Product Search for novus: Novus Biologicals

NB300-221

GAPDH Antibody (1D4)

(19 Reviews)

(411 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 80% of endogenous Sin1 while levels of myc-FL Sin1 associated with Rictor are comparable with endogenous Sin1 levels. Image collected and cropped by CiteAb from the following open publication (//www.oncotarget.com/lookup/doi/10.18632/oncotarget.20086), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Immunodepletions and the effects of RNases and various transcription inhibitors on chromosome condensation and cell cycle state.(A) Western blot for CAP-E, XPB, and Tubulin in Mock or CAP-E depleted extracts. Dilution series of Mock-depleted extracts was used to calculate the % depletion of CAP-E using quantitative fluorescence. (B) 1% agarose gel stained with SYBR safe stain showing RNase A dependent removal of total RNAs from high-speed supernatant egg extracts. (C) Representative fluorescence images of chromatid assembly at steady state (180 min after sperm addition) in the presence of indicated buffers and enzymes. See Materials and methods for details. Note that the high salt in the RNase H buffer causes morphological changes to chromatids regardless of activity. Mean condensation parameters for each condition are indicated in lower left corner of each image. (D) Western blot for XPB and Tubulin in IgG or XPB-depleted extracts. Dilution series of IgG-depleted extracts was used to calculate the % depletion of XPB using quantitative fluorescence. (E) Western blot for XPF, ERCC1, and Tubulin in IgG or ERCC1-depleted extracts. Dilution series of IgG-depleted extracts was used to calculate the % depletion of ERCC1 and XPF using quantitative fluorescence. (F) Representative fluorescence images of chromatid assembly at steady state (180 min after sperm addition) in the presence of DMSO, 30 μM CDK7 inhibitor THZ1, or 30 μM THZ1 and 50 μM triptolide (TPL). (G) Triptolide does not affect CDK1 activation or maintenance of M phase. Western blot for CDK1 T161ph, histone H3T3ph, and Tubulin in M phase HSS extracts in the presence of DMSO or 50 μM triptolide. Both CDK1T161ph (a CDK7 substrate) and H3T3ph are only highly phosphorylated in M phase, and their appearance is not affected by triptolide treatment.Figure 1—figure supplement 1—source data 1.Source data for Figure 1—figure supplement 1A, B,D, E, G.Source data for Figure 1—figure supplement 1A, B,D, E, G. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/35293859), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Activation of the ATM‐Chk2‐p53 pathway upon CDDP treatmentAConfocal images showing the basal region of organ of Corti cultures treated with either culture medium alone or medium containing 10 μM CDDP for 1 day and immunolabeled for myosin 7A (red) and p‐ATM (green). Scale bar = 15 μm.BHigher magnification images showing representative OHC and IHC nuclei from control and CDDP‐exposed cells. Scale bar = 5 μm.CHistograms displaying green fluorescent signal intensity of x‐projections of OHC and IHC nuclei from control and CDDP‐exposed cells.DQuantification analysis of p‐ATM foci numbers in both OHCs and IHCs exposed to either culture medium alone (light blue and red lines for OHCs and IHCs, respectively) or 10 μM CDDP (blue and red lines for OHCs and IHCs, respectively; n = 50 nuclei per condition and per time point). Data are expressed as mean ± SEM. One‐way ANOVA test followed by post hoc Tukey's test (**P < 0.008, ***P = 0.00005; CDDP‐exposed OHCs versus CDDP‐exposed IHCs).EHigher magnification confocal and 3D images showing the co‐localization of p‐ATM foci (green) with 53BP1 foci (red) in an OHC nucleus from the basal region of the organ of Corti culture treated with 10 μM CDDP for 1 day. Scale bar = 5 μm.FConfocal images showing the basal region of organ of Corti cultures treated with either culture medium alone or medium containing 10 μM CDDP for 1 day and immunolabeled for myosin 7A (red) and p‐Chk2 (green). Scale bar = 15 μm.GHistograms of green fluorescent signal intensity from OHC and IHC nuclei of a CDDP‐treated organ of Corti explant.HQuantification of Chk2‐positive nuclei in both IHCs (red bars) and OHCs (blue bars) from control and CDDP‐treated organ of Corti cultures (n = 50 nuclei per condition and per time point). Data are expressed as mean ± SEM. Kruskal–Wallis test followed by post hoc Dunn's test (*P = 0.045, ***P = 0.0002; CDDP‐exposed IHCs versus control IHCs, CDDP‐exposed OHCs versus control OHCs).IRepresentative Western blots using antibodies against p‐p53 (serine 15), p53, and beta ‐actin in control and 10 μM CDDP‐exposed whole cochlear extracts.J, KHistograms representing the levels of total p53 protein (J) and p53 phosphorylation (K) in control (gray bars) and CDDP‐exposed cochleae (green bars; n = 6 cochleae per condition and per time point). Actin served as a loading control. Data are expressed as mean ± SEM. One‐way ANOVA test followed by post hoc Tukey's test (J: *P ≤ 0.023; K: *P = 0.032, **P = 0.007, ***P ≤ 0.0008; cochleae at the different times after CDDP exposure versus control 12 h).Data information: All experiments were performed in triplicate. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/27794029), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Reactivity:

