Neuroscience 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

Available Formulations

Formulation	Catalog #	Availability	Price
BSA Free	NB300-221SS

compare

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

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

compare

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

NB100-56708

Caspase-3 Antibody (31A1067) - (Pro and Active) - BSA Free

(2 Reviews)

(202 Publications)

0.1 mg

NB100-56708

Image of Caspase-3 Antibody (31A1067) - (Pro and Active). Whole cell protein from Jurkat cells treated with and without 2 uM staurosporine as indicated was separated on a 4-15% gel by SDS-PAGE, transferred to 0.2 um PVDF membrane and blocked in 5% non-fat milk in TBST. The membrane was probed with 5 ug/ml anti-Caspase 3 in 1% milk, and detected with an anti-mouse HRP secondary antibody using a Femto sensitivity chemiluminescence reagent. Note the detection of both pro-caspase 3 at 35 kDa and the cleaved active caspase 3 at 15-17 kDa.

<b>Biological Strategies Validation. </b>Tissue section of human spleen using 1:200 dilution of Caspase-3 antibody (clone 31A1067). The staining was developed with HRP labeled anti-mouse IgG secondary antibody and DAB reagent, and nuclei of cells were counter-stained with hematoxylin. This Caspase 3 antibody generated primarily a specific cytoplasmic staining in a subset of spleenocytes with some nuclear signal in a few cells.

Simple Western lane view shows a specific band for Caspase-3 Antibody (31A1067) - (Pro and Active) in 0.1 mg/ml of HeLa lysate. This experiment was performed under reducing conditions using the 12-230kDa separation system.

Caspase-3 was detected in immersion fixed paraffin-embedded sections of human bladder tissue using 1:50 dilution of mouse aCaspase-3 Antibody (31A1067) - (Pro and Active) (NB100-56708), for 1 hour at room temperature followed by anti-mouse IgG VisUCyte HRP polymer(VC001). Tissue was stained using DAB (brown) and counterstained with hematoxylin (blue).

Paclitaxel in combination with MWE retarded tumor growth in a human bladder carcinoma TSGH 8301 xenograft model. The levels of total (t-PTEN) and phospho-PTEN (p-PTEN) and Caspase 3 in the tumor specimens were determined by Western blotting and then quantified using beta-actin as the protein loading control; the results are expressed as a percentage of the control. Image collected and cropped by CiteAb from the following publication (//www.nature.com/articles/srep20417), licensed under a CC-BY license.

An intracellular stain was performed on NIH3T3 cells with Caspase-3 Antibody (31A1067) - (Pro and Active) Antibody NB100-56708AF700 (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 10 ug/mL for 30 minutes at room temperature. Both antibodies were conjugated to Alexa Fluor 700.

<b>Biological Strategies Validation. </b>Lysates of Jurkat human acute T cell leukemia cell line untreated (-) or treated (+) with VP-16. PVDF membrane was probed with 0.1 ug/mL of mouse monoclonal Caspase-3 Antibody (31A1067) - (Pro and Active) (NB100-56708, Novus Biologicals) followed by 1:2000 dilution donkey anti-mouse IgG.

An intracellular stain was performed on HeLa cells with Caspase-3 Antibody (31A1067) - (Pro and Active) NB100-56708 (blue) and a matched isotype control (orange). Cells were fixed with 4% PFA and then permeablized with 0.1% saponin. Cells were incubated in an antibody dilution of 5 ug/mL for 30 minutes at room temperature, followed by mouse F(ab)2 IgG (H+L) APC-conjugated secondary antibody (F0101B, R&D Systems).

Western Blot: Mouse Monoclonal Caspase-3 Antibody (31A1067) - (Pro and Active) [IMGENEX: IMG-144A] [NB100-56708] - Whole cell lysates from MDA-MB-231, MCF-7, SUM149 and SUM159 cells were loaded with 50 ug/lane. 10% SDS-PAGE. Caspase-3 Antibody (NB100-56708) was used for primary antibody: 1:2000, 4℃, overnight. Image from a verified customer review.

Immunocytochemistry/ Immunofluorescence: Caspase-3 Antibody (31A1067) - (Pro and Active) - BSA Free [NB100-56708] - rOPN administration influenced the interaction & balance between Beclin 1 & Caspase‐3 at 24 h after SAH. Double immunofluorescence staining of Caspase‐3 & Beclin 1 in Sham group, SAH + Vehicle group & SAH + rOPN group at 24 h after SAH induction. Sample size is 9, n = 3 per group. Localization of Caspase‐3 can be cytoplasmic & nuclear. Staining in the nucleus is considered to be an indication of active Caspase‐3. The dashed lines & the red box on brain slice images indicate the locations observed. Vehicle, phosphate‐buffered saline; Scale bar = 50 μm Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31436915), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: Caspase-3 Antibody (31A1067) - (Pro and Active) - BSA Free [NB100-56708] - PEM induces YIPF2 upregulation & apoptosis in NSCLC cells.a, b H1792 (a) & H1299 (b) NSCLC cells were treated with PEM at various concentrations (0–10.0 μM) for 36 h. Cell lysates were analyzed by Western blotting with antibodies against YIPF2 & ACTB. c Overexpression of YIPF2 in H1299 cells in the presence or absence of PEM at 5.0 μM for 36 h. Cell lysates were analyzed by Western blotting with antibodies against YIPF2, CASP8, CASP3, PARP1 & ACTB. d Knockdown of YIPF2 expression by YIPF2–1 siRNA in A549 NSCLC cells in the presence or absence of PEM at 5.0 μM for 36 h. Cell lysates were analyzed by Western blotting with antibodies against YIPF2, CASP8, CASP3, PARP1 & ACTB. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/32303681), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Immunocytochemistry/ Immunofluorescence: Caspase-3 Antibody (31A1067) - (Pro and Active) - BSA Free [NB100-56708] - Lipofection of top broccoletti-miR candidates does not influence basal & induced apoptosis.(A) BxPc-3 & Bx-Gem cells were transfected as described in Figure 3. Seventy-two hours later, the cells were stained with Annexin V-PE & 7-AAD, followed by FACS analysis. The percentage of Annexin V- & 7-AAD-positive cells is shown. (B) Lipofected BxPc-3 & Bx-Gem cells were stained with an antibody specific for the proliferation marker Ki-67 (green) or the apoptosis marker cleaved fragment of caspase-3 (red), which indicates apoptosis. Representative images at ×100 magnification are shown. The percentage of Ki-67- or caspase-3-positive cells was counted in 18 visual fields, & the means ± SD are shown in the diagram below. (C) BxPc-3 & Bx-Gem were lipofected as described above, & at 24 h later, the cells were treated with gemcitabine (10 nM) or were left untreated. Ninety-six hours after gemcitabine treatment, viability was determined by MTT assay. The data are presented as the means ± SD (**P < 0.01). Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/32292571), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: Caspase-3 Antibody (31A1067) - (Pro and Active) - BSA Free [NB100-56708] - PEM induces apoptosis of NSCLC cells via YIPF2-TNFRSF10B axis.a, b A549 (a) & H1792 (b) cells were treated with PEM at 5.0 μM for the indicated times (0, 6, 12, 24, 36 & 48 h). Cell lysates were analyzed by Western blotting with antibodies against YIPF2, TNFRSF10B & ACTB. c A549 cells were treated with doxorubicin (DOX) at various concentrations (0–2.0 μM) for 18 h. Cell lysates were analyzed by Western blotting with antibodies against YIPF2, TNFRSF10B & ACTB. d Overexpression of YIPF2 in H1792 & H1299 cells in the presence or absence of PEM at 5.0 μM for 36 h. Cell lysates were analyzed by Western blotting with antibodies against YIPF2, TNFRSF10B & ACTB. e Knockdown of YIPF2 expression by YIPF2–1 siRNA in A549 & H1792 cells in the presence or absence of PEM at 5.0 μM for 36 h. Cell lysates were analyzed by Western blotting with antibodies against YIPF2, TNFRSF10B & ACTB. f Overexpression of YIPF2 in H1299 cells (left) or Knockdown of YIPF2 expression by YIPF2–1 siRNA in H1792 cells (right) in the presence or absence of PEM at 5.0 μM for 36 h. Cell lysates were analyzed by Western blotting with antibodies against YIPF2, TNFRSF10A & ACTB. g Three A549 cell lines (Ctrl, YIPF2, YIPF2 + siTNFRSF10B) in the presence or absence of PEM at 5.0 μM for 36 h. Cell lysates were analyzed by Western blotting with antibodies against YIPF2, TNFRSF10B, CASP8, CASP3 & ACTB. h Three H1299 cell lines (Ctrl, siYIPF2–1, siYIPF2–1 + TNFRSF10B (short isoform)) in the presence or absence of PEM at 5.0 μM for 36 h. Cell lysates were analyzed by Western blotting with antibodies against YIPF2, TNFRSF10B, CASP8, CASP3 & ACTB. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/32303681), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Immunocytochemistry/ Immunofluorescence: Caspase-3 Antibody (31A1067) - (Pro and Active) - BSA Free [NB100-56708] - Cell numbers positively stained for NeuN, DCX, PCNA & caspase-3 in the subgranular region of the dentate gyrus in WT & RanBP9−/− (KO) mice.(A), DAPI-stained brain sections to show the highlighted subgranular zone within the dentate gyrus region of the hippocampus used for cell counts shown in B. (B), Representative brain sections stained with anti-NeuN, anti-DCX, anti-PCNA, anti-capsase-3 & counter stained with DAPI. Cell counting revealed significantly decreased numbers of NeuN positive cells in RanBP9−/− (KO) brains (22%) compared to WT controls. However DCX, PCNA & caspase positive cell numbers were not significantly altered. In each group, n = 3, data presented as mean± SEM. **, p<0.01 by Student’s t-test. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/23840553), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

