Lipid-and-Metabolism reagents: Novus Biologicals

NB300-221

GAPDH Antibody (1D4) - BSA Free

(19 Reviews)

(455 Publications)

0.1 ml

NB300-221

Analysis of GAPDH in human nucleus pulposus cell culture (40ug/lane) using anti-GAPDH antibody. LI-COR Odyssey imaging system was used for detection. Western blot image submitted by a verified customer review.

Analysis of of HeLa cells stained with GAPDH antibody, dilution 1:100 (Green). DAPI staining of nuclear DNA (Blue). The GAPDH antibody produces strong cytoplasmic staining of healthy cells.

Analysis of cell line lysates probed with mouse mAb to GAPDH (theoretical molecular weight: 36 kDa), NB300-221, dilution 1:2,000: [1] protein standard, [2] HEK293, [3] HeLa, [4] SH-SY5Y, [5] COS1, [6] NIH-3T3, and [7] C6 cells. The GAPDH antibody reveals a single band at ~37 kDa in all cell lines. GAPDH is a house keeping protein, the level of which is relatively unaffected by most experimental manipulations, and, as a result, this antibody has been widely used as a western blotting loading control.

Human eye cell lysate. Antibody used at 1:500. WB image submitted by a verified customer review.

Analysis of GAPDH in chicken pectoralis major using anti-GAPDH antibody. The primary antibody was used at a dilution of 1:4000, incubated for 1 hour at room temperature. Western blot image submitted by a verified customer review.

Application of the approach to other cell lines. The remainder of the protocol from Figure 2 was then applied using 100 ug/mL digitonin as the optimal cytosolic extract in each case. An aliquot of each extract was then analyzed by 4-12% SDS PAGE followed by Western blotting and probing with antibodies to GAPDH, BiP and Histone H3 (Used as an alternative nuclear marker due to weakness of the Lamin A signal in HeLa cells). Image collected and cropped by CiteAb from the following publication (//bmcresnotes.biomedcentral.com/articles/10.1186/1756-0500-2-243) licensed under a CC-BY license.

Endothelial responses provoked by Hb-lipid interactions are attenuated by sulfide donors. Confluence HAoECs were exposed to the obtained Hb samples for 8 hours and VCAM-1 expression was determined by Western blotting. GAPDH were used as a loading control. Representative experiment, n = 3. Image collected and cropped by CiteAb from the following publication (//www.hindawi.com/journals/omcl/2018/3812568/), licensed under a CC-BY license.

Regulation of cell migration-associated proteins by NCKU-21 in A549 and CL1-5 cells. Protein expressions of matrix metalloproteinase-2 (MMP-2) and MMP-9 were analyzed in A549 cell treated with NCKU-21 for 24 hr. * P 1.2 to ≤1.3) & high (>1.3) of 3 × MYC-GFP-Bub1 signal & localization in live cells synchronized in mitosis by a thymidine release. Data represent the mean±s.e. of 3 independent experiments, with 58–61 cells measured per condition. Significance was measured for the high group by one-way analysis of variance (ANOVA) & pairwise t-test (Holm–Sidak). (e) Scatter plot of the cytoplasm versus kinetochore GFP levels of individual cells from each of the stable cell lines. The number of cells, R2 (measure of the goodness-of-fit) & significance (one-way ANOVA) are indicated. (f) Western blottings showing levels of the 3 × MYC-GFP-Bub1 proteins in the stable cell lines in whole cell extracts (left) & in cytoplasmic extracts (right). Scale bar, 10 μM. Image collected & cropped by CiteAb from the following publication (//www.nature.com/articles/ncomms9364), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

$Western Blot: GAPDH Antibody (1D4) [NB300-221] - Notch1, ApoER2 & Dab1 colocalize in hippocampal neurons. (A) Representative image of fluorescent immunolabeling shows that Notch1 is localized in a subset of CA3 neurons, co-expressing Dab1 & ApoER2 (magnified insert). ApoER2 is highly expressed in all CA3 neurons. (B) Fluorescent immunolabeling shows the distribution of Notch1 & Dab1 as compared to Arc/Arg3.1 in CA3 neurons. (B′) Close up of a dendrite showing colocalization of the three proteins (white arrowheads). (C) Western blot analysis on immunoprecipitated samples from whole hippocampal lysate shows that Notch1 displays a strong interaction with Dab1 whereas Notch1 & ApoER2 interaction appears weaker in the preparation (n = 4 independent experiments). (D) Immunolabeling on immunoprecipitated samples from whole cortical lysates show that Notch1 & Dab1 interact. ApoER2 is bound to both Notch1 & Dab1 (n = 3 independent experiments). (E) Co-IP from synaptosomal membrane fractions reveals a stronger interaction between Notch1 & ApoER2, which is reduced in the N1cKO (n = 3 independent pulldowns). In (C–E) GAPDH is used as a loading control for the inputs & to detect contamination in the IP samples. Scale bar in (A) is 50 μm & (B) 25 μm. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/26635527), licensed under a CC-BY license. Not internally tested by Novus Biologicals.$

Western Blot: GAPDH Antibody (1D4) [NB300-221] - Reduced expression of UNC5A in FancC−/− cells. a Reduced expression of Unc5A in brain cortex of FancC−/− mice compared to wild-type littermates. Western blotting was performed with the indicated antibodies. Each lane represents a different animal (WT: n = 6; FancC−/−: n = 8). b Bar graph represents ratio of Unc5A normalized to tubulin from WT (n = 6) & FancC−/− mice (n = 8). c Bar graph representation of UNC5A expression normalized to Sdha & Tbp from wild-type (WT) & FancC−/−-derived fibroblasts (n = 3). RLU: Relative light units. d–f HEK293T cells were transfected with UNC5AICD, FANCE & FANCC constructs expressing full-length FANCC (in d), FANCC1–306 (in e) or FANCC307–558 (in f). Constructs were transfected at a molecular ratio of 1:1:1 or with 10 times the molar amount of FANCE, FANCC or UNC5AICD as indicated in the figure. The total amount of transfected plasmid was equalized for all strategies with control empty vectors. Representative immunoblots performed with anti-HA (UNC5AICD), anti-FANCC, anti-FANCE or anti-GAPDH antibodies are shown. Arrows indicate appropriate protein bands. Bar graphs represent the mean fold change ± SEM of UNC5A protein levels normalized to GAPDH compared to 1:1:1 transfection controls in at least 4 separate experiments. *p < 0.05; **p < 0.005 Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/30213274), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: GAPDH Antibody (1D4) [NB300-221] - Depletion of RAD21 & other cohesin subunits leads to differentiation of ESCs.(A): qPCR analysis of esiRNA knock-down efficiency for indicated genes (48 h RNAi, n = 3, error bars denote s.d. & *, ** indicate p<0.05 & 0.01 respectively). Transfection of a non-targeting esiRNA (Luc) was used as a control. Numbers adjacent to the gene names indicate independent, non-overlapping esiRNAs transfected. (B): Western Blot analysis of esiRNA knock-down efficiency for indicated genes (48 h RNAi; esi-1 & esi-2 indicate independent, non-overlapping esiRNAs transfected). Transfection of a non-targeting esiRNA (Luc) was used as a control. GAPDH served as a protein loading control. (C): Alkaline phosphatase staining of ESCs, which had been transfected with esiRNAs targeting RAD21, SMC1a & SMC3 (72 h post RNAi) showed a strong differentiation phenotype compared to a control (Luc). Nanog depletion served as a positive control for ESC differentiation. Scale bars correspond to 100 µm. (D): Quantification of alkaline phosphatase staining (n = 3) separated into undifferentiated (green), mixed (yellow) & differentiated colonies (red). (E+F): qPCR validation of expression changes of (E) stem cell maintenance genes & (F) lineage marker genes upon knock-down of RAD21 (two independent esiRNAs) & Luc control (48 h RNAi, n = 3, error bars denote s.d. & *, **, *** indicate p<0.05, 0.01 & 0.001 respectively). Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/21589869), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: GAPDH Antibody (1D4) [NB300-221] - Application of the approach to other cell lines. (A) HT1080 cells (2 × 105) & HeLa cells (1 × 105) were plated in the wells of a 12 well plate & the digitonin concentration required for optimal extraction of the cytosol was determined as in Figure1. (B) The remainder of the protocol from Figure 2 was then applied using 100 μg/ml digitonin as the optimal cytosolic extract in each case. An aliquot of each extract was then analyzed by 4-12% SDS PAGE followed by Western blotting & probing with antibodies to GAPDH, BiP & Histone H3 (Used as an alternative nuclear marker due to weakness of the Lamin A signal in HeLa cells). (C) Samples were analyzed by 4-12% SDS PAGE followed by staining with Coomassie blue & then silver staining showing the difference in protein composition of each sample. The bracket alongside the gels marks the position of Histones in the RIPA nuclear extract & the asterisk next to the silver stained gels denotes protein bands unique to the E-RIPA extracts. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/20003239), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

$Western Blot: GAPDH Antibody (1D4) [NB300-221] - Role of the TRIM11-USP14 axis in cell growth & apoptosis. a Levels of endogenous TRIM11 in HCT116 cells grown at 43 °C for 0 or 90 min, or at 43 °C for 90 min, & then at 37 °C for 60 or 120 min. b, c Levels of endogenous TRIM11 (b), or Flag-TRIM11, the indicated proteasome subunits, & USP14 (c) in the SN & P fractions of HCT116 cells with & without heat shock at 43 °C for 90 min. d, g TRIM11 overexpression (d) or knockdown (g) HCT116 cells & the corresponding control cells grown under unstressed, heat shock, & heat shock plus recovery conditions were analyzed for K48 polyUb conjugates & caspase-3 activation. e, f, h Apoptosis in TRIM11 overexpression (e, f) or knockdown (h) HCT116 cells, & the corresponding control HCT116 cells, treated with & without heat shock. i, j Caspase-3 activation (i) & apoptosis (j) in HCT116 cells expressing the indicated proteins and grown under normal or heat stress conditions. k–m K48 polyUb conjugates, caspase-3 activation (k), amyloid-like fibrils (l), & apoptosis (m) in HCT116 cells expressing the indicated proteins and grown under normal & heat stress conditions. In e, f, h, j, l, & m, data represent mean ± SEM (n = 3 unless otherwise indicated). *P < 0.05; **P < 0.01; ***P < 0.001. Uncropped blots are presented in Supplementary Fig. 14 Image collected & cropped by CiteAb from the following publication (//www.nature.com/articles/s41467-018-03499-z), licensed under a CC-BY license. Not internally tested by Novus Biologicals.$

Reactivity:

Hu, Mu, Rt, Po, Av, Bv, Ca, Ch, ChHa, Dr, Eq, Fe, Ha, Ma-Op, Pm, Rb, Sh, Ze

Species Glossary

Reactivity: Hu, Mu, Rt, Po, Av, Bv, Ca, Ch, ChHa, Dr, Eq, Fe, Ha, Ma-Op, Pm, Rb, Sh, Ze

Applications:

, , , , , , ,

Applications: , , , , , , ,

Host:

Mouse Monoclonal

Host: Mouse Monoclonal

Sizes:

Sample Size Available

Sizes: Sample Size Available

Conjugate:

Unconjugated

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BSA Free	NB300-221SS

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NBP1-04676

PGC1 alpha Antibody - BSA Free

(11 Reviews)

(303 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.

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

An intracellular stain was performed on A431 human skin carcinoma cell line using Rabbit anti-PGC1 alpha Affinity Purified Polyclonal Antibody conjugated to Alexa Fluor® 647 (Catalog # NBP1-04676AF647, blue histogram) or matched control antibody (Catalog # NBP2-24981AF647, orange histogram) at 2.5 µg/mL for 30 minutes at RT.

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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BC100-494

PINK1 Antibody - BSA Free

(13 Reviews)

(300 Publications)

0.1 ml

BC100-494

$PINK1/Parkin-mediated mitophagy. Western Blot of mitochondrial and cytosolic fractions for PINK1, Parkin, and ubiquitin. E Quantitation of protein levels, normalized to VDAC and GAPDH, Ubiquitin: n = 6, PINK1: n = 5, Parkin: n = 8. R, post-reoxygenation. Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/33980811/) licensed under a CC-BY license.$

Confocal microscopy analysis of the mitophagy initiation in the RPE cells by staining PINK1 and PARKIN. One-year-old WT and dKO mice focusing on the RPE cells in the vicinity of the optic nerve (a,e). PINK1 (b, red) and PARKIN (c, green) were double-stained and the merged image (d) was used to count the colocalized puncta from WT. Similarly, in dKO PINK1 (f, red) and PARKIN (g, green) were double-stained, and the merged image (h) was used to count the colocalized puncta. dKO = NFE2L2/PGC1a double knockout. Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/32183173/) licensed under a CC-BY license.

Western blot image of PINK1 antibody (BC100-494) in multiple cells lines. Human HeLa (lane 1), Mouse NIH-3T3 (lane 2), L929 (lane 3) and Rat PC12 (lane 4) whole cell protein were separated by SDS-PAGE on a 7.5% polyacrylamide gel. Protein was transferred to PVDF membrane and probed with 2 ug/mL BC100-494 in 1% BSA and detected with an HRP-conjugated anti-rabbit secondary antibody using chemiluminescence. Observed molecular weight ~55 kDa (arrowhead).

Analysis of PINK1 in mouse liver and hypatocytes using PINK1 antibody. Observed molecular weight ~55 kDa. WB image submitted by a verified customer review.

Pathogenic mutants of Parkin are subjected to Ser65 phosphorylation. Phos-tag Western blotting for Parkin and Western blotting for PINK1 were performed using Parkin WT and a series of pathogenic mutants. Image collected and cropped by CiteAb from the following publication (//www.nature.com/articles/srep01002) licensed under a CC-BY license.

Alteration of mitochondria and PD associated proteins in SH-SY5Y cells with telomere removal by CRISPR-Cas9. Representative Western blot of PGC-1alpha, NRF1, and PINK1 in SH-SY5Y cells transfected with either gTel or gCont (72 h). Beta-actin served as a loading control. Image collected and cropped by CiteAb from the following publication (//www.mdpi.com/1422-0067/18/10/2093), licensed under a CC-BY license.

35 ug Neuro2A whole cell lysate separated on 8% PAGE and stained for PINK1 (1:1000 in 5% milk powder in TBST; secondary antibody AP at 1:5000). WB image submitted by a verified customer review.

Rabbit heart tissue. IHC-P image submitted by a verified customer review.

HEK293 cells were co-transfected with PINK1 siRNA (#1 or #2) or scrambled siRNA (scrambled) and untagged wild-type (WT) or Ser65Ala (S65A) mutant Parkin as indicated using TransFectin reagent (Bio-Rad). 48 hrs post-transfection, cells were treated with/without 10 uM CCCP for 3 h. 0.25 mg of 1% Triton whole-cell lysate were subjected to immunoprecipitation with GST-Parkin antibody (S966C) covalently coupled to protein G Sepharose and then immunoblotted with anti-phospho-Ser65 antibody in the presence of dephosphorylated peptide. 5% of the IP was immunoblotted with total anti-Parkin antibody. 0.25 mg of whole-cell lysates were immunoprecipitated with anti-PINK1 antibody (S085D) and immunoblotted with anti-PINK1 antibody. Representative of three independent experiments. Image collected and cropped by CiteAb from the following publication (//rsob.royalsocietypublishing.org/cgi/doi/10.1098/rsob.120080) licensed under a CC-BY license.