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

Species Glossary

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

Applications:

, , , , , , ,

Applications: , , , , , , ,

Host:

Mouse Monoclonal

Host: Mouse Monoclonal

Sizes:

Sample Size Available

Sizes: Sample Size Available

Conjugate:

Unconjugated

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NBP1-04676

PGC1 alpha Antibody - BSA Free

(11 Reviews)

(261 Publications)

0.1 ml

NBP1-04676

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

HeLa cells were fixed in 4% paraformaldehyde for 10 minutes and permeabilized in 0.5% Triton X-100 in PBS for 5 minutes. The cells were incubated with anti-PGC1 alpha Antibody NBP1-04676 at 2 ug/ml overnight at 4C and detected with an anti-rabbit Dylight 488 (Green) at a 1:1000 dilution for 60 minutes. Nuclei were counterstained with DAPI (Blue). Cells were imaged using a 100X objective and digitally deconvolved.

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

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

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

Total protein from human adipose and skeletal muscle tissue, HeLa and A431 cells lines was separated on a 7.5% gel by SDS-PAGE, transferred to PVDF membrane and blocked in 5% non-fat milk in TBST. The membrane was probed with 2.0 ug/mL PGC1 alpha Antibody (Molecular weight: 91 KDa) in 1% non-fat milk in TBST and detected with an anti-rabbit HRP secondary antibody using chemiluminescence

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

HeLa cells were fixed for 10 minutes using 10% formalin and then permeabilized for 5 minutes using 1X TBS + 0.5% Triton X-100. The cells were incubated with PGC1 alpha Antibody [NBP1-04676] at a 1:200 dilution overnight at 4C and detected with an anti-rabbit DyLight 488 (Green) at a 1:500 dilution. Alpha tubulin (DM1A) [NB100-690] was used as a co-stain at a 1:1000 dilution and detected with an anti-mouse DyLight 550 (Red) at a 1:500 dilution. Nuclei were counterstained with DAPI (Blue). Cells were imaged using a 40X objective.

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

An intracellular stain was performed on HeLa cells with NBP1-04676AF647 (blue) and a matched isotype control (orange). Cells were fixed with 4% PFA and then permeabilized with 0.1% saponin. Cells were incubated in an antibody dilution of 2.5 ug/mL for 30 minutes at room temperature. Both antibodies were conjugated to Alexa Fluor 647.

An intracellular stain was performed on HepG2 cells with PGC1 alpha Antibody and a matched isotype control. Cells were fixed with 4% PFA and then permeablized with 0.1% saponin. Cells were incubated in an antibody dilution of 2.5 ug/mL for 30 minutes at room temperature, followed by Rabbit IgG (H+L) Cross-Adsorbed Secondary Antibody.