$Western Blot: Caspase-3 Antibody (31A1067) - (Pro and Active) - BSA Free [NB100-56708] - NFATc1 regulates DcR3 expression at a transcriptional level. (A,B) Immunoblot analysis of whole-cell lysates & quantitative real-time-PCR assaying relative DcR3 mRNA expression of ACHN & 769-P cells 24 h after treatment with cyclosporin A (CsA, 25 μM) or Tacrolimus (FK-506, 50 μM) (A); 48 h post transfection with NFATc1 or an empty vector control (neo) (B). Expression data were normalized to internal 18S rRNA expression (mean ± SEM; n=3; *p<0.05, **p<0.01, ***p<0.001; T-test). (C) Immunoblot analysis of cytoplasmic & nuclear fractions of ACHN & 769-P cells after treatment with LY294002 (50 μM), Everolimus (1 μM), or Cyclosporine A (25 μM). (D) Relative NFATc1–luciferase reporter activity of ACHN & 769-P cells 24 h post transfection with myrAkt or an empty vector control (neo) (mean ± SEM; n=3; *p<0.05, **p<0.01; T-test). Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/24107265), licensed under a CC-BY license. Not internally tested by Novus Biologicals.$

Western Blot: Caspase-3 Antibody (31A1067) - (Pro and Active) - BSA Free [NB100-56708] - rOPN administration elevated the expression of autophagy‐related proteins while suppressing apoptosis in rat brain at 24 h after SAH. The effects of rOPN on expression levels of (A) Beclin 1, mean ± SD is 1.016 ± 0.2262 in Sham group, 2.874 ± 1.147 in SAH + Vehicle group, 4.963 ± 2.05 in SAH + rOPN group, F = 15.52, (B) ATG5, mean ± SD is 0.8908 ± 0.2545 in Sham group, 2.332 ± 0.6431 in SAH + Vehicle group, 4.364 ± 1.309 in SAH + rOPN group, F = 25.02, (C) LC3, mean ± SD is 1 ± 0.1845 in Sham group, 1.755 ± 0.3017 in SAH + Vehicle group, 2.7 ± 0.7957 in SAH + rOPN group, F = 17.23, (D) Cleaved Caspase‐3, mean ± SD is 1.008 ± 0.186 in Sham group, 4.112 ± 1.528 in SAH + Vehicle group, 2.291 ± 0.6268 in SAH + rOPN group, F = 15.86, (E) Bax, mean ± SD is 1.006 ± 0.321 in Sham group, 37.47 ± 10.86 in SAH + Vehicle group, 23.83 ± 8.143 in SAH + rOPN group, F = 33.13, (F) Bcl‐2, mean ± SD is 1.005 ± 0.2736 in Sham group, 0.2309 ± 0.1257 in SAH + Vehicle group, 0.7843 ± 0.2278 in SAH + rOPN group, F = 20.1, in the left hemisphere of rat brain at 24 h after SAH. Sample size is 18, n = 6 per group. Data were presented as mean ± SD. *P < .05, ***P < .001 vs Sham group; #P < .05, ##P < .01 vs SAH + Vehicle group Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31436915), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: Caspase-3 Antibody (31A1067) - (Pro and Active) - BSA Free [NB100-56708] - RAB8 suppresses PEM-induced apoptosis of NSCLC cells by promoting the removing of TNFRSF10B from plasma membrane to cytoplasm.a, b Knockdown of RAB8 expression by RAB8 siRNA in H1792 (a) & A549 (b) cells in the presence or absence of PEM at 5.0 μM for 36 h. The surface expression of TNFRSF10B was confirmed by flow cytometry analyses. c Overexpression of RAB8 in H1299 cells in the presence or absence of PEM at 5.0 μM for 36 h. Cell lysates were analyzed by Western blotting with antibodies against RAB8, TNFRSF10B, CASP8, CASP3, PARP1 & ACTB. d Knockdown of RAB8 expression by RAB8 siRNA in H1792 cells in the presence or absence of PEM at 5.0 μM for 36 h. Cell lysates were analyzed by Western blotting with antibodies against RAB8, TNFRSF10B, CASP8, CASP3, PARP1 & ACTB. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/32303681), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Reactivity:

Hu, Mu, Rt, Po, Ch, ChHa, Ma

Species Glossary

Reactivity: Hu, Mu, Rt, Po, Ch, ChHa, Ma

Applications:

, , , , , , , , , , ,

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

Host:

Mouse Monoclonal

Host: Mouse Monoclonal

Alt Catalog#

IMG-144A

Alt Catalog# IMG-144A

Sizes:

Sample Size Available

Sizes: Sample Size Available

Conjugate:

Unconjugated

Available Conjugates:

Validated by:

Validated by:

Conjugate	Catalog #	Availability	Size	Price
Alexa Fluor 350	NB100-56708AF350
Alexa Fluor 405	NB100-56708AF405
Alexa Fluor 488	NB100-56708AF488
Alexa Fluor 532	NB100-56708AF532
Alexa Fluor 594	NB100-56708AF594
Alexa Fluor 647	NB100-56708AF647
Alexa Fluor 700	NB100-56708AF700
Alexa Fluor 750	NB100-56708AF750
Allophycocyanin	NB100-56708APC
Biotin	NB100-56708B
CoraFluor 1	NB100-56708CL1
DyLight 350	NB100-56708UV
DyLight 405	NB100-56708V
DyLight 488	NB100-56708G
DyLight 550	NB100-56708R
DyLight 594	NB100-56708DL594
DyLight 650	NB100-56708C
DyLight 680	NB100-56708FR
DyLight 755	NB100-56708IR
FITC	NB100-56708F
HRP	NB100-56708H
Janelia Fluor 525	NB100-56708JF525
Janelia Fluor 549	NB100-56708JF549
Janelia Fluor 646	NB100-56708JF646
Janelia Fluor 669	NB100-56708JF669
PE	NB100-56708PE
PerCP	NB100-56708PCP
mFluor Violet 450 SE	NB100-56708MFV450
mFluor Violet 500 SE	NB100-56708MFV500
mFluor Violet 610 SE	NB100-56708MFV610

Available Formulations

Formulation	Catalog #	Availability	Price
BSA Free	NB100-56708SS
Azide and BSA Free	NBP2-33244

compare

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

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

compare

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

NB300-213

MAP2 Antibody - BSA Free

(5 Reviews)

(132 Publications)

0.05 ml

NB300-213

Mouse primary cultures stained with MAP2 antibody. ICC/IF image submitted by a verified customer review.