Characterisation of mitochondrial content and function in PINK1-/- platelets. Cropped immunoblots showing PINK1 expression in 10 uM CCCP (6 hours) treated WT, but not KO platelets by IP (upper panel) with loading control of IP inputs by blotting for PINK1 (lower panel). Uncropped blots for PINK1 are provided in Supplementary Fig. S1b. Image collected and cropped by CiteAb from the following publication (//www.nature.com/articles/s41598-018-32716-4), licensed under a CC-BY license.

Representative TEM picture. The red and green arrows indicate PINK and PARKIN immunogold particles in the dKO RPE samples, respectively (e). ML, melanosome. Scale = 0.2 um. Mitochondria (M). Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/32183173) licensed under a CC-BY license.

Protein content and oxidation. Gastrocnemius muscle was analyzed by immunoblotting (A) for oxidatively modified protein, STIM1, PARKIN, PINK1, PGC‐1 alpha , VDAC1, and 4HNE (B). Data are means ± SEM. *Significantly different from Tp53inp1+/+.

Western Blot: PINK1 Antibody - BSA Free [BC100-494] - PPM1H does not dephosphorylate Ser111 of Rab8A or key phosphorylation sites of AMPK & Akt signaling pathways.(A) HEK293 cells were transiently transfected with constructs expressing the indicated components. 24 hr post-transfection, cells were treated ±10 µM CCCP (Carbonyl cyanide m-chlorophenyl hydrazine) for 3 hr to induce activation of the PINK1 kinase & trigger Rab8A phosphorylation at Ser111 (Lai et al., 2015). (B) As in (A) except cells were immunoblotted with the indicated antibodies that recognize key phosphorylation sites of AMPK & Akt signaling pathways. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31663853), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: PINK1 Antibody - BSA Free [BC100-494] - PINK1 & Parkin are phosphorylated after a decrease in delta Ψm in mouse primary neurons. Neurons were infected with lentivirus encoding PINK1-Flag (A), wild-type HA-Parkin (B) or HA-Parkin with either the S65A or S65E mutation (C). Cells were treated with the mitochondrial uncoupler CCCP (30 μm) for 1–3 h & subjected to SDS-PAGE in the absence or presence of 50 μm phos-tag. Note that mobility does not reflect the molecular weight of proteins in phos-tag PAGE (Kinoshita et al. 15), & thus, molecular weight markers are not shown in the bottom gels. The red & black asterisks in (C) indicate phosphorylation of Parkin at Ser65 & an additional minor phosphorylation site, respectively. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/23751051), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: PINK1 Antibody - BSA Free [BC100-494] - PINK1 translation is critical for the accumulation of PINK1 upon mitochondrial damage. aPINK1 mRNA levels were not altered by mitochondrial damage. HeLa cells were incubated with 10 μM CCCP or combination of 10 μM oligomycin & 4 μM antimycin for 2 h & then, PINK1 mRNA levels were measured by qRT-PCR. PINK1 mRNA level was normalized to the corresponding GAPDH levels & quantified as a percentage of control (n = 8, t-test). b, c Translation is involved in PINK1 accumulation upon CCCP treatment. HeLa cells were first pre-incubated with 100 μM cycloheximide (CHX) for 2 h & then washed. Cells were further incubated with 10 μM CCCP with or without CHX for 2 h (n = 4, two-way ANOVA). Values are mean ± SEM (n.s. = non-significant, ***p 1000 cells) & are shown as a percentage of control. Values are mean ± SEM (*p < 0.05, **p < 0.01, ***p < 0.001) Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/27456084), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: PINK1 Antibody - BSA Free [BC100-494] - Inhibition of endogenous miR-27a/b function increases human PINK1 expression. a Schematic diagram of sequence alignment of miR-27a/b & anti-miR-27a/b. Asterisks (*) indicate conserved nucleotides. b Inhibition of endogenous miR-27a/b function increased luciferase activities in HeLa cells. Cells were transfected with the reporter constructs containing the full-length 3′UTR of human PINK1 mRNA with wild-type (WT) or mutated (Mut) seed match sites downstream of Renilla luciferase gene. 48 h post-transfection, luciferase activities were measured (n = 4, t-test). c-f Inhibition of endogenous miR-27a/b increased PINK1 protein levels in HeLa (C-D) & M17 cells (E-F). Cells were transfected with 150 nM of anti-miR-27a/b or anti-control (anti-Ctl). 48 h post-transfection, cells were harvested for Western blot. PINK1 protein level was normalized to corresponding GAPDH level & quantified as a percentage of control (n = 4, t-test). Data are shown as a percentage of control. Values are mean ± SEM (n.s. = non-significant, **p < 0.01, ***p < 0.00) Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/27456084), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: PINK1 Antibody - BSA Free [BC100-494] - Regulation of PINK1 by miRNA. a Schematic diagram of AGO-specific RNA immunoprecipitation assay. b, cPINK1 mRNAs are associated with miRNA/RISC complex. HeLa cells were transfected with 50 nM of AGO2 siRNA or negative control. 48 h post-transfection, AGO2-bound mRNAs were pulled down from cell lysates with 2A8 anti-AGO2 antibody or non-specific IgG antibody. PINK1 mRNA levels were then measured by qRT-PCR. siRNA against AGO2 served as a quality control for AGO-specific RNA immunoprecipitation assay. PINK1 mRNA levels were quantified as a percentage of group 1 (n = 6, two-way ANOVA). d, e Knock-down of DICER1 increased PINK1 protein levels. HeLa cells were transfected with 50 nM DICER1 siRNA (DICER1 KD) or negative control (Ctl). 48 h post-transfection, cells were harvested for Western blot. The arrowhead indicates a full-length PINK1 band & the asterisk indicates a non-specific band. Each protein level was normalized to corresponding GAPDH level & quantified as a percentage of control (n = 4, t-test). Values are mean ± SEM (n.s. = non-significant, **p < 0.01, ***p < 0.001) Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/27456084), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: PINK1 Antibody - BSA Free [BC100-494] - The expression levels of microtubule protein light chain 3 (LC3B), PTEN inducing putative kinase 1 (PINK1), Parkin, mitofusin 1 (Mfn1), toll-like receptor (TLR) 9, cytochrome c oxidase 4 (COX4), myeloid differentiation factor 88 (MyD88), & nuclear factor (NF)-kappa B in lung tissues from animals with spontaneous breathing (CON) or mechanical ventilation at high tidal volume (HTV) with saline, antimycin A (AmA) or cyclosporine A (CsA). (A) Levels of PINK1, Parkin, & Mfn1 mRNA. (B) Levels of LC3B, PINK1, Parkin, & Mfn1 protein by Western blot. (C) Relative expression of LC3B-II/LC3B-I & PINK1 protein. (D) Relative expression of Parkin & Mfn1 protein. (E) Levels of TLR9 & COX4 mRNA. (F) Levels of MyD88 & nuclear factor-kappa B (NF-kappa B) mRNA. (G) Levels of TLR9, COX4, MyD88, & NF-kappa B protein by Western blot. (H) Relative expression of TLR9 & COX4 protein. (I) Relative expression of MyD88 & NF-kappa B protein. Fold expression for target genes was normalized to that measured for the beta -actin gene. Both of these experiments were in triplicate. aP < 0.05 vs. CON group;bP < 0.05 vs. HTV group; & cP < 0.05 vs. AmA group. Image collected & cropped by CiteAb from the following publication (//www.frontiersin.org/article/10.3389/fimmu.2018.01477/full), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: PINK1 Antibody - BSA Free [BC100-494] - Mitophagy contributes to removal of excess mitochondrial fragments in preeclampsia.(a, left panel) Representative TEM image of a cytotrophoblast from PTC & PE placenta collected at 29 weeks. Mitochondrial proximity to ER (MAM) is indicated by white arrows, mitochondrial fission events are depicted by white stars (scale bar: 500 nm; n = 8 separate PE placentae). (a, right panel) percentage of mitochondrial tethering to the ER in in PE vs. PTC (PE placentae, n = 8; PTC placentae, n = 7; unpaired Student’s t-test *P < 0.05). b Representative western blots for MFN2 & calreticulin in ER isolated from PE & PTC placentae (PE & PTC, n = 3 separate samples). c WB & associated densitometry of ASAH2 (normalized to TOM20) in mitochondria from PTC & PE placentae. d Representative TEM depicting mitophagy (white arrow) in cytotrophoblast cell from PE placenta (scale bar: 500 nm, n = 8 separate PE placentae). e Western blot & associated densitometry of PINK1 & Parkin in PE vs. PTC mitochondrial isolates. Densitometry for PINK1 blot was used to calculate the ratio of full-length PINK63kDa to cleaved PINK153kDa (PE & PTC, n = 4 separate placentae, *P < 0.05) Image collected & cropped by CiteAb from the following publication (//www.nature.com/articles/s41419-018-0360-0), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: PINK1 Antibody - BSA Free [BC100-494] - Deficiency or mutant PINK1 reduces phosphorylation of LETM1 at Thr192. a, b Proteins extracted from PINK1 WT or KO MEFs (a) or mouse brain (b) were subjected to IP with anti-LETM1, probed with pT192 & reprobed with anti-LETM1 by WB. c Proteins extracted from human fibroblast of control (Con) or a PINK1-Q456X patient (Q456X) were subjected to IP with anti-LETM1, probed with pT192 & reprobed with anti-LETM1 by WB. d HEK293 cells were transfected with Adtrack GFP control, AdPINK1-WT, & AdPINK1-Q456X mutant for 1 day. Endogenous LETM1 protein was isolated by IP with anti-LETM1, probed with pT192 & reprobed with anti-LETM1 by WB. e SH-SY5Y cells were treated with 25 µM rotenone for 8 or 16 h. Total cell lysates were either analyzed by WB with anti-PINK1, or subjected to IP with anti-LETM1, probed with pT192 & reprobed with anti-LETM1 antibodies by WB. All above experiments were replicated three times, respectively Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/29123128), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: PINK1 Antibody - BSA Free [BC100-494] - Polyphyllin I suppressed, & PINK1 knockdown further suppressed, tumor growth in a MDA-MB-231 xenograft modelA. Tumor volumes were measured every week & differed at the end of the treatment period (*P < 0.01 compared to shCon cells treated with PPI, ##P< 0.01 compared to shPINK1 cells treated with PPI). B. Representative image of tumors from each group. C. Body weight changes in mice during the 6 weeks of PPI treatment. There were no differences in body weights between the PPI-treated shCon & vehicle-treated shCon groups or between the PPI-treated shPINK1 group & shCon groups. D. Representative tumor tissues were sectioned & subjected to H&E staining, TUNEL assay, & immunohistochemistry staining for C-CASP3. Scale bars: 50 μm. E. Representative tumor tissues from each group were prepared & subjected to western blot using anti-DRP1, -PARK2, -LC3B, -PINK1, & -C-CASP3 antibodies. Image collected & cropped by CiteAb from the following publication (//www.oncotarget.com/lookup/doi/10.18632/oncotarget.14413), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: PINK1 Antibody - BSA Free [BC100-494] - Corticosterone affects NIX-dependent mitophagy through decreasing PGC1 alpha in vivo.a–f Mice exposed to vehicle, corticosterone (10 mg/kg), corticosterone w/ phorbol 12-myristate 13-acetate (PMA pretreatment, 200 μg/kg), or PMA alone for 7 days. a Slide samples for IHC immunostained w/ LAMP1 (green), TOMM20 (red), & DAPI (blue). Scale bars, 100 μm (magnification, ×200). n = 5. b The expressions of NIX, PTEN-induced kinase 1 (PINK1), & BCL2 interacting protein 3 (BNIP3) detected w/ WB where beta -actin used as a loading control. n = 5. c Slide samples for IHC immunostained w/ synpatophysin (green), PSD95 (red), & DAPI (blue). Scale bars, 100 μm (magnification, ×200). n = 5. d Synaptophysin & PSD95 detected by WB. Loading control is beta -actin. n = 5. e The mice subjected to Y-maze test to evaluate spatial memory function. n = 6. f The mice subjected to forced swim test to evaluate depression-like behavior. n = 5. g Vehicle or RU 486 (5 mg/kg) injected mice presented w//w/out corticosterone (10 mg/kg) for 3 days. The expressions of peroxisome proliferator-activated receptor gamma coactivator 1-alpha (PGC1 alpha ) & NIX visualized via WB. Loading control is beta -actin. n = 5. h The schematic model for mechanisms of inhibition in NIX-dependent mitophagy by glucocorticoid shown. All blots & IF images representative. n = 5 or 6 from each animal w/ two technical replicates each in results of IHC & WB. Quantitative data presented as a mean ± S.E.M. The representative images acquired by SRRF imaging system. Two-sided two-way ANOVA conducted except Fig. 8b, data of which analyzed by two-sided unpaired student’s t test. ** indicates p < 0.01 versus control & ## indicates p < 0.01 versus corticosterone, respectively. Data provided as a Source data file. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/33473105), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

$Western Blot: PINK1 Antibody - BSA Free [BC100-494] - Polyphyllin I triggers PINK1/PARK2-dependent mitophagyA. MDA-MB-231 cells were treated with 8 μM PPI for different periods of time as indicated, & PARK2, P62, & ubiquitin (UB) levels in mitochondrial fractions were determined by western blot. B. Cells were cotransfected with GFP-UB & RFP-mito & treated with 8 μM PPI for 9 h, after which PARK2 (Alexa Fluor 405, pink) & P62 (Alexa Fluor 647, blue) immunostaining was detected using confocal microscopy. C. Cells cotransfected with GFP-UB & RFP-LC3 were treated with 8 μM PPI for 9 h, after which PARK2 (Alexa Fluor 405, pink) & TOMM20 (Alexa Fluor 647, blue) immunostaining was detected using confocal microscopy. Scale bars: 10 μm. D-E. MDA-MB-231 cells were treated with 8 μM PPI for different periods of time as indicated; whole-cell lysates were then separated on 8% SDS-PAGE gels & analyzed by western blot using the anti-PINK1 antibody. Relative full-length (∼63 kDa) & cleaved (∼52 kDa) PINK1 levels were quantified by densitometry & normalized to Tubulin. The results were expressed as a percentage of control, which was set at 100%. Data are presented as mean ± SD (*P< 0.01 vs. the control). F. Cells were treated with 8 μM PPI for different periods of time as indicated, & whole-cell lysates were then subjected to western blot analysis. G. Cells were treated with 8 μM PPI for 9 h, after which mitochondrial fractions were prepared & subjected to immunoprecipitation using anti-PINK1 antibody; associated PARK2 was detected using immunoblotting. H. RFP-mito-expressing MDA-MB-231 cells were treated with 8 μM PPI for 9 h, & PINK1 (Alexa Fluor 488, green) & PARK2 (Alexa Fluor 405, pink) immunostaining were evaluated using confocal microscopy. Scale bars: 10 μm. Image collected & cropped by CiteAb from the following publication (//www.oncotarget.com/lookup/doi/10.18632/oncotarget.14413), licensed under a CC-BY license. Not internally tested by Novus Biologicals.$

