields of a 12-mm coverslip. Data are means ± SEM from one representative experiment from three (A, B, E, & F) or two (C & D) independent experiments. ****, P ≤ 0.0001, Student's t test. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/30482832), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Immunocytochemistry/ Immunofluorescence: LAMP-1/CD107a Antibody [NB120-19294] - Characterization of selected mutant protein glycosylation status or localization.(A) Two independent, representative experiments to analyze the glycosylation status of GFP-NPC1 wild type & GFP-NPC1 P251C/L929C, as determined by immunoblot of indicated samples with anti-GFP antibodies after 6% SDS PAGE; samples were incubated at 70°C in SDS PAGE sample buffer for 10 min prior to loading. Molecular weight markers are shown at left in kilodaltons here & in all subsequent gels shown. (B), Localization of NPC1 P251/L929C/P249K/P259K in NPC1−/− HeLa cells as in Figure 1C. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/32410728), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Immunocytochemistry/ Immunofluorescence: LAMP-1/CD107a Antibody [NB120-19294] - NPC1 delta loop mutant cannot rescue cholesterol export from lysosomes.(A) Cholesterol-cross-linked peptides (Hulce et al., 2013) are highlighted in red for two orientations of the crystal structure of N-terminal domain- & first transmembrane domain-deleted NPC1 (PDBID: 5u74). The disordered cytoplasmic loop residues 800–814 are shown as a blue dotted line. (B) Confocal immunofluorescence microscopy analysis of the localization of mouse NPC1-delta 807–811, NPC1-807-811Ala & LAMP1 proteins in HeLa cells (bar, 20 μm). White boxes in images indicate regions of cells enlarged in the insets shown at the lower right of each image. (C) Confocal immunofluorescence microscopy of cholesterol accumulation rescue. NPC1−/− HeLa cells were transfected with GFP-tagged mouse NPC1-delta 807–811 or mouse NPC1-807-811Ala plasmids for 48 h & assayed for cholesterol accumulation rescue as in Figure 1 (bar, 20 μm). (D) Quantitation of cholesterol accumulation rescue using flow cytometry. GFP-positive cells with similar expression levels were analyzed: 2480 NPC1; 427 NPC1-delta 807–811; 764 NPC1-807-811Ala; LAMP1 expressing control, 1753 cells counted. Shown are the normalized data from mean fluorescence intensity flow cytometry values. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/32410728), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Immunocytochemistry/ Immunofluorescence: LAMP-1/CD107a Antibody [NB120-19294] - Cathepsin D (CathD) & B (CathB) expression & localization in primary neurons. A. Western blot analyses of CathD & CathB protein levels after transfection. Primary cortical neurons were transfected with 23QHtt, 23QHtt plus CathD, 23QHtt plus CathB, 145QmHtt, 145QmHtt plus CathD & 145QmHtt plus CathB constructs. Western blot analyses were performed with anti-CathD & anti-CathB antibodies. beta -actin western blots were used as loading controls. Relative expression levels were quantified by band intensity. Positions of molecular weight markers were indicated. Quantification of the western blots are shown in the bar graphs. *p < 0.05 compared to without cathepsin transfection. B. Analyses of CathD & CathB enzymatic activities after transfection. Primary cortical neurons were transfected with CathD, CathB & as described in A. CathD & CathB activities were assayed by CathD or CathB activity assay kit. *p < 0.05 compared to without cathepsin transfection. C & D. Colocalization of transfected CathD (C) & CathB (D) with LAMP-1. CathD & CathB transfected neurons were examined by co-immunostaining of LAMP-1 & CathD or CathB. Yellow colored cytoplasmic spots are indicative of co-localization of transfected cathepsins & LAMP-1. Scale bar = 10 micron. Image collected & cropped by CiteAb from the following publication (//molecularneurodegeneration.biomedcentral.com/articles/10.1186/1750-1326-6-37), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: LAMP-1/CD107a Antibody [NB120-19294] - Effects on autophagic activity & dendritic length of neurons exposed to supernatant from HIV-1-infected microglia in combination with morphine. (A) Representative images of neurons with the indicated treatments. Sup, supernatant from uninfected [HIV(-)] & HIV-1-infected [HIV(+)] microglia. Cells were immunolabeled with antibodies to the autophagic activity marker p62/SQSTM1 (red) & the neuronal cell-type-specific marker MAP2 (green). DAPI (blue) staining indicates cell nuclei. (B) Quantification of p62/SQSTM1 immunoreactivity from (A). Data are presented as the percentage of control cells which was set at 100; F(5,24) = 5.882, p = 0.0011; ∗p < 0.05 when compared to HIV(+)Sup + morphine treatment. (C) Western blotting analysis of p62/SQSTM1 & LAMP1 expression levels for the indicated treatments. GAPDH was used as a loading control. Blots are representative of three independent experiments. (D) Measurement of dendrite length from (A). F(5,24) = 26.15, p = < 0.0001; Φp < 0.05 when compared to morphine; Ψp < 0.05 when compared to HIV(-)Sup; Ωp < 0.05 when compared to HIV(-)Sup + morphine; #p < 0.05 when compared to HIV(+)Sup; & ∗p < 0.05 when compared to HIV(+)Sup + morphine treatment. Error bars show the SEM for five randomly selected fields totaling at least 100 cells from each group. Image collected & cropped by CiteAb from the following publication (//journal.frontiersin.org/Article/10.3389/fmicb.2015.00653/abstract), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Immunocytochemistry/ Immunofluorescence: LAMP-1/CD107a Antibody [NB120-19294] - NPC1 Disulfide bond-locked MLD & CTD fails to rescue cholesterol export from lysosomes.(A) Partial NPC1 structure; inset, close-up view of the MLD/CTD interface. The amino acid residues mutated to cysteines for disulfide bond formation are shown & highlighted in red. (B) Confocal immunofluorescence microscopy analysis of mouse NPC1-A521C/K1013C & LAMP1 proteins in HeLa cells (bar, 20 μm). White boxes in images indicate regions of cells enlarged in the insets shown at the lower right of each image. (C) Confocal immunofluorescence microscopy of cholesterol accumulation rescue for NPC1-A521C or mouse NPC1-A521C/K1013C. (D) Flow cytometry of the rescue experiment analyzed in (C). GFP-positive cells with similar expression levels were analyzed: 17746 NPC1-/- cells; 1315 NPC1 wild type; 1137 NPC1-A521C/K1013C cells; 837 NPC1-A521C cells; cell numbers were normalized for comparison.Extracted ion chromatograms from LC-MS analysis of proteolyzed A521C/K1013C NPC1.Protein was carbamidomethylated in the presence or absence of reducing agent prior to deglycosylation & proteolysis. In both samples, blue traces represent m/z = 596.2818 (corresponding to the NPC1 peptide APCSLNDTSLL carbamidomethylated at the engineered cysteine A521C & deamidated at the N524 glycosylation site). Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/32410728), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Reactivity:

Hu, Mu, Rt

Species Glossary

Reactivity: Hu, Mu, Rt

Applications:

, ,

Applications: , ,

Host:

Rabbit Polyclonal

Host: Rabbit Polyclonal

Conjugate:

Unconjugated

Available Conjugates:

Conjugate	Catalog #	Availability	Size	Price
Alexa Fluor 350	NB120-19294AF350
Alexa Fluor 405	NB120-19294AF405
Alexa Fluor 488	NB120-19294AF488
Alexa Fluor 532	NB120-19294AF532
Alexa Fluor 594	NB120-19294AF594
Alexa Fluor 647	NB120-19294AF647
Alexa Fluor 700	NB120-19294AF700
Alexa Fluor 750	NB120-19294AF750
Allophycocyanin	NB120-19294APC
Biotin	NB120-19294B
CoraFluor 1	NB120-19294CL1
DyLight 350	NB120-19294UV
DyLight 405	NB120-19294V
DyLight 488	NB120-19294G
DyLight 550	NB120-19294R
DyLight 594	NB120-19294DL594
DyLight 650	NB120-19294C
DyLight 680	NB120-19294FR
DyLight 755	NB120-19294IR
FITC	NB120-19294F
HRP	NB120-19294H
Janelia Fluor 525	NB120-19294JF525
Janelia Fluor 549	NB120-19294JF549
Janelia Fluor 646	NB120-19294JF646
Janelia Fluor 669	NB120-19294JF669
PE	NB120-19294PE
PerCP	NB120-19294PCP
mFluor Violet 450 SE	NB120-19294MFV450
mFluor Violet 500 SE	NB120-19294MFV500
mFluor Violet 610 SE	NB120-19294MFV610

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At	=	A. thaliana	SyHa	=	Golden Syrian Hamster
All	=	All Species	Ha	=	Hamster
An	=	Animal	Hu	=	Human
ArHa	=	Armenian Hamster	I	=	Insect
Av	=	Avian	Ll	=	Llama
Bb	=	Baboon	Ma	=	Mammal
Ba	=	Bacteria	Mk	=	Monkey
Bv	=	Bovine	Mu	=	Mouse
Ca	=	Canine	Multi	=	Multi-species
Ce	=	C. Elegans	NA	=	Non-species specific
Ch	=	Chicken	Or	=	Orangutan
ChHa	=	Chinese Hamster	Pl	=	Plant
Cm	=	Cynomolgus Monkey	Pm	=	Primate
Do	=	Donkey	Po	=	Porcine
Dr	=	Drosophilia	Rb	=	Rabbit
Ec	=	E. Coli	Rt	=	Rat
Eq	=	Equine	RM	=	Rhesus Macaque
Fe	=	Feline	Sh	=	Sheep
Ft	=	Ferret	Vb	=	Vertebrate
Fi	=	Fish	Vi	=	Virus
Fu	=	Fungi	Xp	=	Xenopus
Ge	=	Gerbil	Ye	=	Yeast
GP	=	Guinea Pig	Ze	=	Zebrafish
Gt	=	Goat

Category

Protein/Target

Applications

Reactivity

Citation

Antibody Validation

Reviews

Host

Available Conjugates

Format

Marker

Modification

Clonality

Clone

Gene Symbol

Images Type

Isotype

Kit Type

Preservative

Protein Or Peptide

Research Areas

Has Sample Size

Promotional Item

Species Glossary

ABCA1 Antibody - BSA Free

PGC1 alpha Antibody - BSA Free

SR-BI Antibody - BSA Free

ABCG1 Antibody - BSA Free

SR-BI Antibody - BSA Free

BMAL1 Antibody

SREBP1 Antibody (2A4) - BSA Free

SREBP1 Antibody - BSA Free

Niemann-Pick C1 Antibody - BSA Free

SR-BI Antibody

Caveolin-1 Antibody (7C8)

LAMP-1/CD107a Antibody