Immunofluorescent analysis of cortical neuron-glial cell culture from E20 rat stained with chicken pAb to microtubule associated protein 2 (MAP2), NB300-213, dilution 1:10,000 in red, and mouse mAb to MAP-tau, NPB2-25162, dilution 1:2,000, in green. The blue is DAPI staining of nuclear DNA. NB300-213 antibody stains dendrites and perikarya of neurons, while NBP2-25162 antibody labels neuronal perikarya, dendrites and also axonal process. As a result perikarya and dendrites appears orange-yellow, since they contain both MAP2 and tau, while axons are green.

Western blot analysis of whole brain tissue lysates using chicken pAb to microtubule associated protein 2 (MAP2), NB300-213, dilution 1:50,000 in green: [1] protein standard (red), [2] adult rat brain, [3] embryonic E20 rat brain, [4] adult mouse brain. Strong band observed at ~280 kDa mark corresponds to two major isoforms of MAP2 protein referred to as MAP2A and MAP2B. Smaller fragments of these isoforms are also detected if the antibody is used at higher concentrations.

PEA decreases astrocyte activation in organotypic cultures of rat hippocampi and rescues neuronal CA3 damage caused by Abeta challenge. Abeta-challenged (1 ug/ml) slices of rat hippocampi were treated for 24 hours with PEA (0.1 uM) in the presence of the selective PPAR? antagonist (GW9662, 9 nM) or the selective PPARalpha antagonist (MK886, 3 uM). Representative photomicrographs of the CA3 region showing the results of immunofluorescence experiments aimed at investigating the effect of treatments on astrocyte activation and neuronal loss, as determined by immunostaining for GFAP (green) and MAP2 (red) alone or merged, respectively. Nuclei were stained with Hoechst (blue). Scale bar: 10 um. Arrows in the photomicrographs indicate astrocyte infiltration events and apoptotic condensation in the nuclei of adjacent neurons.

Human iPS derived neurons labeled with MAP2 (in green) at 1:5000 dilution. Image from verified customer review.

MAP2 in the retina detected by NB300-213 antibody (magenta). DAPI (blue). Image from verified customer review.

Human DA neurons 28 DIV stained with MAP2 antibody (blue). ICC/IF image submitted by a verified customer review.

PEA inhibits astroglial proliferation and reduces neuronal loss in mixed neuroglia co-cultures exposed to Abeta. Abeta-challenged (1 ug/ml) astrocyte/neuron mixed cultures were treated with PEA (0.1 uM) i9662, 9 nM) on the presence of the selective PPAR-gamma antagonist (GWr the selective PPARalpha antagonist (MK886, 3 uM). After 24 hours of treatment, cells were processed for analyses. Immunofluorescence photomicrographs showing the effect of the treatments on astrocyte proliferation and neuronal loss, as determined by immunostaining for GFAP (green) and MAP2 (red), respectively. Arrows indicate chromatin condensation in nuclei stained with Hoechst dye (blue) as markers of apoptotic events. Scale bar: 10 um. Image collected and cropped by CiteAb from the following publication (//jneuroinflammation.biomedcentral.com/articles/10.1186/1742-2094-9-49), licensed under a CC-BY license.

Oxytocin receptors (Oxtr) are expressed in mouse hippocampus. Confocal images of Oxtr-expressing neurons in the CA1 subfields of the medial and caudal hippocampus from OxtrVn/+ sections, triple stained with antibodies directed against NeuN (red), MAP2 (magenta), and Venus (green). Image collected and cropped by CiteAb from the following publication (//elifesciences.org/articles/22466), licensed under a CC-BY license.

Differential and neuron-specific Oxtr expression in mouse hippocampus. Immunohistochemical mapping of Venus expression in coronal sections of the rostral, medial, and caudal hippocampus from three weeks old OxtrVn/+ mice triple-labeled with antibodies against NeuN (red), Venus (green), and Map2 (magenta). Image collected and cropped by CiteAb from the following publication (//elifesciences.org/articles/22466), licensed under a CC-BY license.

ATM activation by chloroquine alleviates senescence.(a) Immunoblots showing protein levels of ATM, NBS1, and RAP80 in human skin fibroblasts (HSFs). A gradually increased level of p16 indicates cellular senescence, while elevated gamma H2AX level indicates accumulated DNA damage. (b) Immunoblots showing protein levels of ATM, NBS1, and RAP80 in mouse embryonic fibroblasts (MEFs). (c) Immunoblots showing protein levels of ATM, NBS1, and RAP80 in brain tissues isolated from 3-, 10-, and 18-month-old male mice. (d) SA-beta -Gal staining in HSFs treated with sh-ATM or scramble shRNA. Scale bar, 100 µm. (e) Quantification of SA-beta -Gal-positive staining of (d) from five views randomly captured for each group. Data represent means ± SEM. ***p<0.001. (f) Immunoblots showing increased gamma H2AX and unaffected LC3I/II in HSFs treated with sh-ATM or scramble shRNA. (g) Immunoblots showing protein levels of pS1981 ATM, gamma H2AX, and cleaved caspase-3 in HSFs treated with 10 μM of CQ for indicated time. (h) SA-beta -Gal staining in HSFs expressing either scramble or ATM shRNA treated with 1 μM CQ or DMSO (12 hr). Scale bar, 100 µm. (i) Quantification of SA-beta -Gal-positive staining of (h) from five views randomly captured for each group. Data represent means ± SEM. ***p<0.001; ‘N.S.’ indicates no significant difference. (j) HSFs at passage 20 were continuously cultured with 1 μM CQ or DMSO, and cell number was calculated at each passage. Data represent means ± SEM. ***p<0.01. (k) Immunoblots showing protein levels of gamma H2AX, p62, and LC3 in MEFs treated with 1 μM CQ or DMSO. Note that CQ had little effect on the expression levels of p62 and LC3. (l) MEFs at passage one were continuously cultured in 20% O2 with 1 μM CQ or DMSO, and cell number was determined at each passage. Data represent means ± SEM. ***p<0.01.10.7554/eLife.34836.006Figure 1—source data 1.Statistical analysis for SA-beta -Gal positive staining.10.7554/eLife.34836.007Figure 1—source data 2.Statistical analysis for EdU positive staining.Statistical analysis for SA-beta -Gal positive staining.Statistical analysis for EdU positive staining.Decline of ATM-centered DNA repair machinery during senescence.(a) Real-time PCR analysis showing progressively elevated mRNA level of p21 in continuously cultured human endothelial cells (HUVEC). **p<0.01. (b) SA-beta -Gal staining of HUVEC cells at indicated passages. Scale bar, 100 µm. (c) HUVEC cells at P21, P18, P12, and P7 were subjected to transcriptome analysis. A minimum average rpkm value of 1.0 and maximum 10% fluctuation in young cells (P7 Vs P12) was set as the threshold. Genes were downregulated by more than 20% in pre-senescent, and senescent cells compared with young cells (P21/P18 Vs P12/P7) were selected. (d) Pathway analysis of genes identified in (c) by STRING v10. (e) Downregulation of ATM-related DNA repair genes during senescence.ATM regulates replicative senescence.(a) Representative images showing cells treated with Scramble (sh-NC) or sh-ATM. (b) Percent EdU-positive cells in sh-NC or sh-ATM treated HSFs. Views were randomly captured and at least 100 cells were included in each group. Data represent means ± SEM. ***p<0.001. (c) Immunoblots showing protein levels of pS1981 ATM and gamma H2AX in HSFs treated with 10 μM chloroquine (CQ) or 0.4 μM CPT (4 hr). Note that CQ activated ATM (pS1981) without increasing gamma H2AX, while CPT activated ATM accompanied by increased gamma H2AX. (d) SA-beta -Gal staining in primary MEFs treated with 1 μM CQ or DMSO. Scale bar, 100 µm. (e) Quantification of SA-beta -Gal-positive staining of (d) from five views randomly captured for each group. Data represent means ± SEM. ***p<0.001. (f) Percent EdU-positive cells in HSFs treated with DMSO, 1 μM or 10 μM CQ. Views were randomly captured and at least 100 cells were included in each group. Data represent means ± SEM. ***p<0.001. (g) Representative images showing proliferative HSFs treated with different doses of CQ for the indicated time points. (h) Immunoblots showing LC3B levels in HSFs treated with indicated dose of CQ for indicated period of time. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/29717979), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Immunocytochemistry/ Immunofluorescence: MAP2 Antibody [NB300-213] - SUMO1 conjugates are not localized to amyloid plaques. (a) Sagittal brain sections of 24‐week‐old KI/AD & WT/AD animals were stained using anti‐HA antibodies (red), 6E10 antibodies (green) that label amyloid beta 1–42 among other amyloid beta variants (epitope lies within amino acids 3–8 of amyloid beta) & anti‐MAP2 antibodies (blue). Sections of the hippocampal subiculum are shown. Images are representatives of three independent experiments. Scale bar, 25 μm. (b) Anti‐HA signal intensity in amyloid plaques & in cell nuclei was quantified using ImageJ (N = 3, ***significance between WT/AD & KI/AD, p = .0007 in Student's t test) Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/29633471), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Immunocytochemistry/ Immunofluorescence: MAP2 Antibody [NB300-213] - Oxytocin receptors (Oxtr) are expressed in mouse hippocampus.(a & b) Coronal sections of the hippocampus (a) & striatum (b) from OxtrVn/+ & Oxtr+/+ mice stained for Venus & DAPI (ac, anterior commisure; cx, cortex; hip, hippocampus; str, striatum). (c) Confocal images of rostral Oxtr+/+ & OxtrVn/+ brain sections including hippocampus, double-labeled for Venus (green) & NeuN (red). (d) Confocal images of Oxtr-expressing neurons in the CA1 subfields of the medial & caudal hippocampus from OxtrVn/+ sections, triple stained with antibodies directed against NeuN (red), MAP2 (magenta), & Venus (green). (e) Representative images of hippocampal mass cultures obtained from OxtrVn/+ mice at P0 mice & processed for immunofluorescence staining at 5, 10, & 14 DIV using antibodies to Venus (green) & GAD67 (red), & DAPI (blue). (f) Quantitative analysis of Venus-positive neurons with (GAD67+) & without colabeling for GAD67 (GAD67-) in hippocampal mass cultures obtained from OxtrVn/+ mice at P0 mice & processed for immunofluorescence staining at 5, 10, & 14 DIV. Data are shown as mean ± SEM.DOI://dx.doi.org/10.7554/eLife.22466.015 Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/28231043), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