Western Blot: PINK1 Antibody - BSA Free [BC100-494] - miR-27a/b suppress human PINK1 expression. a Schematic diagram of the conserved target sites of miR-27a/b in the 3′UTR of human PINK1 mRNA. Seed sequences were indicated in red. Asterisks (*) indicate the conserved nucleotides. b Schematic diagram of the luciferase reporter plasmids. The reporter constructs contain the full-length 3′UTR of human PINK1 mRNA with wild-type (WT) or mutated (Mut) seed match sites downstream of Renilla luciferase gene. c Overexpression of miR-27a/b decreased luciferase activities in HeLa cells. Cells were transfected with miR-27a/b or negative control (Ctl) along with reporter constructs as indicated. 48 h post-transfection, luciferase activities were measured (n = 4, one-way ANOVA). Renilla luciferase activity was normalized to the corresponding firefly luciferase activity. d-g Overexpression of miR-27a/b decreased PINK1 protein levels in HeLa (D-E) & M17 cells (F-G). Cells were transfected with miR-27a/b or negative control (Ctl). 48 h post-transfection, cells were harvested for Western blot (n = 4, t-test). PINK1 protein level was normalized to corresponding GAPDH level & quantified as a percentage of control. Data are shown as a percentage of control. Values are mean ± SEM (n.s. = non-significant, **p < 0.01, ***p < 0.001) Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/27456084), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: PINK1 Antibody - BSA Free [BC100-494] - Increased p62 expression is prevented in PINK1 knock‐down cells. (a) SH‐SY5Y cells expressing scrambled shRNA or PINK1 shRNA (117‐2, 118‐3, & 118‐4) were treated with 10 μM carbonyl cyanide m‐chlorophenylhydrazone (CCCP) for 24 h & full‐length (FL) PINK1 protein levels measured by western blot. No accumulation of FL PINK1 was observed in 118‐3 & 118‐4 PINK1 shRNA clones. (b) SH‐SY5Y cells constitutively expressing scrambled (scram) or PINK1 shRNA (clone 118‐3) were treated with vehicle or 10 μM CCCP for 24 h & p62 protein expression measured by western blotting. **p < 0.05 versus scram CCCP; n = 9. (c) SH‐SY5Y cells were incubated in serum‐free culture media for up to 24 h to induce starvation‐mediated macroautophagy. p62 protein levels were measured by western blotting. *p < 0.05 versus 0 h; **p < 0.01 versus 0 h; n = 4. (d) SH‐SY5Y cells were transfected with scrambled (scram) or p62 siRNA for 72 h. For the last 24 h, cells were treated with vehicle (ethanol) or 10 μM CCCP. p62 protein expression was then measured by western blotting. p62 protein was significantly decreased in p62 siRNA cells under basal conditions & following CCCP treatment, when compared to scram cells. **p < 0.01 versus scram vehicle or scram CCCP; n = 3. (e) Mitochondrial content was measured in SH‐SY5Y cells treated with scram or p62 siRNA for 72 h by measuring citrate synthase (CS) activity. For the last 24 h, cells were treated with vehicle or 10 μM CCCP & data are expressed as % of vehicle. *p < 0.05 versus scram CCCP treatment; n = 5. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/26509433), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: PINK1 Antibody - BSA Free [BC100-494] - NF kappa B upregulates human PINK1 gene expression. (A) NF kappa B increases the endogenous human PINK1 mRNA level. HEK293 cells were transfected with either the NF kappa B expression vector or empty vector pMTF. RT-PCRs were performed using either primers specific to the human PINK1 coding sequence or the human beta -actin coding sequence. (B) NF kappa B increases the endogenous human PINK1 protein levels. HEK293 cells transfected with NF kappa B were harvested 48 h after transfection for protein detection. Cell lysates were run on 10% glycine gel & images were collected by Licor. A significant increase of endogenous PINK1 was observed. (C) The endogenous human PINK1 protein level was dramatically increased by NF kappa B in SH-SY5Y cells. SH-SY5Y cells were transfected with NF kappa B p65 plasmids or the control vector pMTF & then harvested for protein detections. The human PINK1 protein & its proteolysis products ∆1-PINK1 (55kD) & ∆2-PINK1 (45kD) were all increased. beta -actin acted as the internal control. (D) LPS treatment facilitated PINK1 expression in SH-SY5Y cells. Cells were harvested after being treated for 16 h & then subjected to Western blot. The human beta -actin level was served as a control. Quantification was performed by Image J software. Values indicate means ± SEM. n = 3, *p <0.01 by Student’s t-test. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/25108683), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: PINK1 Antibody - BSA Free [BC100-494] - G-TPP induces PINK1 stabilization & kinase activity in HeLa cells(A) G-TPP treatment leads to PINK1 stabilization & pS65-Ub induction in HeLa cells. HeLa cells stably expressing untagged Parkin were treated with 10 µM G-TPP for the indicated times. Western blots were prepared with cell lysates & probed with antibodies against PINK1 & pS65-Ub. GAPDH served as a loading control. (B) pS65-Ub is induced in G-TPP treated cells & co-localizes with EGFP-Parkin & mitochondria. HeLa cells stably expressing EGFP-Parkin (green) were treated with 10 µM G-TPP for the indicated times & fixed. Cells were stained with antibodies against pS65-Ub (red) & the mitochondrial marker TOM20 (cyan). Scale bars correspond to 10 µM. (C) Quantification of Parkin translocation using High Content Imaging. HeLa EGFP-Parkin cells were treated for 4 or 8 h with or without 10 µM G-TPP. CCCP treatment (10 µM for 2 h) was used as a positive control. Cells were fixed, counterstained with Hoechst dye to visualize nuclei, imaged & analyzed using the ratio of cytoplasmic to nuclear EGFP signal [21]. Data was normalized to positive (2 h 10 µM CCCP treatment) & negative (2 h DMSO) controls. G-TPP significantly induced Parkin re-localization to levels similar to or beyond 2 h CCCP treatment. Shown are the mean values of three independent experiments with triplicate wells each ± SEM (one-way ANOVA with Tukey’s posthoc, ***p < 0.0005). Image collected & cropped by CiteAb from the following publication (//www.oncotarget.com/lookup/doi/10.18632/oncotarget.22287), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: PINK1 Antibody - BSA Free [BC100-494] - G-TPP leads to recruitment of autophagy adapters & degradation of mitochondria(A) HeLa cells stably expressing untagged Parkin were treated with 10 µM G-TPP for 8 h. Western blots were prepared from cell lysates & probed with antibodies against LC3, phospho-TBK1 (Ser172) & TBK1. GAPDH was used as a loading control. Upon 8 h the levels of LC3-I & LC3-II were both increased. At 8 h after treatment with G-TPP but not at 4 or 24 h, TBK1 was phosphorylated. (B) HeLa cells stably expressing EGFP-Parkin were treated with 10 µM G-TPP & fixed 8 h after treatment. Cells were stained with antibodies against the autophagy adapter proteins NBR1, NDP52, OPTN, p62, & TAX1BP1 (red). Mitochondria were counterstained with TOM20 antibodies (cyan), nuclei with Hoechst (blue). EGFP-Parkin epifluorescence is shown in green. Scale bar corresponds to 10 µM. (C) HeLa cells stably expressing EGFP-Parkin & the reporter protein mitoKeima were treated with 10 µM CCCP or G-TPP & imaged over time. The ratio of ‘neutral’ mitoKeima to ‘acidic’ mitoKeima was calculated as readout for mitophagy. Parkin translocation was monitored at the same time. Values for Parkin translocation & mitophagy were normalized to 12 h treatment with 10 µM CCCP as positive control & DMSO as negative control (two-way ANOVA with Tukey’s post-hoc test, **p < 0.005, ***p < 0.0005). Image collected & cropped by CiteAb from the following publication (//www.oncotarget.com/lookup/doi/10.18632/oncotarget.22287), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: Rabbit Polyclonal PINK1 Antibody [BC100-494] - PINK1 detection in mouse and postmortem human cortex samples. 1:1000 dilution at 4 degrees overnight to detect endogenous PINK1 from mouse and postmortem human cortex samples (10 ug total protein). Image from a verified customer review.

Reactivity:

Hu, Mu, Rt, Rb

Species Glossary

Reactivity: Hu, Mu, Rt, 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	BC100-494AF350
Alexa Fluor 405	BC100-494AF405
Alexa Fluor 488	BC100-494AF488
Alexa Fluor 532	BC100-494AF532
Alexa Fluor 594	BC100-494AF594
Alexa Fluor 647	BC100-494AF647
Alexa Fluor 700	BC100-494AF700
Alexa Fluor 750	BC100-494AF750
Allophycocyanin	BC100-494APC
Biotin	BC100-494B
CoraFluor 1	BC100-494CL1
DyLight 350	BC100-494UV
DyLight 405	BC100-494V
DyLight 488	BC100-494G
DyLight 550	BC100-494R
DyLight 594	BC100-494DL594
DyLight 650	BC100-494C
DyLight 680	BC100-494FR
DyLight 755	BC100-494IR
FITC	BC100-494F
HRP	BC100-494H
Janelia Fluor 525	BC100-494JF525
Janelia Fluor 549	BC100-494JF549
Janelia Fluor 646	BC100-494JF646
Janelia Fluor 669	BC100-494JF669
PE	BC100-494PE
PerCP	BC100-494PCP
mFluor Violet 450 SE	BC100-494MFV450
mFluor Violet 500 SE	BC100-494MFV500
mFluor Violet 610 SE	BC100-494MFV610

Available Formulations

Formulation	Catalog #	Availability	Price
BSA Free	BC100-494SS

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NB400-135

CHREBP Antibody - BSA Free

(7 Reviews)

(165 Publications)

0.1 ml

NB400-135

Immunohistochemistry-Paraffin: CHREBP Antibody - BSA Free [NB400-135] - CHREBP Antibody [NB400-135] - Staining of human colon, epithelium at a 40X magnification.

Chromatin Immunoprecipitation: CHREBP Antibody - BSA Free [NB400-135] - CHREBP Antibody [NB400-135] - Effects of glucose on ChREBP binding.HepG2 cells were treated with low (2.7 mM) and high (25 mM) glucose for 8 h. Chromatin was isolated and fragmented, and ChIP was performed with control IgG or anti-ChREBP antibody. Validated primers for each gene were used for quantitative real-time PCR. The data presented as fold increase for the signal from anti-ChREBP relative to control IgG. The negative control, Cyclo, showed no enrichment (data not shown). Values represent the mean +/- S.D. of three independent samples. *p<0.005 vs. IgG, #p<0.0001 vs. 2.7 mM glucose with anti-ChREBP. Image collected and cropped by CiteAb from the following publication (//dx.plos.org/10.1371/journal.pone.0022544), licensed under a CC-BY license.

Western Blot: CHREBP Antibody - BSA Free [NB400-135] - CHREBP Antibody [NB400-135] - Detection of ChREBP in 20 ug of human hepatocyte lysate using NB400-135. 5-10 second film exposure.

Western Blot: CHREBP Antibody - BSA Free [NB400-135] - CHREBP Antibody [NB400-135] - Detection of ChREBP in liver nuclear extracts from well-fed rats. 7% SDS-PAGE gel, 1:1000 dilution of NB400-135. Photo courtesy of Dr. Uyeda, UT Southwestern University.

Western Blot: CHREBP Antibody - BSA Free [NB400-135] - CHREBP Antibody [NB400-135] - RetSat depletion in mouse liver reduces protein levels and target gene expression of ChREBP. RetSat and ChREBP protein expression by immunoblotting. Image collected and cropped by CiteAb from the following publication (//www.nature.com/articles/s41467-017-00430-w), licensed under a CC-BY license.

Western Blot: CHREBP Antibody - BSA Free [NB400-135] - CHREBP Antibody [NB400-135] - Protein expression levels of carbohydrate-responsive element-binding protein (ChREBP), in livers of rats receiving normal water (CON), a 13% (w/v) glucose solution (GLU), a 13% (w/v) fructose solution (FRUC), or a 0.4% (w/v) aspartame solution (n = 6 per diet group). All data were normalized to beta-actin expression levels and are expressed relative to the controls (CON). Data are expressed as means +/- SEM. * p < 0.05, ** p < 0.01, *** p < 0.001 vs. CON; +p < 0.05, ++p < 0.01, +++p < 0.001 vs. ASP; p < 0.01, p < 0.001 vs. GLU. Image collected and cropped by CiteAb from the following publication (//www.mdpi.com/2072-6643/9/5/476), licensed under a CC-BY license.

Immunocytochemistry/Immunofluorescence: CHREBP Antibody - BSA Free [NB400-135] - CHREBP Antibody [NB400-135] - HeLa cells were fixed for 10 minutes using 10% formalin and permeabilized for 5 minutes using 1X TBS + 0.5% Triton X-100. The cells were incubated with anti-ChREBP (NB400-135) at a 1:200 dilution overnight at 4C and detected with an anti-rabbit DyLight 488 (Green) at a 1:500 dilution. Alpha tubulin was used as a co-stained at 1:1000 and detected with an anti-mouse DyLight 550 (Red) at a 1:500. Nuclei were counterstained with DAPI (Blue). Cells were imaged using a 40X objective.

Immunohistochemistry: CHREBP Antibody - BSA Free [NB400-135] - CHREBP Antibody [NB400-135] - Analysis of CHREBP in mouse liver using DAB with hematoxylin counterstain.

<b>Genetic Strategies Validation. </b>Western Blot: CHREBP Antibody - BSA Free [NB400-135] - Immunoblot analysis of ChREBP in liver lysates of control and L-Chrebp -/- mice. Aliquots (60 ug of protein) of liver whole-cell lysates were subjected to SDS-PAGE and immunoblot analysis with anti-ChREBP and anti-calnexin antibodies. ChREBP delta denotes a truncated aberrant ChREBP protein present only in lysates prepared from L-Chrebp -/- livers. Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/29335275/) licensed under a CC-BY license.

Analysis of protein levels in livers transfected with GK and GKA456V. Livers excised from mice in postabsorptive state were homogenized and resolved by Western blot. (a, b) Representative blots from three independent experiments. The densitometric analysis is presented (N = 4, *P < 0.05 versus pControl, ***P < 0.001 versus pGKA456V). (c) Liver sections of 5-hour fasted mice injected with pControl, pGK, or pGKA456V were immunostained with Glc6Pase antibody. TO-PRO-3 was used to visualize nuclei.