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

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

Feeding the diabetes mellitus (DM) mice with the RSV-enriched diet improved mitochondrial biogenesis in the quadriceps muscle. A) Representative western blots using antibodies against nuclear respiratory factor (NRF-1), ATP synthase, H+ transporting, mitochondrial F1 complex, beta polypeptide (ATP5B), cytochrome c oxidase subunit IV (Cox IV), peroxisome proliferator-activated receptor-gamma coactivator 1-alpha (PGC-1alpha), and GAPDH. Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/29578301), licensed under a CC-BY licence.

Mitochondrial content and biogenesis. (d) Immunoblot analysis of PGC1alpha in MEFs (n = 7; t = 5.764; df = 6). Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/28970491), licensed under a CC-BY licence.

Atg7 deficiency in vascular smooth muscle cells (VSMCs) alters mitochondrial quality control and enhances apoptosis. c) Western blot analyses of the expression of TFEB and PGC-1-alpha proteins in aortic VSMCs isolated from Atg7+/+Tagln-Cre+, ApoE-/- and Atg7F/FTagln-Cre+, ApoE-/- mice after 10 weeks of HFD. Cells were incubated either with or without oxidized LDL (200 ug ApoB/mL) for 8 h. beta-Actin was used as the loading control. The graph represents the densitometric analysis of the expression level of TFEB and PGC-1-alpha proteins. The data are expressed as mean +/- SEM of four independent experiments from different primary VSMC cultures. *P 12 in each group. (B) Western blot images using S100 beta , tubulin beta‐3, and beta ‐actin antibodies to total protein lysate in hippocampal area. The statistical results of internal standardized S100 beta / beta ‐tubulin ratio by beta ‐actin levels relative to young adult wild‐type C57BL/6J. White and black bars indicate the wild‐type C57BL/6J and Tet‐mev‐1 mice, respectively. Data are expressed as mean ± SD; *P 12 in each group. (C) Micrographs of immunohistochemical analysis on paraffined hippocampal tissue sections using GFAP and S100 beta antibody. Brown cells indicate GFAP‐stained astrocytes. Scale bar = 100 μm. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/27623715), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

At the time of second passage, vessels in successfully growing xenografts of four different tumor types surveyed were of murine origin: A-C Colon; D-F Lung; G-I Pancreatic; J-L Renal Cell Carcinoma. For each tumor type, a representative section of an original patient specimen labeled with anti-huCD31 is shown (A, D, G, J). For each tumor, sections of the first passage xenografted tumor when it was resected are also shown; while no huCD31(+) vessels were identified in the xenografts (B, E, H, K), msCD34(+) vessels were abundant (C, F, I, L). (bars = 50 μ). Image collected and cropped by CiteAb from the following open publication (//translational-medicine.biomedcentral.com/articles/10.1186/1479-5876-11-110), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Knockdown of autophagy-related gene 5 (ATG5) inhibits trehalose-induced autophagy in normal human primary airway epithelial cells.Normal human tracheobronchial epithelial cells were transfected with Naito1 chimera RNAi (control siRNA) or ATG5 chimera siRNA (ATG5 siRNA). Twenty-four hours after siRNA transfection, cells were treated with medium or trehalose (TRE, 100 mM) for 48 h. ATG5 protein (A) and LC3 I and LC3 II proteins (B) were examined by Western blot analysis with GAPDH protein used as loading control. The representative Western blot picture was shown from 2 independent experiments with each being performed in triplicate wells. Image collected and cropped by CiteAb from the following open publication (//dx.plos.org/10.1371/journal.pone.0124524), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