$Immunocytochemistry/ Immunofluorescence: MAP2 Antibody [NB300-213] - SUMO1 conjugates remain nuclear during increased amyloid burden. (a) Western blot analysis of subcellular fractions of 36‐week‐old KI/WT & KI/AD mouse brain using anti‐HA antibody (upper two panels) & antibodies to GluN1 (a marker of the postsynaptic compartment) & Synaptophysin (a marker of the presynaptic compartment) to validate the fractionation procedure (lower two panels). H, homogenate; P1, nuclear pellet; S1, supernatant after P1 sedimentation; P2, crude synaptosomal pellet; S2, supernatant after P2 sedimentation; LP1, lysed synaptosomal membranes; LS1, supernatant after LP1 sedimentation; LP2, pellet after LS1 sedimentation, SPM, synaptic plasma membranes. Bracket indicates the anti‐HA signal representing SUMOylation, arrow indicates RanGAP1, stars indicate nonspecific signal detected by the anti‐HA antibody. (b) Brain sagittal sections of aged (36 weeks old) KI/AD (left panels) & WT/AD (right panels) mice were immunostained using antibodies directed against HA (red, labels HA‐HA conjugates), MAP2 (green, labels neuronal somata & dendrites), & Synapsin1 (Syn1, magenta, labels synapses). The images show triple‐labeled neurons of hippocampal subiculum (b), cortical layer 5 (c), & proximal apical dendrite from hippocampal CA3 (d). The white line shows the orientation of the line‐scan used to generate the image stack shown in the bottom side view. Scale bar: 10 μm. Note that the anti‐HA immunosignal is mainly located in neuronal nuclei, only background staining is observed in WT/AD mice. Little anti‐HA signal is observed along MAP2‐positive structures & does not colocalize with Synapsin1 Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/29633471), licensed under a CC-BY license. Not internally tested by Novus Biologicals.$

Immunocytochemistry/ Immunofluorescence: MAP2 Antibody [NB300-213] - Validation of the CRISPR/Cas9 Alsin-/- cells in iPSC, NPC & iPSC-sMN.(A) Electrophoresis result of the PCR reaction using primers flanking exon three & within exon 3. Homozygous deletion was confirmed by the absence of a 2.8 kb. (B) Protein lysates from WT KOLF & Alsin-/- iPSC were loaded onto SDS-PAGE & immunoblotted with Alsin antibody. A band detected at ~184 kDa, but absent in Alsin-/-, corresponds to full-length Alsin. (C) WT KOLF, Alsin-/- iPSC, & neuroprogenitor cells (NPC) were immunostained with pluripotency markers Oct4 & Lin28, & neuroprogenitor markers Sox2 & Pax6, respectively. (D–E) WT KOLF & Alsin-/- iPSC-sMN were immunostained with motor neuron markers such as ChAT, HB9, & ISL1, nuclear dye DAPI, & cytoskeletal marker MAP2. (F) WT KOLF & Alsin-/- iPSC-sMN were immunostained with antibodies against Rab5 & Alsin, along with DAPI (nuclear) & phalloidin (actin) stains. Scale bars, 10 μm. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/29469808), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Immunocytochemistry/ Immunofluorescence: MAP2 Antibody [NB300-213] - PEA decreases astrocyte activation in organotypic cultures of rat hippocampi & rescues neuronal CA3 damage caused by A beta challenge. A beta -challenged (1 μg/ml) slices of rat hippocampi treated for 24 hours w/ PEA (0.1 μM) in presence of selective PPAR gamma antagonist (GW9662, 9 nM) or selective PPAR alpha antagonist (MK886, 3 μM). (A) Nissl staining showing effect of treatment on morphology of organotypic hippocampal slices. Scale bar: 80 μm. A beta caused a marked neuronal loss, mainly in CA3 region of hippocampus, as highlighted by arrows. PEA able to reverse this effect. (B) Representative photomicrographs of CA3 region showing Results of immunofluorescence experiments aimed at investigating effect of treatments on astrocyte activation & neuronal loss, as determined by immunostaining for GFAP (green) & MAP2 (red) alone or merged, respectively. Nuclei stained w/ Hoechst (blue). Scale bar: 10 μm. Arrows in photomicrographs indicate astrocyte infiltration events & apoptotic condensation in nuclei of adjacent neurons. (C) Relative quantification of GFAP-positive cell number as a count of astrocyte proliferation. (D) Apoptotic events detected on MAP2-expressing cells as an indication of neuronal death. For (C) & (D), average value determined by counting cells in at least five microscopic fields for each treatment. Results are presented as means ± SEM of four separate experiments. At least four slices from each experimental group observed for each experiment. Statistical analysis performed using parametric one-way analysis of variance, & multiple comparisons performed using Bonferroni test. ***P < 0.001 & *P < 0.05 vs. control; ∘∘P < 0.01 & ∘P < 0.05 vs. A beta -challenge slices. Image collected & cropped by CiteAb from following publication (//jneuroinflammation.biomedcentral.com/articles/10.1186/1742-2094-9-49), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Immunocytochemistry/ Immunofluorescence: MAP2 Antibody [NB300-213] - PEA inhibits astroglial proliferation & reduces neuronal loss in mixed neuroglia co-cultures exposed to A beta . A beta -challenged (1 μg/ml) astrocyte/neuron mixed cultures were treated with PEA (0.1 μM) in the presence of the selective PPAR gamma antagonist (GW9662, 9 nM) or the selective PPAR alpha antagonist (MK886, 3 μM). After 24 hours of treatment, cells were processed for analyses. (A) Immunofluorescence photomicrographs showing the effect of the treatments on astrocyte proliferation & neuronal loss, as determined by immunostaining for GFAP (green) & MAP2 (red), respectively. Arrows indicate chromatin condensation in nuclei stained with Hoechst dye (blue) as markers of apoptotic events. Scale bar: 10 μm. (B) Relative quantification of GFAP-positive cell number as a count of astrocyte proliferation. (C) Apoptotic events detected on MAP2-expressing cells as an indication of neuronal death. For (B) & (C), the average value was determined by counting cells in at least nine microscopic fields for each treatment. Results are presented as means ± SEM of three separate experiments. Statistical analysis was performed using parametric one-way analysis of variance, & multiple comparisons were performed using the Bonferroni test. ***P < 0.001 vs. unstimulated cells, ∘∘P < 0.01 & ∘P < 0.05 vs. A beta -stimulated cultures. Image collected & cropped by CiteAb from the following publication (//jneuroinflammation.biomedcentral.com/articles/10.1186/1742-2094-9-49), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Reactivity:

Hu, Mu, Rt, Fe

Species Glossary

Reactivity: Hu, Mu, Rt, Fe

Applications:

, , ,

Applications: , , ,

Host:

Chicken Polyclonal

Host: Chicken Polyclonal

Conjugate:

Unconjugated

compare

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

NB300-143

GAP-43 Antibody - BSA Free

(1 Review)

(111 Publications)

0.1 ml

NB300-143

Immunohistochemistry: GAP-43 Antibody [NB300-143] - Representative images of immunohistological staining (brown) of OMP-positive (OMP+) cells, GAP43+ immature ORNs. Tissue sections were counterstained with the nuclear dye hematoxylin (blue). Numbers of SOX2+ ORN progenitors and Ki67+ actively proliferating cells per mm of the basal layer and OMP+ mature ORNs, GAP43+ immature ORNs, and Cas3+ apoptotic cells per mm of the OE in saline or rhIGF-1-treated mice. Open circles, rectangles, and triangles represent the values for each mouse in the saline, low-IGF-1, and high-IGF-1 treated groups (each n = 6), respectively. Image collected and cropped by Citeab from the following publication (Dose-Dependent Effects of Insulin-Like Growth Factor 1 in the Aged Olfactory Epithelium. Front Aging Neurosci (2018)) licensed under a CC-BY license.

Immunohistochemistry-Paraffin: GAP-43 Antibody [NB300-143] - Posterior MOE sections at approximately the same region where EOG was recorded were obtained from control and Skn-1a-/- mice exposed to either water or chemicals for 2 wks. The sections were immunoreacted with antibodies against GAP43 and OMP and stained with DAPI. Confocal images were taken from olfactory turbinate II. Similar morphology and marker expression were found in four groups of mice, indicating there was no obvious tissue damage in both control and Skn-1a-/- mice after chemical exposure in the posterior MOE regions where EOG recordings were performed. Scale bar: 50 um. Image collected and cropped by CiteAb from the following publication (//eneuro.sfn.org/lookup/doi/10.1523/ENEURO.0135-17.2017), licensed under a CC-BY license.

Immunocytochemistry/Immunofluorescence: GAP-43 Antibody [NB300-143] - Cortical neuron-glial cell culture from E20 rat stained with rabbit pAb to GAP43, dilution 1:2,000 in green, and costained with mouse mAb to vimentin, dilution 1:2,000, in red. Blue: DAPI staining of nuclear DNA. GAP43 antibody labels protein expressed in the axonal membrane of neuronal cells, while vimentin antibody stains intermediate filaments in fibroblasts and other non-neuronal cells.

Immunocytochemistry/Immunofluorescence: GAP-43 Antibody [NB300-143] - Rat E18 mixed neuron/glia cultures with rabbit GAP43 (red) and 5B10, mouse monoclonal to MAP-tau (green).

Western Blot: GAP-43 Antibody [NB300-143] - Western blots of homogenate of cow cerebellum stained with RPCA-GAP-43 . A prominent band running at ~43kDa represents the full length GAP-43.

Immunocytochemistry/Immunofluorescence: GAP-43 Antibody [NB300-143] - Immunofluorescence of GAP-43 (green), a molecular marker of neurite outgrowth, demonstrates intense staining in overexpressing wild-type PS-1 (E) PC-12 cells. (Teo, et al, 2005)

Immunocytochemistry/Immunofluorescence: GAP-43 Antibody [NB300-143] - Mixed neuron-glial cultures stained with RPCA-GAP43 (red), blue is DNA staining.