$Immunoblot analysis of livers from control & L-Chrebp−/− mice subjected to fasting & refeeding with a high-sucrose diet. Littermate control & L-Chrebp−/− mice (same as those described in supplemental Tables S2A & S2B) were subjected to fasting & refeeding. The nonfasted (N) groups were fed chow diet ad libitum. The fasted (F) group was fasted 12 h, & the refed (R) group was fasted for 12 h & then refed with 60% (w/w) high-sucrose diet for 12 h prior to study. Liver whole-cell lysates & membrane fractions were prepared individually, & equal amounts of protein from each mouse of the same group (four per group) were pooled. Aliquots (40 μg for whole-cell lysates & 30 μg for membrane fractions) of the pooled protein were subjected to SDS-PAGE & immunoblot analysis. Immunoblot analysis of Insig-1 & Insig-2 were carried out using membrane fractions. Whole-cell lysates were used to detect other proteins. The precursor & nuclear forms of SREBPs are denoted as P & N, respectively. Calnexin was used as loading control. Image collected & cropped by CiteAb from the following publication (//linkinghub.elsevier.com/retrieve/pii/S0022227520331369), licensed under a CC-BY license. Not internally tested by Novus Biologicals.$

Western Blot: CHREBP Antibody - BSA Free [NB400-135] - Raffinose stimulates transcription of genes involved in epidermal barrier function in HaCaT cells.(a & b) HaCaT cells were treated with vehicle, 1 μM or 10 μM raffinose (Raf), or 1 μM TO901317 (T17) for 24 h. Expressions of transcripts (a) & proteins (b) were analyzed by qRT-PCR or western blotting, respectively. FLG; filaggrin. IVL; involucrin, LOR; loricrin, AQP3; aquaporin3. (c) HaCaT cells were transfected with siGFP control, siLXR alpha , or siLXR beta , & then treated with 1 μM raffinose for 24 h. Expression of proteins was analyzed by western blotting. The original blots are shown in Supplementary Fig. S9. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/28266648), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Immunohistochemistry-Paraffin: CHREBP Antibody - BSA Free [NB400-135] - Impaired hepatic SIRT1-FoxO signaling in L-G6pc-/- mice.(A) Western blots & densitometry analysis (n = 5), & quantification of mRNA for hepatic SIRT1 & FoxO3a (n = 8). (B) Hepatic NAD+ levels (n = 9). (C) Western blots & densitometry analysis of PPAR-gamma , PPAR-alpha & beta -actin (n = 5). (D) Immunohistochemical analysis of hepatic ChREBP & quantification of nuclear ChREBP-translocated cells (n = 4). Scale bar, 25 μm. (E) Quantification of mRNA for hepatic Acaca, Fasn & Elovl6 by real-time RT-PCR (n = 6). (F) Western blots of acetylated & total FoxO3a after immunoprecipitation of nuclear extracts using anti-FoxO3a, & quantification of the acetylated FoxO3a/total FoxO3a (n = 5). Data represent the mean ± SEM. *P < 0.05, **P < 0.005. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/28558013), licensed under a CC0-1.0 license. Not internally tested by Novus Biologicals.

Western Blot: CHREBP Antibody - BSA Free [NB400-135] - Expressing recombinant ChREBP beta in Rictor-deficient adipocytes rescues expression of DNL enzymes.Western blot of indicated proteins in differentiated adipocytes with or without Rictor deletion transfected with various rescue constructs that were stably expressed in cells before differentiation. ‘*' indicates ChREBP beta based on molecular weight. Image collected & cropped by CiteAb from the following publication (//www.nature.com/articles/ncomms11365), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: CHREBP Antibody - BSA Free [NB400-135] - Hepatic expression of mRNAs encoding carbohydrate response element-binding protein (ChREBP) (a), liver pyruvate kinase (LPK) (c), & microsomal triglyceride transfer protein (MTTP) (d), & nuclear ChREBP protein (b) in water-control, 10% fructose solution-control, & fructose pair-fed oleanolic acid- (OA-) treated rats at week 10. Animals were administered with OA (25 mg/kg/day) or vehicle (OA: 0 mg/kg, 5% Gum Arabic) by oral gavage daily for 10 weeks. mRNA was determined by real-time PCR. Protein expression was determined by Western blot. Data are means ± SEM (n = 6 each group). *P < 0.05. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/23737835), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: CHREBP Antibody - BSA Free [NB400-135] - LXR mediate the induction of lipogenesis induced by an oleic acid-rich diet.(A) Hepatic Acly, Acaca, Acacb, Fasn, Elovl6, Scd1 mRNA levels quantified by qPCR. (B) Cytoplasmic protein expression levels of P-ACLY, ACLY, ACC, ELOVL6, SCD1, FASN & beta -ACTIN assayed by Western Blotting. (C) Fads1, Fads2, Elovl5, Gpat, Pnpla3 & Lpk mRNA quantification assayed by qPCR. (D) Srebp-1c & Chrebp mRNA quantification assayed by qPCR. (E) Cytoplasmic & nuclear expression levels of LXR, SREBP-1c & ChREBP assayed by Western Blotting. Data are the mean±SEM of values measured in LXR+/+ & LXR-/- mice fed REF or OLIV diet. a Significant genotype effect. b Significant difference versus REF diet (n = 6 mice per group). Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/28732092), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: CHREBP Antibody - BSA Free [NB400-135] - Analysis of protein levels in livers transfected with GK & GKA456V. Livers excised from mice in postabsorptive state were homogenized & resolved by Western blot. (a, b) Representative blots from three independent experiments. The densitometric analysis is presented (N = 4, *P < 0.05 versus pControl, ***P < 0.001 versus pGKA456V). (c) Liver sections of 5-hour fasted mice injected with pControl, pGK, or pGKA456V were immunostained with Glc6Pase antibody. TO-PRO-3 was used to visualize nuclei. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/22194744), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: CHREBP Antibody - BSA Free [NB400-135] - ChREBP knockdown inhibited glycolysis, lipogenesis & p21 in HT29 cells. (A) Inhibited relative mRNA expression of ChREBP alpha & ChREBP beta normalized to B2M after control or ChREBP siRNA transfection for 48 hours. (B) Western-blot of ChREBP, phospho-p53 & p21 & their quantification on the right. beta -actin was served as a loading control. Proteins were extracted from cells transfected with sicontrol & siChREBP after 48 hours. The quantification of western blot was normalized to beta -actin. (C) Decreased relative mRNA expression of glycolytic & lipogenic genes, normalized to B2M. (D) Relative mRNA expression of p53 & p21, normalized to B2M. (E) Relative mRNA expression of cell Cyclins, normalized to B2M. n = 4. *p < 0.05; **p < 0.01; ***p < 0.001. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/32144313), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: CHREBP Antibody - BSA Free [NB400-135] - Ligand-activated LXR reduces ChREBP binding to chromatin. (A). Left panels: Local pattern of LXR-ChREBP co-occupancy. Browser view of LXR & ChREBP tracks in the promoter region of Lpk (Pklr), Txnip, Fasn & Scd1. Square brackets indicate the scale maxima of ChIP/input ratios. Arrows indicate the genomic locations of quantitative RT-PCR primers. Right panel: AML12 cells transfected with ChREBP alpha /Mlx gamma & LXR alpha /RXR alpha were treated with DMSO (0.1%) or GW3965 (10 µM) for 18 h. ChREBP or LXR binding to genomic location indicated in the right panels were detected by ChIP using antibodies against ChREBP, LXR or IgG as negative control. Data are presented as mean ± SEM (n = 3–5). Significant differences are shown as * p < 0.05, ** p < 0.01, *** p < 0.001 compared to ChIP-IgG & #p < 0.05, ##p < 0.01, ###p < 0.001 between DMSO & GW3965 groups. ns, not significant. (B). CoIP of LXR alpha & ChREBP alpha , expressed in COS-1 cells cultured in 25 mM glucose, treated with DMSO (0.1%) or GW3965 (1 µM) for 18 h. Lysates were immunoprecipitated with ChREBP antibody (n = 3). Input & immunoprecipitated proteins were immunoblotted with ChREBP or LXR alpha antibodies. One representative western blot is shown. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/32414201), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: CHREBP Antibody - BSA Free [NB400-135] - Induction of hepatic Srebp-1 & carbohydrate response element-binding protein (Chrebp) beta expression by dietary glucose is reduced in LXR alpha −/− mice. (A) Hepatic gene expression of Lxr alpha / beta , Srebp-1, & Chrebp alpha / beta was analyzed by quantitative RT-PCR & normalized to Tbp; (B) Cytosolic & nuclear lysates were immunoblotted with antibodies against LXR, SREBP-1, & ChREBP with alpha -Tubulin & Lamin A as loading controls. Each lane represents independent mice from each group. One representative western blot is shown (n = 3). Data represent the mean ± SEM (n = 5). Significant differences were found using two-way ANOVA followed by Tukey’s multiple comparison test (fasted vs. fructose fed & fasted vs. glucose fed RNA data were analyzed separately). * p < 0.05, ** p < 0.01, *** p < 0.001 compared to fasted. #p < 0.05, ##p < 0.01, ###p < 0.001 compared to LXR alpha +/+ mice. Image collected & cropped by CiteAb from the following publication (//www.mdpi.com/2072-6643/9/7/678), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: CHREBP Antibody - BSA Free [NB400-135] - Decreased glucose uptake & Chrebp beta -driven DNL is a primary consequence of Rictor loss in adipocytes.(a) Western blots of indicated proteins at different days of differentiation using Rictor iKO primary adipocytes (described in Methods). (b) Oil Red O staining of differentiated adipocytes. (c) The relative mRNA level of ChREBP beta in differentiated cells at various time points. n=3. (d) 2-DG uptake in differentiated adipocytes without or with insulin stimulation. n=3. (e) The C14-glucose-derived FA in differentiated adipocytes. n=3. (f) The C14-glucose derived triglyceride (TAG) in differentiated adipocytes. n=3. (g) Relative glut4 expression in differentiated cells at various time points. n=3. (h) Relative glut4 expression in sWAT. n=8. (i) Glycerol release in differentiated adipocytes under basal & isoproterenol (Iso) stimulation. n=4. (j) Glycerol release in ex vivo pgWAT under basal & isoproterenol stimulation. n=6. Data were analysed by Student's t-test. Values are expressed as mean+s.e.m. *P<0.05; **P<0.01; ***P<0.001. Image collected & cropped by CiteAb from the following publication (//www.nature.com/articles/ncomms11365), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: CHREBP Antibody - BSA Free [NB400-135] - RetSat controls ChREBP activity & glucose sensing in primary hepatocytes. Primary mouse hepatocytes were treated with Control or RetSat siRNA for 48 h, (a, left) ChREBP mRNA expression determined by qPCR, & RetSat & ChREBP protein levels determined by immunoblotting (a, right). left, Data are shown as mean ± 11s.d., n = 3 independent transfections of hepatocyte cultures from the same mouse. Two independent experiments yielded similar results. b Hepatocytes were treated as described in a & mRNA expression of a selection of known ChREBP target genes visualized in a heatmap. c Primary hepatocytes were depleted of RetSat using two siRNA’s targeting different sites of the RetSat transcript for 48 h, & expression of the indicated genes analyzed by qPCR. Data are shown as mean ± s.d., n = 6 independent transfections of hepatocyte cultures from two different mice; *P < 0.05 between siControl und siRetSat by one-way ANOVA with Bonferroni post test. An independent experiment yielded similar results. d Hepatocytes treated with Control or RetSat siRNA were transfected with a ChoRE-Luc reporter, exposed to low & high glucose concentrations as indicated, & analyzed for luciferase activity. e Hepatocytes treated with Control or RetSat siRNA were exposed to low & high glucose concentrations as indicated, & mRNA expression determined by qPCR. In d, e, data are shown as mean ± s.d., n = 6 independent transfections of hepatocyte cultures from two mice; two-way ANOVA with Bonferroni post test revealed significances between low & high glucose concentrations (#P < 0.05) & between siControl & siRetSat (*P < 0.05). An independent experiment yielded similar results Image collected & cropped by CiteAb from the following publication (//www.nature.com/articles/s41467-017-00430-w), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: CHREBP Antibody - BSA Free [NB400-135] - LXR alpha & ChREBP alpha interact via key activation domains. (A). Top panel: Schematic representation of the ChREBP alpha full-length (FL), ChREBP beta & the low glucose inhibitory domain (LID) protein. Bottom panel: CoIP of LXR alpha & ChREBP alpha , ChREBP beta or LID, expressed in COS-1 cells cultured in 25 mM glucose. The ChREBP expression plasmids were transfected with a DNA ratio of ChREBP alpha :ChREBP beta :LID = 1:6:1, to obtain comparable protein levels. Lysates were immunoprecipitated with ChREBP, FLAG (for LID) or LXR alpha antibodies & input & immunoprecipitated proteins immunoblotted with the same antibodies (n = 3). One representative western blot is shown. LID, low-glucose inhibitory domain; GRACE, glucose-response activation conserved element; bHLH, basic helix-loop-helix domain: ZIP, leucine zipper. (B). Top panel: Schematic representation of the LXR alpha FL & truncations. Bottom panel: CoIP of ChREBP alpha & LXR alpha FL or truncations expressed in COS-1 cells cultured in 25 mM glucose. Lysates were immunoprecipitated with ChREBP antibody (n = 3). Input & immunoprecipitated proteins were immunoblotted with ChREBP or FLAG (for LXR alpha FL & truncations) antibodies. One representative western blot is shown. NTD, N-terminal domain; DBD, DNA-binding domain; LBD, ligand-binding domain. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/32414201), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: CHREBP Antibody - BSA Free [NB400-135] - FXR inhibits glucose-induced proglucagon expression(a) Proglucagon qPCR on cDNA from GLUTag cells starved for 12h with lactate (10 mmol L−1) & then incubated for 24h in lactate (10 mmol L−1), glucose (5.6 mmol L−1) or 2-deoxyglucose (5.6 mmol L−1) media containing DMSO, GW4064 (5 μmol L−1) or CDCA (100 μmol L−1) (n=3; performed 3 times). Data are represented as mean +/− SD. Two-Way ANOVA analysis followed by Bonferronni’s posthoc test. ***P≤0.001: effect of GW4064 & CDCA on proglucagon mRNA levels in each medium conditions. §§§P≤0.001: effect of glucose on proglucagon mRNA levels in DMSO, GW4064 & CDCA conditions. (b) Chrebp qPCR on cDNA from FACS-sorted proglucagon-negative & proglucagon-positive cells from the ileum (ileum L−; ileum L+) & colon (colon L−; colon L+) of GLU-VENUS mice (lower panel; n=3) & ChREBP protein expression from cytoplasm & nucleus extract from GLUTag cells (upper panel; performed 3 times). Data are represented as mean +/− SD. Student t-test. *P≤0.05 & **P≤0.01 (c) ChREBP & FXR western-blots after FXR immunoprecipitation on lysates from cytoplasm & nucleus of GLUTag cells treated or not with GW4064 (5 μmol L-1) in presence or not of glucose (5.6 mmol L−1) (performed 2 times). (d) Proglucagon qPCR on cDNA from GLUTag cells electroporated with a siCtrl or siChrebp, starved for 12h with lactate (10 mmol L−1) & then incubated for 24h in lactate 10 mmol L−1 (Glc −) or glucose 5.6 mmol L−1 (Glc +) media supplemented with DMSO or GW4064 (5 μmol L−1) (n=3; performed 3 times). Data are represented as mean +/− SD. Two-Way ANOVA analysis followed by Bonferronni’s posthoc test. *P≤0.05 & **P≤0.01: effect of treatments on each transfection condition. §§§P≤0.001: effect of siChrebp in each treatment condition. Image collected & cropped by CiteAb from the following publication (//www.nature.com/articles/ncomms8629), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: CHREBP Antibody - BSA Free [NB400-135] - Phf2 expression is increased in the liver of obese patients with benign hepatic steatosis & positively correlates with insulin sensitivity. Human liver biopsies from lean subjects with no fatty liver (NoFL) or obese patients with simple steatosis or NASH were obtained from the ABOS cohort. a Representative Western blot analysis of Phf2, ChREBP, SCD1, Nrf2, Gpx4, & alpha -SMA expression (n = 10 per group). b ChIP experiments for H3K9me2 levels & for the recruitment of ChREBP & the RNA polII at the SCD1 & Nrf2 promoter (n = 10 per group). c MUFA/SFA ratio reflecting SCD1 activity (n = 10 per group). d Expression of Nrf2 & Nrf2-regulated genes (n = 10 per group). e Levels of carbonylated proteins (n = 10 per group). f Expression of coll-Ia1, alpha -SMA, & TIMP-1 (n = 10 per group). All error bars represent mean ± SEM. Statistical analyses were made using Anova, followed by Bonferonni’s test. *Obese with steatosis compared to lean with noFL; P < 0.01. **Obese with steatosis compared to obese with NASH; P < 0.05 Image collected & cropped by CiteAb from the following publication (//www.nature.com/articles/s41467-018-04361-y), 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