$Expression of ER stress associated protein and autophagy related protein in the C28I2 chondrocyte infected with Ad-ATG5 or Ad-ATG7. a The ATG5 and ATG7 mRNA level were analysed by RT-PCR in C28I2 cells. b Analysis of ATG5 and ATG7 mRNA level with Q-PCR in C28I2 cells. Ad-ATG5(a), Ad-ATG7(b). c The ATG5 protein expression was analysed by western blotting in the Ad-ATG5 infected C28I2 cells. The level of ATG5 was normalized to beta -actin. d The ATG7 protein expression was analysed by western blotting in the Ad-ATG7 infected C28I2 cells. The level of ATG7 was normalized to beta -actin. e The expression levels of LC3, P62, PERK, p-PERK, Nrf2 proteins after infected with Ad-ATG5 in C28I2 cells for 24 h by western blotting. The levels of related proteins were normalized to beta -actin. f The expression levels of LC3, P62, PERK, p-PERK, Nrf2 proteins after infected with Ad-ATG7 in C28I2 cells for 24 h by western blotting. The levels of related proteins were normalized to beta -actin. *P 100 mitochondria). Data analysis was performed by using one-way ANOVA (∗P 250 cells/chains per sample). c Representative whole-mount IF of adult Plzf-mC/CreER; Z/EG tubules D3 post-TAM (n = 2 mice). Arrowheads: PDX1+ As. Inset shows detail of indicated area. Scale bar, 50 μm. d Representative IF of adult WT testis sections (n = 4 mice). Insets: details of selected areas. EOMES+ GFR alpha 1+ (arrowheads) and EOMES− GFR alpha 1+ cells (bracket) are shown. Tubule stage is indicated. Scale bar, 50 μm. e Representative IF of adult Oct4-GFP testis section (n = 2 mice). Insets: immunostaining within indicated area. EOMES+ GFP− (arrowheads) and EOMES− GFP+ (bracket) spermatogonia are indicated. Asterisks: autofluorescent interstitium. Scale bar, 50 μm. f Representative flow cytometry of fixed and permeabilized testis cells from Oct4-GFP adults (n = 2). PLZF+ cells shown. g Representative IF of adult WT testis sections (n = 4 mice). Insets: immunostaining within indicated area. PDX1+ EOMES+ spermatogonia are indicated (arrowheads). Tubule stage is shown. Asterisk: autofluorescent interstitium. Scale bar, 50 μm. h Representative flow cytometry of fixed and permeabilized WT adult testis cells (n = 4). Mean numbers of EOMES+ and PDX1+ cells in PDX1+ and EOMES+ gates respectively are shown ± s.e.m. i Representative flow cytometry for KI67 in indicated PLZF+ populations of fixed and permeabilized adult WT testis cells (n = 4 mice). j Quantification of flow cytometry from i. Percentage of indicated PLZF+ fractions KI67+ . Horizontal bars: mean values (n = 4 mice). k Representative IF of adult WT testis sections demonstrating PDX1+ Aundiff localisation (arrowheads) within tubules (n = 4 mice). Asterisks: autofluorescent interstitium. Tubule stages are shown. Scale bar, 50 μm. l Quantification of spermatogonial localisation from k. Mean values ± s.e.m. are shown (n = 4 mice, 56–95 tubule sections per mouse). Significance vs. tubule-tubule localisation is indicated. m Representative IF of Id4IRES-GFP adult testis sections (n = 4 mice). Insets show immunostaining within indicated area. Arrowheads: PDX1+ EOMES+ GFP+ spermatogonia. Asterisk: PDX1low EOMES+ GFP+ cell. Tubule stage is shown. Scale bar, 50 μm. n Representative flow cytometry of indicated PLZF+ populations of fixed and permeabilized adult Id4IRES-GFP testis cells (n = 4 mice). Mean numbers of PDX1+ and EOMES+ Aundiff expressing GFP ± s.e.m. o Flow cytometry of Id4IRES-GFP testis cells as in n. PLZF+ fractions are shown. Mean numbers of PLZF+ GFP+ cells positive for EOMES and PDX1 are indicated ± s.e.m. (n = 4 mice). Significance was calculated by two-tailed Student’s t-test (***P < 0.001, ****P < 0.0001) Image collected and cropped by CiteAb from the following open publication (//www.nature.com/articles/s41467-018-04827-z), licensed under a CC-BY license. Not internally tested by Novus Biologicals.$

Reactivity:

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

Species Glossary

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

Applications:

, , , , , , , ,

Applications: , , , , , , , ,

Host:

Rabbit Polyclonal

Host: Rabbit Polyclonal

Sizes:

Sample Size Available

Sizes: Sample Size Available

Conjugate:

Unconjugated

Available Conjugates:

Validated by:

Validated by:

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

Available Formulations

Formulation	Catalog #	Availability	Price
BSA Free	NBP1-04676SS

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BC100-494

PINK1 Antibody - BSA Free

(13 Reviews)

(247 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+/+.