Western Blot: GAP-43 Antibody [NB300-143] - Silencing TFAP4 induces neuroblastoma cell differentiation. a Morphology of neuroblastoma cells after silencing TFAP4. Cells were grown in culture for 8 days, with 1 μg/ml doxycycline (shRNA induced) or without doxycycline. b Neurites # per field, & neurite length (pixels) were quantified with or without doxycycline. Mean ± std dev. *, P < 0.05; **, P < 0.01, ****, P < 0.0001. cGAP43 expression level (qRT-PCR) & protein level (western blot) in neuroblastoma cells. Gene expression was measured by quantitative PCR 4 days after induction of shRNA against TFAP4. Protein samples for western blot were collected from MYCN-amplified cells that were cultured with or without doxycycline (1 μg/ml) for 6 days Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/29880876), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Immunocytochemistry/ Immunofluorescence: GAP-43 Antibody [NB300-143] - LAMP1 increases in SDC-null corneas 14 days after trephine wound. Representative 3D images rotated to generate cross-sectional views show the localization of GAP43 (green), beta III tubulin (red), & LAMP1 (blue) in WT (top) & SDC1-null (bottom) corneas. These images show staining within a 0.5-μm cross-sections. Data indicate that axon fragments are being degraded (arrows). Representative INTs (*) & SBNs (#) have been highlighted & enlarged 3-fold. When LAMP1 expression within apical & basal cell layers 14 days after trephine injury is quantified & compared with unwounded controls (Fig. 2B), LAMP1 increases over 3-fold in SDC1-null corneas but remains the same in WT corneas. Scale bar: 10 μm. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/28973369), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: GAP-43 Antibody [NB300-143] - Obesity & diabetes led to white adipose tissue neuropathy.The BTBR ob/ob (MUT) model of obesity & diabetes was compared to BTBR +/+ wild-type (WT) for body weight measurements (a), & adiposity (b). Body & tissue weight data were analyzed by two-tailed Student’s t-test. Von Frey tactile allodynia analysis was performed on MUT & WT animals to determine onset of peripheral neuropathy (c). Von Frey data was analyzed by ANOVA with Sidak’s post hoc test. For (a-c), all males; WT N = 8, 12–20 weeks old; MUT N = 6, 12–24 weeks old. Protein levels of PGP9.5 (d), as well as TH (e) in inguinal scWAT of the MUT & WT mice were measured by western blotting. For (e), lane 5 was excluded from analyses due to uneven resolution of housekeeper. For (d-e), all males; WT N = 5, 12–20 weeks old & MUT N = 4, 12–20 weeks old. Protein expression of PGP9.5 (f), TH (g), PSD95 (h), & GAP43 (i) in inguinal scWAT of 12–25 weeks old WT, 12 week old MUT & 24–28 week old MUT was measured by western blotting. All males, N = 3 per group. Western blot data were normalized to either beta -Tubulin or Cyclophilin B, band intensity were quantified in Image J, & analyzed by two-tailed Student’s t-test. Error bars are SEMs. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31509546), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Immunocytochemistry/ Immunofluorescence: GAP-43 Antibody [NB300-143] - Intraepithelial nerve terminals extension into the apical most cell layers increases in SDC1-null corneas after trephine injury. Representative 3D images rotated to generate cross-sectional views show the localization of beta III tubulin (red) & GAP43 (green) at 4, 14, & 28 days after trephine wounding in WT & SDC1-null corneas. Punctate GAP43 is increased within the epithelium in SDC1-null compared with WT corneas at 14 days (*). beta III tubulin+ & GAP43+ INTs in the apical most cell layers were quantified as a function of time after trephine injury & normalized relative to control (presented in Fig. 2A). Asterisks within bars indicate differences that are significant relative to unwounded controls; asterisks between bars indicate significant differences between time points. In WT corneas, the numbers of beta III tubulin+ & GAP43+ INTs extending apically decrease relative to controls at 28 days for beta III tubulin+ INTs & at 4 & 28 days for GAP43+ INTS, in SDC1-null corneas, both beta III tubulin+ & GAP43+ INTs increase at all time points assessed. Scale bar: 25 μm. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/28973369), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Immunocytochemistry/ Immunofluorescence: GAP-43 Antibody [NB300-143] - Differences in INTs & LAMP1 localization in WT & SDC1-null adult corneas. Representative high-resolution confocal 3D images rotated as indicated in the cartoon to the left were used to generate cross sectional views to show the localization of beta III tubulin (red) & GAP43 (green) in intraepithelial nerve terminals in control WT & SDC1-null corneas. The images shown in (A) project through 135 μm of tissue, images in (B) project through 0.5 μm of tissue. (A) Intraepithelial corneal nerves are shown to be linear, arise from the subbasal nerves (SBNs), & project apically. Quantitation of beta III tubulin & GAP43 within apical & basal layers of the corneal epithelium reveals that WT corneas have significantly more INTs in both basal & apical cell layers compared with SDC1-null corneas. Although SDC1-null corneas have fewer INTs, they are equally capable of extending toward the apical most cell layers. (B) In the 0.5-μm cross-sectional slices through the tissue, INTs appear discontinuous. In addition to beta III tubulin & GAP43, LAMP1 is shown in blue. LAMP1 is a lysosomal marker; co-localization of GAP43 and/or beta III tubulin within corneal epithelial cell lysosomes indicate that axon fragments have been phagocytozed & are being degraded (arrows). The sites indicated by the asterisks have been digitally enlarged 3-fold. LAMP1 was quantified in WT & SDC1-null corneas. Data show that cells within the apical layers express more LAMP1 compared with basal cells in both genotypes of mice. In addition, WT corneas express 2- to 3-fold more LAMP1 in apical & basal layers compared with SDC1-null corneas. Scale bar: 10 μm. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/28973369), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Reactivity:

Hu, Mu, Rt, Po, Bv, Ca, Ch, Dr, Eq, Pm

Species Glossary

Reactivity: Hu, Mu, Rt, Po, Bv, Ca, Ch, Dr, Eq, Pm

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	NB300-143AF350
Alexa Fluor 405	NB300-143AF405
Alexa Fluor 488	NB300-143AF488
Alexa Fluor 532	NB300-143AF532
Alexa Fluor 594	NB300-143AF594
Alexa Fluor 647	NB300-143AF647
Alexa Fluor 700	NB300-143AF700
Alexa Fluor 750	NB300-143AF750
Allophycocyanin	NB300-143APC
Biotin	NB300-143B
CoraFluor 1	NB300-143CL1
DyLight 350	NB300-143UV
DyLight 405	NB300-143V
DyLight 488	NB300-143G
DyLight 550	NB300-143R
DyLight 594	NB300-143DL594
DyLight 650	NB300-143C
DyLight 680	NB300-143FR
DyLight 755	NB300-143IR
FITC	NB300-143F
HRP	NB300-143H
Janelia Fluor 525	NB300-143JF525
Janelia Fluor 549	NB300-143JF549
Janelia Fluor 646	NB300-143JF646
Janelia Fluor 669	NB300-143JF669
PE	NB300-143PE
PerCP	NB300-143PCP
mFluor Violet 450 SE	NB300-143MFV450
mFluor Violet 500 SE	NB300-143MFV500
mFluor Violet 610 SE	NB300-143MFV610

Available Formulations

Formulation	Catalog #	Availability	Price
BSA Free	NB300-143SS

compare

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

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

compare

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

NB100-56113

Caspase-3 Antibody - (active/cleaved) - BSA Free

(81 Publications)

0.05 ml

NB100-56113

Western Blot: Caspase-3 Antibody - (active/cleaved) [NB100-56113] - Cell apoptosis was detected by flow cytometric analysis, and the percentage of apoptotic cells transfected with miR-200c inhibitor or NC inhibitor and treated with AngII or PBS for 48 h was determined. Image collected and cropped by CiteAb from the following publication (onlinelibrary.wiley.com/doi/abs/10.1111/jcmm.14135), licensed under a CC-BY license.

Immunohistochemistry-Paraffin: Caspase-3 Antibody - (active/cleaved) [NB100-56113] - Dog ischemic brain stained for Active/Cleaved Caspase-3 expression using Caspase-3 Antibody - (active/cleaved)( NB100-56113) at 1:2000. Staining is seen in the nuclei of dying neurons (black arrow) but not in the morphologically normal nuclei (open arrows). Caspase-3 expression in the nucleus is considered to be a marker of active/caspase-3 expression and apoptosis. Hematoxylin-eosin counterstain.

Immunohistochemistry-Paraffin: Caspase-3 Antibody - (active/cleaved) [NB100-56113] - Irradiated mouse spleen stained for Active/Cleaved Caspase-3 expression using Caspase-3 Antibody - (active/cleaved) (NB100-56113) at 1:2000. Staining is seen in the nuclei of a subset of the cell population. Caspase-3 expression in the nucleus is considered to be a marker of active/caspase-3 expression and apoptosis. Hematoxylin-eosin counterstain.

Antidepressants-mediated effect on cellular protein content. HT-22 cells were treated with antidepressants for 48 and 96 h and densitometry analysis of NF-kappa B (b), p16 (c), p21 (d), p27 (e), p53 (f), TRF1 (g), TRF2 (h), calnexin (i), NuMa (j), cleaved caspase 3 (k), Bcl-2 (l) was evaluated. Representative Western Blots are presented (a). Bars indicate SD, n = 3, ***/^^^p < 0.001, **/^^p < 0.01, */^p < 0.05, no indication—no statistical significance (one-way ANOVA and Dunnett’s a posteriori test)