Sizes:

Sample Size Available

Sizes: Sample Size Available

Conjugate:

Unconjugated

Available Conjugates:

Validated by:

Validated by:

Conjugate	Catalog #	Availability	Size	Price
Alexa Fluor 350	NB400-135AF350
Alexa Fluor 405	NB400-135AF405
Alexa Fluor 488	NB400-135AF488
Alexa Fluor 532	NB400-135AF532
Alexa Fluor 594	NB400-135AF594
Alexa Fluor 647	NB400-135AF647
Alexa Fluor 700	NB400-135AF700
Alexa Fluor 750	NB400-135AF750
Allophycocyanin	NB400-135APC
Biotin	NB400-135B
CoraFluor 1	NB400-135CL1
DyLight 350	NB400-135UV
DyLight 405	NB400-135V
DyLight 488	NB400-135G
DyLight 550	NB400-135R
DyLight 594	NB400-135DL594
DyLight 650	NB400-135C
DyLight 680	NB400-135FR
DyLight 755	NB400-135IR
FITC	NB400-135F
HRP	NB400-135H
Janelia Fluor 525	NB400-135JF525
Janelia Fluor 549	NB400-135JF549
Janelia Fluor 646	NB400-135JF646
Janelia Fluor 669	NB400-135JF669
PE	NB400-135PE
PerCP	NB400-135PCP
mFluor Violet 450 SE	NB400-135MFV450
mFluor Violet 500 SE	NB400-135MFV500
mFluor Violet 610 SE	NB400-135MFV610

Available Formulations

Formulation	Catalog #	Availability	Price
BSA Free	NB400-135SS

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NB100-56875

GAPDH Antibody - BSA Free

(5 Reviews)

(131 Publications)

0.1 mg

NB100-56875

$Western Blot: GAPDH Antibody [NB100-56875] - Analysis of GAPDH using this antibody at 1:500 in nuclear and cytoplasmic fractions made from Drosophila head extracts. Data courtesy of Dr. Jerry Lin, University of Wisconsin-Madison.$

Western Blot: GAPDH Antibody [NB100-56875] - Analysis using HeLa cells. Theoretical molecular weight: 36 kDa.

$Western Blot: GAPDH Antibody [NB100-56875] - Vps13 co-fractionates with Rab7 and Rab5. Western blot analysis of control fly head samples fractionated into a cytosolic and membrane fraction from postnuclear supernatant (PNS). EGFR was used as a membrane marker and GAPDH as a cytosolic marker. Image collected and cropped by CiteAb from the following publication (//dx.plos.org/10.1371/journal.pone.0170106), licensed under a CC-BY license.$

Western Blot: GAPDH Antibody [NB100-56875] - Particle-induced Changes in Apoptosis are Restored by Firoin. Peripheral blood neutrophils from healthy donors (n57), 2 h pre-treated with indicated amounts of firoin (F) or 1 mM ectoine (E) before CNP exposition (33 mg/ml). : 6 h post CNP-treatment the anti-apoptotic Mcl-1 expression was measured by Western blot analysis. GAPDH was used as a loading control. Two representative blots from different individuals are shown and irrelevant lanes were removed. Image collected and cropped by CiteAb from the following publication (//dx.plos.org/10.1371/journal.pone.0111485), licensed under a CC-BY license.

Simple Western: GAPDH Antibody [NB100-56875] - Lane view shows a specific band for GAPDH in 0.5 mg/ml of HeLa lysate. This experiment was performed under reducing A246conditions using the 12-230 kDa separation system. Note: band observed higher than predicted 36 kDa molecular weight.

$Western Blot: GAPDH Antibody [NB100-56875] - Vps13 co-fractionates with Rab7 & Rab5.(A) Western blot analysis of control fly head samples fractionated into a cytosolic & membrane fraction from postnuclear supernatant (PNS). EGFR was used as a membrane marker & GAPDH as a cytosolic marker. (B) Membrane fractions from control fly heads treated with 1 M KCl, Na2CO3 pH 11 or 6 M urea were centrifuged to separate the soluble & insoluble (membrane containing) fractions. The level of Vps13 was determined in these fractions. Markers for peripheral membrane proteins (GM130), integral membrane proteins (EGFR) & the cytosolic proteins (GAPDH) were used. The “Vps13 lysate” lane contains a lysate derived from Vps13 homozygous mutant fly heads, as expected no Vps13 is detected, demonstrating the specificity of the antibody against Vps13. (C) Membranes from control fly heads were fractionated on a sucrose gradient. Western blot analysis was performed to analyze the distribution of Vps13 in relation to markers associated with membranes of various organelles: Rab7 (late endosomes), Rab5 (early endosomes), GM130 (golgi), Lamp1 (lysosomes) & ATP5A (mitochondria). (D) Immunoisolation of membranes from fraction 14 of the sucrose gradient using Vps13 NT, Rab7 & Rab5 antibodies. (E) Quantification of the sucrose gradient fractionation of Fig 2C. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/28107480), licensed under a CC-BY license. Not internally tested by Novus Biologicals.$

$Western Blot: GAPDH Antibody [NB100-56875] - Overexpression of HsVps13A rescues phenotypes of Vps13 mutants.(A) Samples from fly heads of Actin-GAL4 / + (as a control) & Actin-GAL4 / UAS-HsVps13A (HsVps13A expressing) flies were separated into a membrane & cytosol fraction & analyzed by Western blot for HsVps13A levels. EGFR & GAPDH used as controls for membrane & cytosolic proteins, respectively. (B) Eclosion rate of Vps13 mutant flies a Actin-GAL4/+ (control) or Actin-GAL4/UAS-HsVp13A (HsVps13A expressing) background at 25°C. (C) Ubiquitylated proteins from samples of 1 day old fly head extracts of Vps13/CyO; Actin-GAL4/+ (as a control), Vps13/ Vps13; Actin-GAL4/+ (representing homozygous mutants) & Vps13/ Vps13; Actin-GAL4/UAS-HsVps13A (representing homozygous mutants expressing human VPS13A). (D) Representative picture of ubiquitylated protein staining of the third instar larval ventral nerve cord of Vps13/CyO; Actin-GAL4/+ (as a control), Vps13/ Vps13; Actin-GAL4/+ & Vps13/ Vps13; Actin-GAL4/UAS-HsVps13A. Arrows indicate accumulations of ubiquitylated positive structures. The scale bar indicates 50 μm & 12,5 μm in the enlargement. (E) Quantification of the number of puncta in third instar larval ventral nerve cord of the experiment presented in Fig 6D. (F) Life span curve of Vps13/ Vps13; Actin-GAL4/+ & Vps13/ Vps13; Actin-GAL4/UAS-HsVps13A. All quantifications show the mean & SEM of at least three independent experiments per condition. For statistical analysis a two-tailed students T-test was used in combination with a Welch’s correction if necessary. P<0.05 is *, P<0.01 is ** & P<0.001 is ***. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/28107480), licensed under a CC-BY license. Not internally tested by Novus Biologicals.$

Western Blot: GAPDH Antibody [NB100-56875] - No dystrophin expression was detected in cardiac & skeletal muscles of Dmdmdx rats.(A) Male 7 month-old rats of line 61, wild-type littermate controls (WT) & Dmdmdx were sacrificed & biopsies from tibialis cranialis muscles (TC) & hearts (H) were harvested. Western-blot of total proteins (50 µg) was incubated with NCL-DYS2 & Manex1011C monoclonal antibodies (C-terminal & exons 10/11 epitopes, respectively). This revealed undetectable levels of the 427 kDa dystrophin band in line 61 Dmdmdx rats. Muscle from a GRMD dog (GD) was used as negative control & samples from WT rats were used as positive controls. Staining with an anti-GAPDH polyclonal antibody validated equal protein loadings. (B–E) Heart & biceps femoris muscles from the same wild-type (B & C) & Dmdmdx rats (D & E) were assessed for dystrophin expression using immunohistochemistry with Mandys110 monoclonal antibody (against exons 38–39 epitope). Compared to the subsarcolemmal expression of dystrophin in wild-type muscles, no dystrophin was detected in Dmdmdx rats except for the presence in skeletal muscle of only rare scattered revertant positive fibers (arrowheads). Immunolabelling of dystrophin (B–E) Bar = 100 µm. Image collected & cropped by CiteAb from the following publication (//dx.plos.org/10.1371/journal.pone.0110371), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: GAPDH Antibody [NB100-56875] - 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.

$Western Blot: GAPDH Antibody [NB100-56875] - Vps13 co-fractionates with Rab7 & Rab5.(A) Western blot analysis of control fly head samples fractionated into a cytosolic & membrane fraction from postnuclear supernatant (PNS). EGFR was used as a membrane marker & GAPDH as a cytosolic marker. (B) Membrane fractions from control fly heads treated with 1 M KCl, Na2CO3 pH 11 or 6 M urea were centrifuged to separate the soluble & insoluble (membrane containing) fractions. The level of Vps13 was determined in these fractions. Markers for peripheral membrane proteins (GM130), integral membrane proteins (EGFR) & the cytosolic proteins (GAPDH) were used. The “Vps13 lysate” lane contains a lysate derived from Vps13 homozygous mutant fly heads, as expected no Vps13 is detected, demonstrating the specificity of the antibody against Vps13. (C) Membranes from control fly heads were fractionated on a sucrose gradient. Western blot analysis was performed to analyze the distribution of Vps13 in relation to markers associated with membranes of various organelles: Rab7 (late endosomes), Rab5 (early endosomes), GM130 (golgi), Lamp1 (lysosomes) & ATP5A (mitochondria). (D) Immunoisolation of membranes from fraction 14 of the sucrose gradient using Vps13 NT, Rab7 & Rab5 antibodies. (E) Quantification of the sucrose gradient fractionation of Fig 2C. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/28107480), licensed under a CC-BY license. Not internally tested by Novus Biologicals.$

Simple Western: GAPDH Antibody [NB100-56875] - Analysis of non-canonical inflammasome pathway.A LDH cytotoxicity assay in the presence of LPS or SCGB3A2 alone, or the two together (SCGB3A2 + LPS). B LDH cytotoxicity assay in the presence of various amount of nigericin. Average ± SD from more than three independent experiments. *P < 0.01, **P < 0.0001 by Tukey’s multiple comparison. C Morphology of cells cultured in the presence of LPS or SCGB3A2 alone, SCGB3A2 + LPS, or nigericin for 3 h. For nigericin-treated group, cells were primed with LPS before addition of nigericin. Black arrow indicates ballooned cells, characteristic feature of pyroptosis. D Western blotting for the cleaved forms of CASP1 (p20), CASP4 (p20), & GSDMD (N-terminal). S: SCGB3A2, N: nigericin. Experiments were repeated more than twice & same results were obtained. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/33452234), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Reactivity:

Hu, Mu, Rt, Po, Ca, Dr, Fe, Ha, Pm, Ma

Species Glossary

Reactivity: Hu, Mu, Rt, Po, Ca, Dr, Fe, Ha, Pm, Ma

Applications:

, , , ,

Applications: , , , ,

Host:

Rabbit Polyclonal

Host: Rabbit Polyclonal

Alt Catalog#

IMG-5143A

Alt Catalog# IMG-5143A

Sizes:

Sample Size Available

Sizes: Sample Size Available

Conjugate:

Unconjugated

Available Formulations

Formulation	Catalog #	Availability	Price
BSA Free	NB100-56875SS

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NB600-502

GAPDH Antibody (6C5cc) - BSA Free

(3 Reviews)

(87 Publications)

0.2 mg

NB600-502

Western Blot: GAPDH Antibody (6C5) [NB600-502] - Western blot of FGF23 in the kidney. GAPDH antibody (6C5) served as an internal control. Each value represents the mean +/- SEM. Citation: Sugiura H, Matsushita A, Futaya M, Teraoka A, Akiyama K-i, Usui N, et al. (2018) Fibroblast growth factor 23 is upregulated in the kidney in a chronic kidney disease rat model. PLoS ONE 13(3): e0191706. //doi.org/10.1371/journal.pone.0191706

Simple Western: GAPDH Antibody (6C5) [NB600-502] - Simple Western lane view shows a specific band for GAPDH in 0.5 mg/ml of HeLa lysate. This experiment was performed under reducing conditions using the 12-230 kDa separation system. Note: band observed higher than predicted 36 kDa molecular weight.

Simple Western: GAPDH Antibody (6C5) [NB600-502] - Anaylsis in rat brain and spinal cord. This image includes the GAPDH at the predicted kDa as well as a glucocorticoid receptor antibody (peak 102). Verified customer review.

Western Blot: GAPDH Antibody (6C5cc) [NB600-502] - Western blot analysis for whole cell & nuclear signal transduction proteins. (A) Phosphorylated FAK (Y397) was significantly decreased at 24 h & significantly increased at 48 h as compared to sham. (B) Nuclear localization of corresponding signal transduction molecules, p38, & p65, were decreased at 24 h & increased at 48 h as compared to sham. *p 0.05.Immortalized Brca1F/C61G MEFs were infected with retroviruses expressing the indicated shRNAs and/or Cre recombinase, followed by selection with puromycin for 72 h. The frequency of end-to-end chromosome-type fusions was analysed as in (A).MEFs of the indicated genotypes were infected with retroviruses expressing TRF2 and/or CtIP shRNAs, followed by selection with puromycin for 72 h. Cell extracts were prepared 48 h later & analysed by Western blotting as indicated. GAPDH was used as a loading control. *non-specific band. Cells treated as in (C) & (E) were arrested in mitosis with colcemid, & mitotic chromosomes isolated 48 h later were fixed & stained with a Cy3-conjugated (CCCTAA)3-PNA probe (D, F). The frequency of end-to-end chromosome-type fusions is represented as a percentage of fusions observed after TRF2 depletion. Error bars represent SD of two independent experiments. P-values were calculated using an unpaired two-tailed t-test. *P ≤ 0.05. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/25582120), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Reactivity:

Hu, Mu, Rt, Po, Am, Ca, ChHa, Fe, Fi, Rb, Bv(-), Gt(-)

Species Glossary

Reactivity: Hu, Mu, Rt, Po, Am, Ca, ChHa, Fe, Fi, Rb, Bv(-), Gt(-)

Applications:

, , , , ,

Applications: , , , , ,

Host:

Mouse Monoclonal

Host: Mouse Monoclonal

Conjugate:

Unconjugated

Available Conjugates:

Conjugate	Catalog #	Availability	Size	Price
Alexa Fluor 350	NB600-502AF350-0.2ml
Alexa Fluor 405	NB600-502AF405-0.2ml
Alexa Fluor 488	NB600-502AF488-0.2ml
Alexa Fluor 532	NB600-502AF532-0.2ml
Alexa Fluor 594	NB600-502AF594-0.2ml
Alexa Fluor 647	NB600-502AF647-0.2ml
Alexa Fluor 700	NB600-502AF700-0.2ml
Alexa Fluor 750	NB600-502AF750-0.2ml
Biotin	NB600-502B-0.2ml
CoraFluor 1	NB600-502CL1
DyLight 350	NB600-502UV-0.2ml
DyLight 405	NB600-502V-0.2ml
DyLight 488	NB600-502G-0.2ml
DyLight 550	NB600-502R-0.2ml
DyLight 594	NB600-502DL594-0.2ml
DyLight 650	NB600-502C-0.2ml
DyLight 680	NB600-502FR-0.2ml
DyLight 755	NB600-502IR-0.2ml
FITC	NB600-502F-0.2ml
HRP	NB600-502H-0.2ml
Janelia Fluor 525	NB600-502JF525
Janelia Fluor 549	NB600-502JF549-0.2ml
Janelia Fluor 646	NB600-502JF646-0.2ml
Janelia Fluor 669	NB600-502JF669
mFluor Violet 450 SE	NB600-502MFV450
mFluor Violet 500 SE	NB600-502MFV500
mFluor Violet 610 SE	NB600-502MFV610

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NB110-39113

Glut1 Antibody - BSA Free

(7 Reviews)

(70 Publications)

0.1 ml

NB110-39113

Immunohistochemistry-Paraffin: Glut1 Antibody [NB110-39113] - Immunohistochemical analysis of FFPE tissue section of human placenta using 1:200 dilution of Glut1 antibody. The staining was developed using HRP-DAB detection method and the sections were further counterstained with hematoxylin. This antibody generated a specific strong membrane cytoplasmic staining of Glut1 primarily in the syncytiotrophoblast layers of various villi and in the red blood cells (RBCs). Cytotrophoblasts showed a very weak expression of this protein.

Flow Cytometry: Glut1 Antibody [NB110-39113] - An intracellular stain was performed on HepG2 with NB110-39113 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 5 ug/mL for 30 minutes at room temperature, followed by Rabbit IgG (H+L) Cross-Adsorbed Secondary Antibody.

Immunocytochemistry/Immunofluorescence: Glut1 Antibody [NB110-39113] - HepG2 cells were fixed for 10 minutes using 10% formalin and then permeabilized for 5 minutes using 1X TBS + 0.5% Triton X-100. The cells were incubated with anti-GLUT1 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

Western Blot: Glut1 Antibody [NB110-39113] - Analysis of HeLa lysates using NB110-39113. Image courtesy of Gregg Semenza (PMID: 21620138).

Western Blot: Glut1 Antibody [NB110-39113] - Glut1 in human brain lysate (55 kDa). Antibody at 1:500. Western blot image submitted by a verified customer review.

<b>Biological Strategies Validation. </b>Flow Cytometry: Glut1 Antibody [NB110-39113] - Flow cytometry analysis using the PE conjugate of NB110-39113. Staining of Glut 1 expression on CD4+ T cells stimulated with anti-CD3/CD28 beads and insulin (1ug/mL) for 5 days in culture media with additional glucose provided. FMO control (red) and isotype control (blue, NBP2-24983) were compared to CD4+ T cells (orange), and this PE conjugated Glut 1 antibody positively stained CD4+ lymphocytes isolated from Mouse. Flow cytometry image submitted by a verified customer review.

Immunocytochemistry/ Immunofluorescence: Glut1 Antibody - BSA Free [NB110-39113] - LAIR-1 inhibits Glut1-related glucose uptake in OS cells. a Heatmap showing the levels of differentially expressed mRNAs. b Top 20 KEGG pathway annotation categories for target gene functions of predicted mRNAs. c Selected significantly differentially expressed mRNA-related to EMT in RNA-seq data between two groups, ***P < 0.001. d qPCR validation of differentially expressed EMT-related genes in LV-NC & LV-LAIR-1-overexpressing OS cells, **P < 0.01. e Glut1 expression analyzed by western blotting. f Immunofluorescence staining of Glut1 in the LV-LAIR-1-overexpressing OS cells. Scale bar = 50 μm. Data were obtained from at least two independent experiments. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/32563267), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: Glut1 Antibody - BSA Free [NB110-39113] - LAIR-1 inhibits Glut1-related glucose uptake in OS cells. a Heatmap showing the levels of differentially expressed mRNAs. b Top 20 KEGG pathway annotation categories for target gene functions of predicted mRNAs. c Selected significantly differentially expressed mRNA-related to EMT in RNA-seq data between two groups, ***P < 0.001. d qPCR validation of differentially expressed EMT-related genes in LV-NC & LV-LAIR-1-overexpressing OS cells, **P < 0.01. e Glut1 expression analyzed by western blotting. f Immunofluorescence staining of Glut1 in the LV-LAIR-1-overexpressing OS cells. Scale bar = 50 μm. Data were obtained from at least two independent experiments. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/32563267), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Simple Western: Glut1 Antibody - BSA Free [NB110-39113] - Protein changes in ONHAs corroborate bioenergetics data. (A) Glucose transporter-1 protein levels in Stretched ONH astrocytes are significantly higher than Control (*p = 0.0225, n = 7 Control, n = 8 Stretch). Retinal lysate from a 2 month-old mouse was used as a positive control for each protein analyzed, while negative control was the signal obtained when no primary antibody was included in the capillary. (B) Lactate dehydrogenase-A, the astrocyte-specific isoform of the enzyme that catalyzes the interconversion of pyruvate & lactate, has equivalent protein levels in Control & Stretch ONH astrocytes. (C) Glucose-6-phosphate dehydrogenase, the enzyme that shunts glucose into the pentose phosphate pathway, is no different in Control & Stretch ONH astrocytes. (D) Glutamine synthetase, the enzyme that synthesizes glutamine from glutamate, is no different in Control & Stretch ONH astrocytes. (E) The monomeric form of glutamate-aspartate transporter (GLAST) has significantly higher protein levels in the Stretch as compared to the Control ONH astrocytes (p = 0.020; n = 4 Control, n = 5 Stretch). (F) GLAST dimer protein levels are no different in Control & Stretch ONH astrocytes. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/35992925), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Reactivity:

Hu, Mu, Rt, Rb, Bv, Pm

Species Glossary

Reactivity: Hu, Mu, Rt, Rb, Bv, 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	NB110-39113AF350
Alexa Fluor 405	NB110-39113AF405
Alexa Fluor 488	NB110-39113AF488
Alexa Fluor 532	NB110-39113AF532
Alexa Fluor 594	NB110-39113AF594
Alexa Fluor 647	NB110-39113AF647
Alexa Fluor 700	NB110-39113AF700
Alexa Fluor 750	NB110-39113AF750
Allophycocyanin	NB110-39113APC
Allophycocyanin/Cy7	NB110-39113APCCY7
Biotin	NB110-39113B
CoraFluor 1	NB110-39113CL1
DyLight 350	NB110-39113UV
DyLight 405	NB110-39113V
DyLight 488	NB110-39113G
DyLight 550	NB110-39113R
DyLight 594	NB110-39113DL594
DyLight 650	NB110-39113C
DyLight 680	NB110-39113FR
DyLight 755	NB110-39113IR
FITC	NB110-39113F
HRP	NB110-39113H
Janelia Fluor 525	NB110-39113JF525
Janelia Fluor 549	NB110-39113JF549
Janelia Fluor 646	NB110-39113JF646
Janelia Fluor 669	NB110-39113JF669
PE	NB110-39113PE
PE/Atto594	NB110-39113PEATT594
PE/Cy5.5	NB110-39113PECY55
PE/Cy7	NB110-39113PECY7
PerCP	NB110-39113PCP
mFluor Violet 450 SE	NB110-39113MFV450
mFluor Violet 500 SE	NB110-39113MFV500
mFluor Violet 610 SE	NB110-39113MFV610

Available Formulations

Formulation	Catalog #	Availability	Price
BSA Free	NB110-39113SS

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NB300-320

GAPDH Antibody

(2 Reviews)

(69 Publications)

0.1 mg

NB300-320

Immunohistochemistry-Paraffin: GAPDH Antibody [NB300-320] - Staining of paraffin embedded Human Pancreas. Antibody at 2.5 ug/mL. Steamed antigen retrieval with citrate buffer pH 6, AP-staining.

Western Blot: GAPDH Antibody [NB300-320] - stai Mutants Have Reduced Levels of alpha-Tubulin, Acetylated alpha-Tubulin, and Kinesin Heavy Chain Protein. Representative western blots of total protein extracted from stai mutant third instar larvae. Heterozygous stai/+ mutant larvae exhibit mild reductions in the levels of alpha-tubulin and acetylated alpha-tubulin compared with wild type larvae. Homozygous stai mutant larvae have dramatic reductions in the levels of alpha-tubulin, acetylated alpha-tubulin and the heavy chain subunit of the microtubule motor protein kinesin compared to wildtype. Df(2L) BSC239 represents a second chromosomal deficiency that excludes the stai gene. GAPDH is used as a loading control. Image collected and cropped by CiteAb from the following publication (//dx.plos.org/10.1371/journal.pone.0068324), licensed under a CC-BY license.

Western Blot: GAPDH Antibody [NB300-320] - Staining of HEK293 (A) and HeLa (B) cell lysate (35 ug protein in RIPA buffer). Antibody at 0.001 ug/mL. Detected by chemiluminescence. Approx 36 kDa band observed in lysates of cell line HEK293 and approx. 35 kDa in HeLa cell lysates.(calculated MW of 36.1 kDa according to Human NP_002037.2).

Immunocytochemistry/Immunofluorescence: GAPDH Antibody [NB300-320] - Immunofluorescence analysis of paraformaldehyde fixed A549 cells, permeabilized with 0.15% Triton. Primary incubation 1hr (10 ug/mL) followed by Alexa Fluor 488 secondary antibody (2 ug/mL), showing cytoplasmic and vesicle staining. The nuclear stain is DAPI (blue). Negative control: Unimmunized goat IgG (10 ug/mL) followed by Alexa Fluor 488 secondary antibody (2 ug/mL). Strong expression of the protein seen in the cytoplasm and vesicles of A549 cells.

Immunohistochemistry-Paraffin: GAPDH Antibody [NB300-320] - Upregulation of GAPDH and Tom20 in C6 gliomas. A small glioma labeled with antibodies against GAPDH. The brightness and contrast have been increased. Image collected and cropped by CiteAb from the following publication (//www.biomedcentral.com/1756-0500/8/207), licensed under a CC-BY license.