Immunohistochemistry: Caspase-3 Antibody - (active/cleaved) [NB100-56113] - Pathology in DOX treated acute & recovery phase mice. Regions of myofiber loss & frank replacement fibrosis were noted, most commonly in atria (A, acute phase), & rarely in ventricles (D, recovery phase). These areas were accompanied by macrophage infiltration (B, E) & myofibroblast proliferation (C) consistent with fibroplasia. Rare myofibers were matrix metalloproteinase 2 (F, recovery phase animal) or caspase-3 positive (G, acute phase animal). Reticulin staining (A, D); Immunohistochemistry: Iba 1(B, E; macrophages), alpha SMA (C), MMP-2 (F) & cleaved caspase -3 (G) Bar = 100µm (A-C); 50µm (D-F); 20µm (G). Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31263061), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: Caspase-3 Antibody - (active/cleaved) [NB100-56113] - Antidepressants-mediated effect on cellular protein content. HT-22 cells were treated with antidepressants for 48 & 96 h & densitometry analysis of NF-kappa B (b), p16 (c), p21 (d), p27 (e), p53 (f), TRF1 (g), TRF2 (h), calnexin (i), NuMa (j), cleaved caspase 3 (k), Bcl-2 (l) was evaluated. Representative Western Blots are presented (a). Bars indicate SD, n = 3, ***/^^^p < 0.001, **/^^p < 0.01, */^p < 0.05, no indication—no statistical significance (one-way ANOVA & Dunnett’s a posteriori test) Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31278507), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Immunocytochemistry/ Immunofluorescence: Caspase-3 Antibody - (active/cleaved) [NB100-56113] - Morphological changes & expression of key apoptosis-related molecules in 4T1 cells after DE-EDCP treatment(A) Morphological changes of 4T1 cells exposed to various concentrations of DE-EDCP for 24h. (B) Immunofluorescence staining for Bcl-2 (green), Bax (green) & cleaved caspase-3 (green) together with DNA staining with DAPI (blue) in 4T1 cells incubated with DE-EDCP or cisplatin (31.25 μM) for 24h, as well as in untreated cells (magnification at x200). (C) mRNA expression of Bcl-2, Bax & caspase-3 quantified by RT-PCR in 4T1 cells after DE-EDCP 24h treatment. DE-EDCP treatment markedly increased the expression of Bax & caspase-3 mRNA & decreased the expression of Bcl-2 mRNA in 4T1 cells. beta -actin mRNA was used as an internal control. Data points are represented by the expression ratio & mean±SD fold of control in 4T1 cells. (* Bcl-2-: DE-EDCP vs. untreated p=0.03; DE-EDCP vs. cisplatin p=0.006; cislatin vs. untreated p=0.001; Bax-: DE-EDCP vs. untreated p=0.011; cislatin vs. untreated p=0.009; caspase-3-: DE-EDCP vs. untreated p=0.015; DE-EDCP vs. cisplatin p=0.021) Image collected & cropped by CiteAb from the following publication (//www.oncotarget.com/lookup/doi/10.18632/oncotarget.25610), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Reactivity:

Hu, Mu, Rt, Ma

Species Glossary

Reactivity: Hu, Mu, Rt, Ma

Applications:

, , , , ,

Applications: , , , , ,

Host:

Rabbit Polyclonal

Host: Rabbit Polyclonal

Alt Catalog#

IMG-5700

Alt Catalog# IMG-5700

Sizes:

Sample Size Available

Sizes: Sample Size Available

Conjugate:

Unconjugated

Validated by:

Validated by:

Available Formulations

Formulation	Catalog #	Availability	Price
BSA Free	NB100-56113SS

compare

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

NB300-223

Vimentin Antibody

(6 Reviews)

(83 Publications)

0.1 ml

NB300-223

Immunocytochemistry/Immunofluorescence: Vimentin Antibody [NB300-223] - Human A7 cells. Cells were fixed with 10% formalin and permeabilized with 0.1% TritonX-100. After blocking, cells were incubated with primary antibody (1:600) at 4C O/N followed with Alexa Fluor 488 labeled secondary antibody and counterstained with DAPI and Phalloidin for nuclei and F-actin respectively. Imaged with Leica TCS SP5 confocal microscope. ICC/IF image submitted by a verified customer review.

Immunohistochemistry: Vimentin Antibody [NB300-223] - Increased numbers of differentiating NSPCs in SVZ of G93A-SOD1 brain. Confocal microscopy images of dorsal and ventral regions of SVZ in G93A-SOD1 and Wt-SOD1 brain at postnatal week 18, stained for nestin (green), GFAP (red), and vimentin (blue). Scale bar = 50 um. Image collected and cropped by CiteAb from the following publication (//www.molecularbrain.com/content/8/1/5), licensed under a CC-BY license.

Immunocytochemistry/Immunofluorescence: Vimentin Antibody [NB300-223] - Comparative analysis of epithelial and mesenchymal markers expressions. Fluorescence immunocytochemistry staining for E-cadherin (green), N-cadherin (red) and vimentin (cyan) was performed on esophageal cancer cells under static and microfluidic flow conditions at different time points. Image collected and cropped by CiteAb from the following publication (//www.nature.com/articles/srep38221), licensed under a CC-BY license.

Immunocytochemistry/Immunofluorescence: Vimentin Antibody [NB300-223] - Analysis of HeLa cell culture. Antibody at 1:10,000 in green, and costained with mouse mAb to actin, dilution 1:500 in red. The blue is DAPI staining of nuclear DNA. The vimentin antibody stains the intermediate filament network while the actin antibody labels the submembranous cytoskeleton, stress fibers, and bundles of actin associated with cell adhesion sites.

Immunohistochemistry-Frozen: Vimentin Antibody [NB300-223] - 10 um Cryosections from PFA fixed murine brain acute slices stained with Vimentin antibody (1:600) and Alexa Fluor 488 anti chicken IgG. Antibody showed specific staining, also of blood vessels. IHC-Fr image submitted by a verified customer review.

Immunohistochemistry-Frozen: Vimentin Antibody [NB300-223] - Infarcted mouse heart frozen sections stained with vimentin antibody at 1:200. Secondary antibody at 1:500. Fixation with 4% PFA. IHC-Fr image submitted by a verified customer review.

Immunocytochemistry/ Immunofluorescence: Vimentin Antibody [NB300-223] - Increased numbers of differentiating NSPCs in SVZ of G93A-SOD1 brain. (A) Confocal microscopy images of dorsal & ventral regions of SVZ in G93A-SOD1 & Wt-SOD1 brain at postnatal week 18, stained for nestin (green), GFAP (red), & vimentin (blue). Scale bar = 50 μm. (B) Quantification of nestin-, GFAP-, & vimentin-positive cells in SVZ of G93A-SOD1 & Wt-SOD1 mice. Data are means ± SD of 3 mice per group. **p 20 days (PyMT-1099 LT) were injected orthotopically into mammary fat pads of NSG mice. The graph represents tumor growth in PyMT-1099 & PyMT-1099 LT group of mice. (B) Histological tumor sections from tumors of PyMT-1099 or PyMT-1099 LT cells described in (A) were stained with H&E to assess the morphology of primary tumors. Representative microphotographs are shown from tumors of 2 out of the 6 mice used in the experiment. (C) Immunofluorescence analysis was performed to assess the expression of the EMT markers FN1, VIM, E-CAD & N-CAD in tumors formed by PyMT-1099 or PyMT-1099 LT cells in the experiment described in (A). DAPI was used as a nuclear counterstain. Representative pictures are shown from tumors of 2 out of the 6 mice used in the experiment. Scale bar, 100 μm. (D) The graph represents the number of lung metastases formed in NSG mice orthotopically transplanted with PyMT-1099 or PyMT-1099 LT cells; n = 6. (E) The graph represents the number of lung metastases formed in NSG mice injected with PyMT-1099 or PyMT-1099 LT cells through the tail vein; n = 6. The mice were sacrificed 8 weeks post-injection, & lungs were resected for the analysis of cancer cell colonization/ metastases formation. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/30108334), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

DNM1P35 promotes EMT of ovarian cancer cells. (A,B) The expression of EMT markers were assessed by qPCR (A) and Western blotting (B) in SK-OV-3 and OVCAR-3 cells expressing shCTRL and shDNM1P35. (C,D) The expression of EMT markers were assessed by qPCR (C) and Western blotting (D) in SK-OV-3 and OVCAR-3 cells expressing vector and DNM1P35. (E,F) The expression of EMT markers were assessed by qPCR (E) and Western blotting (F) in SK-OV-3 and OVCAR-3 cells expressing shCTRL and shZEB1. (G,H) The expression of EMT markers were assessed by qPCR (G) and Western blotting (H) in SK-OV-3 and OVCAR-3 cells expressing shCTRL and shZEB1 and overexpression of DNM1P35. ***, p < 0.001, ****, p < 0.0001. ns, not significant. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/39732940), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