Upregulation of GAPDH & Tom20 in C6 gliomas. a A section of rat brain stained with hematoxilin & eosin to show a glioma produced by implantation of C6 cells in the right caudate nucleus. In this case, cells also grew in the region of the syringe needle track through the cortex. (b–d). A small glioma labeled by bisbenzamide (b) & with antibodies against Tom20 (c) & GAPDH (d). The brightness & contrast have been increased. e Illustration of a strip perpendicular to the rim of a glioma (labeled with bisbenzamide) & along which intensity profiles were measured. f, g Tom20 & GAPDH fluorescence along such a strip (barely visible without enhancement). The graphs show the raw intensity values given by ImageJ. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/26032618), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: GAPDH Antibody [NB300-320] - PAR2 causes contraction of smooth muscle cells from human prostate. (A & B) Decrease in diameter of collagen hydrogels after PAR2 activation with SLIGKV (80 µM). (C) Representative western blot & (D) densitometry showing time dependent increase in level of phosphorylated MLC20 in PSMC after PAR2 is activated. Data represent mean ± SEM of at least three independent experiments. Diameter of collagen hydrogels were measured in ImageJ (version 1.50i) & significance analyzed in Prism (version 7.04) with one‐way ANOVA followed by Tukey's multiple comparison test. *P < 0.05, **P < 0.01 Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31198907), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Immunocytochemistry/ Immunofluorescence: GAPDH Antibody [NB300-320] - Upregulation of GAPDH & Tom20 in C6 gliomas. a A section of rat brain stained with hematoxilin & eosin to show a glioma produced by implantation of C6 cells in the right caudate nucleus. In this case, cells also grew in the region of the syringe needle track through the cortex. (b–d). A small glioma labeled by bisbenzamide (b) & with antibodies against Tom20 (c) & GAPDH (d). The brightness & contrast have been increased. e Illustration of a strip perpendicular to the rim of a glioma (labeled with bisbenzamide) & along which intensity profiles were measured. f, g Tom20 & GAPDH fluorescence along such a strip (barely visible without enhancement). The graphs show the raw intensity values given by ImageJ. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/26032618), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: GAPDH Antibody [NB300-320] - CDC20B was the protein effector regulated by hsa-miR-633. (a) CDC20B level was up-regulated after ox-LDL treatment revealed by Western blotting. (b) CDC20B level was decreased after the treatment of hsa-miR-633 mimics revealed by Western blotting. (c) CDC20B level was increased after the treatment of hsa-miR-633 inhibitor revealed by Western blotting. (d) The luciferase reporter plasmids were constructed as illustrated. (e) Relative luciferase activities after co-transfection CDC20B WT & hsa-miR-633/Control, or CDC20B Mut & hsa-miR-633/Control were measured. (f) The expression levels of two proliferation markers, Ki67 & PCNA after the treatment of si-CDC20B were measured using Western blotting. (g) Colony formation assay was conducted to examine the proliferation abilityafter the treatment of si-CDC20B. (h) Transwell migration & invasion assays were conducted to examine the migration & invasion abilities of VSMCs after the treatment of si-CDC20B. (i) Quantification results of (g). (j) Quantification results of (h). *P < 0.05, **P < 0.01, ***P < 0.001. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/35212610), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Simple Western: GAPDH Antibody [NB300-320] - MiR-34a affects stroke outcomes via interacting with cytochrome c. (A) WES system image showing CYC, VDAC & GAPDH expression from hemispheres of WT & miR-34a−/− mice at 6 h post-stroke. (B) Relative CYC expression normalized to GAPDH from the data generated by the WES system. CYC level is significantly decreased in ischemic hemispheres of WT mice but no significant changes in miR-34a−/− mice between contralateral hemispheres (Control) & ischemic hemispheres (Ischemia). N = 5 per group, **p < 0.01, One-way ANOVA followed by post hoc Tuckey’s test was used for data analysis. Data are expressed as mean ± S.D. (C) Relative VDAC expression normalized to GAPDH from the data generated by the WES system. VDAC was not significantly altered in WT mice nor miR-34a−/− mice. (D) Multiplexed WES system image showing CYC & GAPDH expression from purified pCECs of WT & miR-34a−/− mice (n = 10 per group, pooled cell samples) at 6 h post-stroke. (E) Relative CYC expression by normalization to GAPDH. A 2.8 fold decrease of CYC level was observed in WT mice but no changes were observed in miR-34a−/− mice between contralateral hemispheres & ischemic hemispheres. (F) A CYC reporter was coexpressed with a miR-34a plasmid, a miR-34a mimic, a miR-34c mimic, or a plasmid control in cultured cerebral vascular endothelial cells for 24 hours. Relative firefly luciferase activity was evaluated & normalized to renilla luciferase activity. Relative firefly luciferase activity was reduced by miR-34a plasmid & miR-34a mimic. The experiment was repeated 3 times & triplicates were used for each analysis. Data represents the mean ± S.D. *p < 0.05. One-way ANOVA followed by post-hoc Tuckey’s test was used for analysis. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/32094435), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: GAPDH Antibody [NB300-320] - Hsa-miR-633 inhibitor could reverse the si-circ_0008896 phenotypes. (a) CCK8 assay was conducted to measure cell viability after up-regulation of hsa-miR-633. (b) The expression levels of two proliferation markers, Ki67 & PCNA after up-regulation of hsa-miR-633 were measured using Western blotting. (c) CCK8 assay was conducted to measure cell viability after the treatment of si-circ0008896, hsa-miR-633 inhibitor & si-circ0008896+ hsa-miR-633 inhibitor. (d) The expression levels of two proliferation markers, Ki67 & PCNA after the treatment of si-circ0008896, hsa-miR-633 inhibitor & si-circ0008896+ hsa-miR-633 inhibitor were measured using Western blotting. (e) Colony formation assay was conducted to examine proliferation ability number of colonies after the treatment of si-circ0008896, hsa-miR-633 inhibitor & si-circ0008896+ hsa-miR-633 inhibitor. (f) Quantification results of (e). (g) Transwell migration & invasion assays were conducted to examine the migration & invasion abilities of VSMCs after the treatment of si-circ0008896, hsa-miR-633 inhibitor & si-circ0008896+ hsa-miR-633 inhibitor. (h) Quantification results of (g). *P < 0.05, **P < 0.01, ***P < 0.001. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/35212610), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: GAPDH Antibody [NB300-320] - Down-regulation of hsa_circ_0008896 inhibited proliferation, migration & invasion in vitro. (a) The expression level of hsa_circ_0008896 after si-circ_0008896 transfection was detected using quantitative PCR. (b) CCK8 assay was conducted to measure cell viability after down-regulation of hsa_circ_0008896. (c) The expression levels of two proliferation markers, Ki67 & PCNA after down-regulation of hsa_circ_0008896 were detected using Western blotting. (d) Colony formation assay was conducted to examine proliferation ability after down-regulation of hsa_circ_0008896. (e) The quantification results of (d). (f) Transwell migration & invasion assays were conducted to examine the migration & invasion abilities of VSMCs after down-regulation of hsa_circ_0008896. (g) The quantification results of (f). *P < 0.05, **P < 0.01, ***P < 0.001. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/35212610), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Reactivity:

Hu, Mu, Rt, Ca, Dr, I, Po

Species Glossary

Reactivity: Hu, Mu, Rt, Ca, Dr, I, Po

Applications:

, , , , ,

Applications: , , , , ,

Host:

Goat Polyclonal

Host: Goat Polyclonal

Alt Catalog#

IMG-3073

Alt Catalog# IMG-3073

Conjugate:

Unconjugated

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NB110-40877

Perilipin-2/ADFP Antibody - BSA Free

(1 Review)

(65 Publications)

0.1 ml

NB110-40877

Formalin-fixed paraffin-embedded tissue sections of mouse intestine were probed for Perilipin-2/ADFP mRNA (ACD RNAScope Probe, catalog #577111; Fast Red chromogen, ACD catalog # 322750). Adjacent tissue section was processed for immunohistochemistry using Rabbit Polyclonal (Novus Biologicals catalog # NB110-40877) at 1:150 dilution 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 intestinal villi.

<b>Orthogonal Strategies Validation. </b>Simple Western lane view shows a specific band for ADFP in 0.5 mg/ml of HepG2 lysate. This experiment was performed under reducing conditions using the 12-230 kDa separation system.

<b>Biological Strategies Validation. </b>Oleic acid increasesI2 oxidation, glucose utilization and expression of genes involved in LCFA metabolism in U138 GBM cells. Cropped western blot images and quantitation of PLIN2 and GAPDH protein levels from cell lysates. Human hepatoma (VL17A) cell line was used as a positive control (+control). Full length blots are in Supplementary Fig. A1. N=3 independent experiments in triplicate. Image collected and cropped by Citeab from the following publication (Lipid accumulation and oxidation in glioblastoma multiforme. Sci Rep (2019)) licensed under a CC-BY license.

ADFP antibody was tested in mouse liver using DAB with hematoxylin counterstain.

NIH3T3 cells were fixed in 4% paraformaldehyde for 10 minutes and permeabilized in 0.05% Triton X-100 in PBS for 5 minutes. The cells were incubated with anti-Perilipin-2/ADFP Antibody NB110-40877 at 1 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.

Detection of murine ADFP in mouse liver lysate.

HepG2 cells were 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-Perilipin-2/ADFP at a 1:100 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.

HepG2 cells were fixed in 4% paraformaldehyde for 10 minutes and permeabilized in 0.05% Triton X-100 in PBS for 5 minutes. The cells were incubated with anti-Perilipin-2/ADFP Antibody NB110-40877 at 1 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.

Western Blot: Perilipin-2/ADFP Antibody - BSA Free [NB110-40877] - Western blot images (A) & quantifications (B–I) of muscle samples from WT & UCHL1 smKO mice for lipase ATGL (B), HSL (C), & MAGL (D), the fatty acid transport protein CD36 (E), the key lipid synthesis enzyme DGAT2 (F), perilipin 3 (G), perilipin 2 (H), & UCHL1 (I). n = 4-5 per group. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/35464088), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: Perilipin-2/ADFP Antibody - BSA Free [NB110-40877] - Western blot images (A) & quantifications (B–G) of cell lysates from C2C12 myotubes with control or UCHL1 siRNA knockdown for perilipin 2 (B), perilipin 5 (C), CD36 (D), HSL (E), MAGL (F), & SDHB (G). n = 4 per group. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/35464088), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Immunocytochemistry/ Immunofluorescence: Perilipin-2/ADFP Antibody - BSA Free [NB110-40877] - Lack of MT4-MMP in patrolling monocytes leads to the accumulation of Mafb+AIM+ macrophages in incipient atherosclerotic plaques. a Representative images of transverse sections of aortic sinus from Ldlr–/– mice transplanted with MT4-MMP+/+ (MT4+/+) or MT4-MMP–/– (MT4–/–) BM cells & fed a HFD for 1 week; sections were labeled for Mac3 (green), Mafb (red), & AIM (white), & with Hoechst (blue; nuclei); scale bar, 10 µm. b Number of Mac3+ cells (left), Mac3+Mafb+ cells (middle), & Mac3+Mafb+AIM+ cells (right) in the plaques of BM-transplanted Ldlr–/– mice fed a HFD for 1 week. c Representative images of transverse sections of aortic sinus from BM-transplanted Ldlr–/– mice fed a HFD for 1 week; sections were labeled for Mac3 (green), Mafb (red), & adipophilin (white), & with Hoechst (blue; nuclei); scale bar, 10 µm. d Relative % of adipophilin-positive & adipophilin-negative cells within the Mac3+Mafb+ population of BM-transplanted Ldlr–/– mice (1 week on HFD); n = 7 mice per genotype in two independent experiments. Data were tested by two-tailed Student’s t-test in b & by Fisher’s exact test in d. Results are expressed as mean ± SEM. *p < 0.05 Image collected & cropped by CiteAb from the following publication (//www.nature.com/articles/s41467-018-03351-4), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Perililpin-2/ADFP was detected in immersion fixed HepG2 human hepatocellular carcinoma cell line using Rabbit anti-Perililpin-2/ADFP Affinity Purified Polyclonal Antibody conjugated to Biotin (Catalog # NB110-40877B) at 5 µg/mL overnight at 4C. Cells were stained using Streptavidin conjugated to DyLight 550 (red) and counterstained with DAPI (blue). Cells were imaged using a 100X objective and digitally deconvolved.

Reactivity:

Hu, Mu, Rt, Bv

Species Glossary

Reactivity: Hu, Mu, Rt, Bv

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	NB110-40877AF350
Alexa Fluor 405	NB110-40877AF405
Alexa Fluor 488	NB110-40877AF488
Alexa Fluor 532	NB110-40877AF532
Alexa Fluor 594	NB110-40877AF594
Alexa Fluor 647	NB110-40877AF647
Alexa Fluor 700	NB110-40877AF700
Alexa Fluor 750	NB110-40877AF750
Allophycocyanin	NB110-40877APC
Biotin	NB110-40877B
CoraFluor 1	NB110-40877CL1
DyLight 350	NB110-40877UV
DyLight 405	NB110-40877V
DyLight 488	NB110-40877G
DyLight 550	NB110-40877R
DyLight 594	NB110-40877DL594
DyLight 650	NB110-40877C
DyLight 680	NB110-40877FR
DyLight 755	NB110-40877IR
FITC	NB110-40877F
HRP	NB110-40877H
Janelia Fluor 525	NB110-40877JF525
Janelia Fluor 549	NB110-40877JF549
Janelia Fluor 646	NB110-40877JF646
Janelia Fluor 669	NB110-40877JF669
PE	NB110-40877PE
PerCP	NB110-40877PCP
mFluor Violet 450 SE	NB110-40877MFV450
mFluor Violet 500 SE	NB110-40877MFV500
mFluor Violet 610 SE	NB110-40877MFV610

Available Formulations

Formulation	Catalog #	Availability	Price
BSA Free	NB110-40877SS

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NB110-93479

Pyruvate Dehydrogenase E1-alpha subunit [p Ser293] Antibody - BSA Free

(5 Reviews)

(61 Publications)

0.05 ml

NB110-93479

<b>Biological Strategies Validation. </b>Immunocytochemistry/Immunofluorescence: Pyruvate Dehydrogenase E1-alpha subunit [p Ser293] Antibody [NB110-93479] - Pyruvate Dehydrogenase E1-alpha subunit [p Ser293] antibody (1:250) was tested in HeLa cells with DyLight 488 (green). Nuclei and alpha-tubulin were counterstained with DAPI (blue) and DyLight 550 (red).

Western Blot: Pyruvate Dehydrogenase E1-alpha subunit [p Ser293] Antibody [NB110-93479] - Detection of PDHE1 alpha [S293] in an in vitro autophosphorylation of PDH complex in response to different stimulants: (-) none, H202-hydrogen peroxide, AR-anhydroretinol, Rol-retinol, RA-retinoic acid, PMA, Lipid-PKC lipid activator. Photo courtesy of Dr. Beatrice Hoyos, Memorial Sloan-Kettering Cancer Center.

Western Blot: Pyruvate Dehydrogenase E1-alpha subunit [p Ser293] Antibody [NB110-93479] - PDH activity and protein levels of PDK4 and p-PDH in hindlimb skeletal muscle. Samples were resolved by electrophoresis, transferred and probed by antibodies and representative immunoblots and normalization of pPDH are presented. The following comparisons were made: within a genotype, fed versus fasted; across genotypes, fed versus fed and fasted versus fasted. Bars that do not share a common symbol differ significantly (P < 0.05). Data presented as mean +/- SEM (n = 6). Image collected and cropped by CiteAb from the following publication (//dx.plos.org/10.1371/journal.pone.0124204), licensed under a CC-BY license.

Western Blot: Pyruvate Dehydrogenase E1-alpha subunit [p Ser293] Antibody - BSA Free [NB110-93479] - PDK4 expression during syncytialization of human placental trophoblasts. (A) Changes of the RPKM values for PDK family members in trophoblasts before (red column, 3 hours) & after (blue column, 48 hours) syncytialization. (B) Changes in PDK4 mRNA (black column, n = 4) & protein (white column, n = 4) abundance during syncytialization. (C) Changes in the phosphorylation of PDHE1 alpha during syncytialization n = 4. (D) Representative images showing intense staining of PDK4 (red) in the cytotrophoblast layer & weak staining of PDK4 in the syncytial layer of human chorionic villi at early gestation. The syncytial & cytotrophoblast layers were labeled with beta -hCG (green) & SPINT1 (green) respectively. Nuclei were counterstained with DAPI (blue). n = 3; *P < 0.05; **P < 0.01; ***P < 0.001 against 3 hours; n.s., not significant. Image collected & cropped by CiteAb from the following publication (//www.nature.com/articles/s41598-017-09163-8), 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

Sizes:

Sample Size Available

Sizes: Sample Size Available

Conjugate:

Unconjugated

Available Conjugates:

Validated by:

Validated by:

Conjugate	Catalog #	Availability	Size	Price
Alexa Fluor 405	NB110-93479AF405
Alexa Fluor 488	NB110-93479AF488
Alexa Fluor 647	NB110-93479AF647
Alexa Fluor 700	NB110-93479AF700
Biotin	NB110-93479B
DyLight 405	NB110-93479V
DyLight 488	NB110-93479G
DyLight 550	NB110-93479R
DyLight 650	NB110-93479C
FITC	NB110-93479F
HRP	NB110-93479H

Available Formulations

Formulation	Catalog #	Availability	Price
BSA Free	NB110-93479SS

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NB300-327

GAPDH Antibody

(3 Reviews)

(57 Publications)

0.1 ml

NB300-327

Western Blot: GAPDH Antibody [NB300-327] - Theoretical molecular weight: 36 kDa. Detection of GAPDH in mouse liver.

Western Blot: GAPDH Antibody [NB300-327] - Western blot analysis of extracts from Jurkat and HeLa cells using NB300-327 at 1:1000. Theoretical molecular weight: 36 kDa.

$Western Blot: GAPDH Antibody [NB300-327] - Analysis of different cell cytosolic or nuclear enriched fractions, GAPDH antibody, dilution 1:20,000 (Red): [1] protein standard, [2] NIH-3T3 cytosolic, [3] NIH-3T3 nuclear, [4] HeLa cytosolic, and [5] HeLa nuclear fractions. Strong band at 37kDa corresponds to GAPDH protein, mainly detected in the cytosolic fractions. The same blot was simultaneously probed with mouse mAb to the nuclear RNA binding protein SF3B4, dilution 1:1,000 (Green). In contrast to GAPDH, SF3B4 is exclusively expressed in the nuclear fraction.$

Immunocytochemistry/Immunofluorescence: GAPDH Antibody [NB300-327] - The GAPDH antibody was tested in Hela cells at a 1:500 dilution against Dylight 488 (Green). Alpha-tubulin and nuclei were counterstained with Dylight 550 (Red) and DAPI (Blue), respectively.

Immunocytochemistry/Immunofluorescence: GAPDH Antibody [NB300-327] - Confocal immunofluorescence analysis of HeLa cells using GAPDH (NB300-327) antibody (green). Nuclei was counterstained with DAPI (blue).

Immunocytochemistry/Immunofluorescence: GAPDH Antibody [NB300-327] - IF Confocal analysis of C2C12 cells using GAPDH antibody (NB300-327, 1:20). An Alexa Fluor 488-conjugated Goat to rabbit IgG was used as secondary antibody (green). Actin filaments were labeled with Alexa Fluor 568 phalloidin (red). DAPI was used to stain the cell nuclei (blue).

Simple Western: GAPDH Antibody [NB300-327] - Simple Western lane view shows a specific band for GAPDH in 0.2 mg/ml of HeLa lysate. This experiment was performed under reducing conditions using the 12-230 kDa separation system. Note: band observed higer than predicted 36 kDa molecular weight.

$Western Blot: GAPDH Antibody [NB300-327] - Effects of subchronic administration (7 and 14 days) of therapeutic relevant concentration of Brex (Brex: 300 nM) and interaction between Brex and 5-HT1A receptor (5-HT1AR) antagonist WAY (10 uM) on protein expression of 5-HT1A receptor in the plasma membrane fraction of cortical primary cultured astrocytes. In left side histograms, ordinate: mean +/- SD (n = 6) of the relative protein level of 5-HT1AR per GAPDH. * p < 0.05, ** p < 0.01: relative to control (Brex-free) by one-way analysis of variance (ANOVA) with Tukey’s post-hoc test, and @ p < 0.05: relative to Brex for 14 days by Student’s T-test. Right side panels indicate their pseudo-gel images using capillary immunoblotting. Antibodies used: 5-HT1A (NBP2-21590) and GAPDH (NB300-327). Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/35743014/) licensed under a CC-BY license.$

Representative immunoblot of KDR and FGFR CAM protein expression levels examined by Western blotting. GNS, graphene nanosheet; NG, graphite nanoparticle; ND, diamond nanoparticle; C60, fullerene C60; MWNT, multi-wall nanotube; KDR, vascular endothelial growth factor receptor; FGFR, fibroblast growth factor receptor; GAPDH, glyceraldehyde-3-phosphate dehydrogenase.

Western Blot: GAPDH Antibody [NB300-327] - Increased PIP expression in the lungs of PF‐PH compared to PF ratsA, BRelative expression of PIP mRNA (A) & protein (B) normalized to GAPDH.CRepresentative images & PIP quantification.Data information: Values are expressed as mean ± SEM. The number of samples per group for each experiment is included within each bar graph (t‐test; *P < 0.05, **P < 0.01). Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31468711), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

$Western Blot: GAPDH Antibody [NB300-327] - Effects of subchronic administration (7 & 14 days) of therapeutic relevant concentration of Brex (Brex: 300 nM) & interaction between Brex & 5-HT1A receptor (5-HT1AR) antagonist WAY100635 (WAY: 10 μM) on protein expression of 5-HT1A (panel A) & 5-HT7 (panel B) receptor in the plasma membrane fraction of cortical primary cultured astrocytes. In left side histograms, ordinate: mean ± SD (n = 6) of the relative protein level of 5-HT1AR & 5-HT7R per GAPDH. * p < 0.05, ** p < 0.01: relative to control (Brex-free) by one-way analysis of variance (ANOVA) with Tukey’s post-hoc test, & @ p < 0.05: relative to Brex for 14 days by Student’s T-test. Right side panels indicate their pseudo-gel images using capillary immunoblotting. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/35743014), licensed under a CC-BY license. Not internally tested by Novus Biologicals.$

Western Blot: GAPDH Antibody [NB300-327] - Online lung microarray analysis revealed PIP as one of the Slug transcriptional targets mediating vascular cell proliferation in PF‐PHAHeatmap of the 20 genes upregulated in GSE24988 microarray & known to be Slug transcriptional target.BVenn diagram showing the overlap between Slug targets implicated in cell proliferation & known to be extracellular.CHeatmap of the seven transcriptional targets of Slug known to promote proliferation & to be extracellular.D, ERelative expression of prolactin‐induced protein (PIP) mRNA (D) & protein (E) expression normalized to GAPDH in PF & PF‐PH patients.FRepresentative images of PIP immunohistochemistry showing its extracellular localization & quantification.G–JProliferation assay on healthy fibroblast (G), pulmonary arterial EC (H), & healthy pulmonary arterial SMC (I & J) in the presence or absence of PIP.Data information: Values are expressed as mean ± SEM. The number of samples per group for each experiment is included within each bar graph. Statistical test: panels (D–F): t‐test; panels (G–J): ANOVA (*P < 0.05, **P < 0.01 ***P < 0.001). Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31468711), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: GAPDH Antibody [NB300-327] - Growth of lactobacilli on IECs & their influence towards C. albicans cytotoxicity, adhesion, hyphal length & translocation. (A) LDH release of IECs colonized (Pre-Inc.) or simultaneously colonized (w/o Pre-Inc.) with L. rhamnosus (L.r.) at different MOI (5, 50 or 250) & infected or not with C. albicans (C.a.) (MOI 1) & measured at 24 h post-infection. (B) Growth of L. paracasei (L.p.), L. rhamnosus, L. salivarius (L.s.), L. fermentum (L.f.), & L. brevis (L.b.) on IECs. (C) Percentage of C. albicans adhered to IECs colonized with different Lactobacillus species (MOI 50) at 1 h post-infection. (D) C. albicans hyphal induction on IECs or on plastic colonized with L. rhamnosus or L. brevis (MOI 50) at 4 h post-infection. Results were normalized to C. albicans single infection. (E) Translocation of C. albicans (MOI 1) across IECs colonized with L. rhamnosus or L. brevis (MOI 50) at 24 h post-infection. (F) Assessment of epithelial barrier integrity measured as the loss of transepithelial electrical resistance (TEER) in response to L. rhamnosus or L. brevis (MOI 50) colonization & C. albicans infection in the presence or absence of Lactobacillus colonization at 24 h post-infection. Data are TEER loss in percentage of uninfected host cells (before pre-incubation). (G) E-Cadherin protein expression analyzed by western blot compared to GAPDH in IECs that were left uninfected or colonized with L. rhamnosus (MOI 50) & infected with C. albicans for 6, 12 & 24 h. Data are mean±s.e.m. *P<0.05, **P<0.01, ***P<0.005 (t-test). Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31413153), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

$Panel (D) indicates the expression of connexin43 (Cx43) and pannexin1 (PANX1) in the plasma membrane fraction of the PPN between wild type (grey columns) and S286L-TG (black columns). Ordinates indicate the mean � SD (n = 6) of the relative expression of connexin43 and pannexin1 per GAPDH. Right-side panels indicate the pseudo-gel images of connexin43, pannexin1 and GAPDH, obtained using capillary immunoblotting. Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/40564986/), licensed under a CC-BY license. Not internally tested by Novus Biologicals.$

Reactivity:

Hu, Mu, Rt, Po, Ba, Bv, Ch, Eq, Fu, In, Ye

Species Glossary

Reactivity: Hu, Mu, Rt, Po, Ba, Bv, Ch, Eq, Fu, In, Ye

Applications:

, , ,

Applications: , , ,

Host:

Rabbit Polyclonal

Host: Rabbit Polyclonal

Sizes:

Sample Size Available

Sizes: Sample Size Available

Conjugate:

Unconjugated

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NBP1-48336

Lactate Dehydrogenase A/LDHA Antibody - BSA Free

(4 Reviews)

(45 Publications)

0.1 ml

NBP1-48336

Immunohistochemistry: Lactate Dehydrogenase A/LDHA Antibody - BSA Free [NBP1-48336] - Staining of postnatal day 8(P8) Plp-EGFP transgenic mice brain section. Image from verified customer review.

Flow Cytometry: Lactate Dehydrogenase A/LDHA Antibody - BSA Free [NBP1-48336] - An intracellular stain was performed on HeLa cells with Lactate Dehydrogenase A/LDHA Antibody NBP1-48336AF488 (blue) and a matched isotype control (orange). Cells were fixed with 4% PFA and then permeabilized with 0.1% saponin. Cells were incubated in an antibody dilution of 5 ug/mL for 30 minutes at room temperature. Both antibodies were conjugated to Alexa Fluor 488.

Western Blot: Lactate Dehydrogenase A/LDHA Antibody - BSA Free [NBP1-48336] - Analysis of Lactate Dehydrogenase A in HeLa whole cell lysates.

Western Blot: Lactate Dehydrogenase A/LDHA Antibody - BSA Free [NBP1-48336] - Analysis of Lactate Dehydrogenase A in NIH/3T3 whole cell lysates.

Western Blot: Lactate Dehydrogenase A/LDHA Antibody - BSA Free [NBP1-48336] - Lactate Dehydrogenase A expression in bovine skeletal muscle lysate. Image from verified customer review.

Western Blot: Lactate Dehydrogenase A/LDHA Antibody - BSA Free [NBP1-48336] - Lactate Dehydrogenase A expression in porcine skeletal muscle lysate. Image from verified customer review.

Immunocytochemistry/Immunofluorescence: Lactate Dehydrogenase A/LDHA Antibody - BSA Free [NBP1-48336] - The effect of the co-culturing of cancer cells and fibroblasts on the expression of Hk2 and Ldha. In the co-cultures, the expression of Ldha was reduced in cancer cells, but was elevated in fibroblasts. Bar = 50 um. The ratio of the fluorescence of Hk2 and Ldha to beta-actin in the MLF monoculture was assumed to be 1. All the experiments were performed in triplicate and obtained similar results, and representative data from one experiment are shown in the figure. Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31947613/) licensed under a CC-BY license.

Immunohistochemistry: Lactate Dehydrogenase A/LDHA Antibody - BSA Free [NBP1-48336] - Staining of Lactate Dehydrogenase A in lung tissue.

Flow Cytometry: Lactate Dehydrogenase A/LDHA Antibody - BSA Free [NBP1-48336]

Simple Western: Lactate Dehydrogenase A/LDHA Antibody - BSA Free [NBP1-48336] - Lane view shows a specific band for Lactate dehydrogenase A in 0.1 mg/ml of HeLa lysate. This experiment was performed under reducing conditions using the 12-230kDa separation system.

Simple Western: Lactate Dehydrogenase A/LDHA Antibody - BSA Free [NBP1-48336] - Protein changes in ONHAs corroborate bioenergetics data. (A) Glucose transporter-1 protein levels in Stretched ONH astrocytes are significantly higher than Control (*p = 0.0225, n = 7 Control, n = 8 Stretch). Retinal lysate from a 2 month-old mouse was used as a positive control for each protein analyzed, while negative control was the signal obtained when no primary antibody was included in the capillary. (B) Lactate dehydrogenase-A, the astrocyte-specific isoform of the enzyme that catalyzes the interconversion of pyruvate & lactate, has equivalent protein levels in Control & Stretch ONH astrocytes. (C) Glucose-6-phosphate dehydrogenase, the enzyme that shunts glucose into the pentose phosphate pathway, is no different in Control & Stretch ONH astrocytes. (D) Glutamine synthetase, the enzyme that synthesizes glutamine from glutamate, is no different in Control & Stretch ONH astrocytes. (E) The monomeric form of glutamate-aspartate transporter (GLAST) has significantly higher protein levels in the Stretch as compared to the Control ONH astrocytes (p = 0.020; n = 4 Control, n = 5 Stretch). (F) GLAST dimer protein levels are no different in Control & Stretch ONH astrocytes. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/35992925), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

The effect of the co-culturing of cancer cells and fibroblasts on the expression of Hk2 and Ldha. (A) and (B): the co-culturing of fibroblasts (murine lung fibroblasts (MLF) or human lung fibroblasts (HLF)) with respective cancer cells (KLN205 or A549) decreased the level of Hk2 in cancer cells, having only a minor effect on the enzyme in fibroblasts. (C) and (D): in the co-cultures, the expression of Ldha was reduced in cancer cells, but was elevated in fibroblasts. Bar = 50 um. The black and white images depict differences in the shape and size of fibroblasts and cancer cells in the co-cultures. The ratio of the fluorescence of Hk2 and Ldha to beta -actin in the MLF and HLF monocultures was assumed to be 1. Asterisks indicate a statistically significant difference (p < 0.05). All the experiments were performed in triplicate and obtained similar results, and representative data from one experiment are shown in the figure. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/31947613), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Reactivity:

Hu, Mu, Po, Bv

Species Glossary

Reactivity: Hu, Mu, Po, Bv

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	NBP1-48336AF350
Alexa Fluor 405	NBP1-48336AF405
Alexa Fluor 488	NBP1-48336AF488
Alexa Fluor 532	NBP1-48336AF532
Alexa Fluor 594	NBP1-48336AF594
Alexa Fluor 647	NBP1-48336AF647
Alexa Fluor 700	NBP1-48336AF700
Alexa Fluor 750	NBP1-48336AF750
Allophycocyanin	NBP1-48336APC
Biotin	NBP1-48336B
CoraFluor 1	NBP1-48336CL1
DyLight 350	NBP1-48336UV
DyLight 405	NBP1-48336V
DyLight 488	NBP1-48336G
DyLight 550	NBP1-48336R
DyLight 594	NBP1-48336DL594
DyLight 650	NBP1-48336C
DyLight 680	NBP1-48336FR
DyLight 755	NBP1-48336IR
FITC	NBP1-48336F
HRP	NBP1-48336H
Janelia Fluor 525	NBP1-48336JF525
Janelia Fluor 549	NBP1-48336JF549
Janelia Fluor 646	NBP1-48336JF646
Janelia Fluor 669	NBP1-48336JF669
PE	NBP1-48336PE
PerCP	NBP1-48336PCP
mFluor Violet 450 SE	NBP1-48336MFV450
mFluor Violet 500 SE	NBP1-48336MFV500
mFluor Violet 610 SE	NBP1-48336MFV610

Available Formulations

Formulation	Catalog #	Availability	Price
BSA Free	NBP1-48336SS

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(select up to 3 products from this page to compare)

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

Lysate Type

Preservative

Protein Or Peptide

Research Areas

Has Sample Size

Promotional Item

Species Glossary

GAPDH Antibody (1D4) - BSA Free

PGC1 alpha Antibody - BSA Free

PINK1 Antibody - BSA Free

CHREBP Antibody - BSA Free

GAPDH Antibody - BSA Free

GAPDH Antibody (6C5cc) - BSA Free

Glut1 Antibody - BSA Free

GAPDH Antibody

Perilipin-2/ADFP Antibody - BSA Free

Pyruvate Dehydrogenase E1-alpha subunit [p Ser293] Antibody - BSA Free

GAPDH Antibody

Lactate Dehydrogenase A/LDHA Antibody - BSA Free