DNM1P35 targets miR-326 to promote ovarian cancer progression and EMT. (A) The potential target of DNM1P35 was predicted by the STAR (database. (B) Dual-luciferase activity assay in HEK293T cells expressing WT and MUT DNM1P35 luciferase reporter and treated with miR-NC or miR-326. (C) The expression of ZEB1 in SK-OV-3 and OVCAR-3 cells transfected with miR-NC and miR-326 was determined by qPCR. (D) The expression of EMT markers in SK-OV-3 and OVCAR-3 cells transfected with miR-NC and miR-326 was determined by Western blotting. (E) The growth of ovarian cancer cells was assessed by CCK-8 assay. (F) SK-OV-3 and OVCAR-3 cell colonies were stained by crystal violet. (G) Migration of SK-OV-3 and OVCAR-3 cells was measured by wound healing assay. (H) Invasion of SK-OV-3 and OVCAR-3 cells was measured by trans-well assay. ***, p < 0.001. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/39732940), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Reactivity:

Hu, Mu, Rt, Po, Bv, Ca, Ch, Eq

Species Glossary

Reactivity: Hu, Mu, Rt, Po, Bv, Ca, Ch, Eq

Applications:

, ,

Applications: , ,

Host:

Chicken Polyclonal

Host: Chicken Polyclonal

Sizes:

Sample Size Available

Sizes: Sample Size Available

Conjugate:

Unconjugated

compare

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

NBP2-13075

beta Amyloid Antibody (MOAB-2) - BSA Free

(2 Reviews)

(75 Publications)

0.1 ml

NBP2-13075

IHC analysis of beta Amyloid on normal mouse brain (left) and 5xFAD mouse brain (right) using DAB with hematoxylin counterstain. The MOAB-2 antibody was used at 1:20 on normal mouse brain and at 1:400 on 5xFAD mouse brain.

Analysis of beta Amyloid (MOAB-2) antibody in (1) 100 pmole beta Amyloid 42, (2) 5xFAD mouse brain homogenate Repetition 1 and (3) 5xFAD mouse brain homogenate Repetition 2.

Western blot analysis in cell lysates from HEK-APP SWE/BACE1 cells probed with an antibody against the C-terminus of APP (Lanes 1 and 2) and beta Amyloid (MOAB-2, Lanes 3 and 4). Beta Amyloid (MOAB-2) does not detect APP (from PMID: 22423893).

IHC analysis of a formalin fixed paraffin embedded tissue section of human brain (Alzheimers disease, hippocampus) using 1:200 dilution of anti-beta Amyloid antibody (clone MOAB-2). The staining was developed with HRP labeled anti-mouse secondary antibody and DAB reagent, and nuclei of cells were counter-stained with hematoxylin. This beta Amyloid antibody specifically stained the cells with Abeta 42/ Abeta aggregates while the normal cells were negative for abeta peptide.

Immunofluorescent detection of beta Amyloid with MOAB-2 in the subiculim of 1-, 2- and 4- month old 5xFAD mice. Scale bar 20 um (from PMID: 22423893).

A plaque load in neocortex and hippocampus in APP/PS1 mice exposed to differential housing. Representative 10x MOAB-2 staining in hippocampus of APP/PS1 mice for each housing group. Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/28584278/) licensed under a CC-BY license.

IHC analysis of a formalin fixed paraffin embedded tissue section of human brain (Alzheimers disease, hippocampus) using 1:40 dilution of anti-beta Amyloid antibody (clone MOAB-2). The staining was developed with HRP labeled anti-mouse secondary antibody and DAB reagent, and nuclei of cells were counter-stained with hematoxylin. This beta Amyloid antibody specifically stained the cells with Abeta 42/ Abeta aggregates while the normal cells were negative for abeta peptide.

Mouse brain (cerebral cortex). Red: MOAB-2 antibody staining, Blue: DAPI. Zeiss LSM800, 40x. Image from verified customer review.

Immunocytochemistry/ Immunofluorescence: beta Amyloid Antibody (MOAB-2) - BSA Free [NBP2-13075] - No difference in A beta plaque load between propofol (n = 8) & vehicle (n = 6) treated APP/PS1 mice. a An example image of A beta plaque immunoreactivity in the cortex of an APP/PS1 mouse following repeated propofol exposure. b A representative image of A beta plaque immunolabeling the cortex of an APP/PS1 mouse following treatment with vehicle. c Bar graph showing the percentage of the cortex occupied by A beta plaques in propofol & vehicle treated APP/PS1 mice. d Bar graph showing the average size (μm2) of A beta plaques in the cortex of APP/PS1 in the propofol & vehicle treatment groups. e Bar graph showing the average density of A beta plaques (/μm2) in the cortex of propofol & vehicle exposed APP/PS1 mice. All data is shown as mean ± SEM. Scale bar = 500 μm Image collected & cropped by CiteAb from the following publication (//bmcanesthesiol.biomedcentral.com/articles/10.1186/s12871-018-0509-5), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Murine brain cryosections stained with primary MOAB-2 antibody followed by a secondary donkey anti-mouse antibody. Image from a verified customer review.

Reactivity:

Hu, Mu, Rt, Ba, Pm

Species Glossary

Reactivity: Hu, Mu, Rt, Ba, Pm

Applications:

, , , , , , ,

Applications: , , , , , , ,

Host:

Mouse Monoclonal

Host: Mouse Monoclonal

Sizes:

Sample Size Available

Sizes: Sample Size Available

Conjugate:

Unconjugated

Available Conjugates:

Conjugate	Catalog #	Availability	Size	Price
Alexa Fluor 350	NBP2-13075AF350
Alexa Fluor 405	NBP2-13075AF405
Alexa Fluor 488	NBP2-13075AF488
Alexa Fluor 532	NBP2-13075AF532
Alexa Fluor 647	NBP2-13075AF647
Alexa Fluor 700	NBP2-13075AF700
Alexa Fluor 750	NBP2-13075AF750
Allophycocyanin	NBP2-13075APC
Biotin	NBP2-13075B
CoraFluor 1	NBP2-13075CL1
DyLight 350	NBP2-13075UV
DyLight 405	NBP2-13075V
DyLight 488	NBP2-13075G
DyLight 550	NBP2-13075R
DyLight 594	NBP2-13075DL594
DyLight 650	NBP2-13075C
DyLight 680	NBP2-13075FR
DyLight 755	NBP2-13075IR
FITC	NBP2-13075F
HRP	NBP2-13075H
Janelia Fluor 525	NBP2-13075JF525
Janelia Fluor 549	NBP2-13075JF549
Janelia Fluor 646	NBP2-13075JF646
Janelia Fluor 669	NBP2-13075JF669
PE	NBP2-13075PE
PerCP	NBP2-13075PCP
mFluor Violet 450 SE	NBP2-13075MFV450
mFluor Violet 500 SE	NBP2-13075MFV500
mFluor Violet 610 SE	NBP2-13075MFV610

Available Formulations

Formulation	Catalog #	Availability	Price
BSA Free	NBP2-13075SS
Azide and BSA Free	NBP2-80594

compare

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

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

compare

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

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

compare

(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

PINK1 Antibody - BSA Free

Caspase-3 Antibody (31A1067) - (Pro and Active) - BSA Free

GAPDH Antibody - BSA Free

MAP2 Antibody - BSA Free

GAP-43 Antibody - BSA Free

GAPDH Antibody (6C5cc) - BSA Free

Caspase-3 Antibody - (active/cleaved) - BSA Free

Vimentin Antibody

beta Amyloid Antibody (MOAB-2) - BSA Free

GAPDH Antibody

GAPDH Antibody