USP30 restricts basal pexophagy. H). Quantification of Keima-SKL

$The FANCD2 NLS is required for efficient FANCD2 and FANCI monoubiquitination and chromatin association.(A) FA-D2 cells stably expressing LacZ, FANCD2-WT, FANCD2-K561R, FANCD2-∆N57, FANCD2-∆N100 and FANCD2-3N were incubated in the absence and presence of 250 nM MMC for 18 h, and whole-cell lysates were immunoblotted with antibodies to FANCD2, V5, FANCI and alpha -tubulin. The FANCD2 and FANCI L/S ratios are the ratios of monoubiquitinated to nonubiquitinated protein, and were calculated by measuring protein band intensities using ImageJ image processing and analysis software (//rsb.info.nih.gov/ij/). (B and C) FA-D2 cells stably expressing FANCD2-WT, FANCD2-∆N57, FANCD2-∆N100 and FANCD2-3N were treated as above and cell pellets were fractionated into soluble (S) and chromatin-associated (C) fractions. Fractions were immunoblotted with antibodies against V5, FANCI, alpha -tubulin and H2A. W, unfractionated whole cell extract. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/24278431), licensed under a CC-BY license. Not internally tested by Novus Biologicals.$

Immunoblot analyses of protein expression for Nrf2 and antioxidant enzymes.A. Analysis of nuclear Nrf2 in young and old mice subjected to EES. In sedentary mice, Nrf2 protein levels were decreased significantly in young versus old mice. EES exacerbated the decrease of nuclear Nrf2 in old mice. Blots/values represent n = 4–6 from each group. *p10 embryos/sample). The blots were probed with antibodies against Lc3 and Actin as a loading control. Western blots were repeated at least three times with independent extracts. (C) Quantification of Lc3-II fold changes in WT and mutant embryos in absence or presence of Baf A1. Western blot band intensities were quantified by Lab Image. Data is combined from three independent experiments. (D) Representative confocal micrographs of GFP-Lc3 puncta present in the tail fin of optn+/+, optn delta 5n/ delta 5n, p62+/+ and p62 delta 37n/ delta 37n at 4 dpf. Scale bars, 10 μm. (E). Quantification of the number of GFP-Lc3 puncta in optn+/+, optn delta 5n/ delta 5n, p62+/+ and p62 delta 37n/ delta 37n larvae with and without Baf A1 treatment. Each larva was imaged at a pre-defined region of the tail fin (as indicated by the red boxed area in Fig3 A) (≥11 larvae/group). Results are accumulated from two independent experiments. ns, non-significant, *p 12 months) were injected i.v. with siScr or siMST. Twenty‐four hours after siRNA injection, a 70% PH was performed and remnant/regenerating liver tissue was harvested 40 h later. p.i. of the livers was calculated by IHC staining of Ki67‐positive hepatocytes and livers were classified as (−) non‐regenerating or (+) regenerating based on the percentage of positive cells. Non‐surviving animals were sacrificed before the 40‐h end time point. “n” indicates the number of animals per group.Ki67 immunostaining of the regenerating aged mice livers, 40 h post‐PH. Sections were scanned using 3DHistech Pannoramic MIDI Scanner and quantitated with Quant Center 2.0 software. p.i. values are provided on the image.Representative photomicrograph of an aged liver treated with siMST and stained with H&E and by IHC for CK19 and Ki67. Arrows indicate ductal regions with no signs of reaction or oval cell expansion.Quantitative RT–PCR analysis of RNA isolated from mouse liver for Foxm1B, Birc5 and Ccnb1 at 0 and 40 h post‐PH. Log2 fold change was calculated using non‐transfected/non‐resected mouse liver as a control. Representative results from a single experiment with n = 6 animals per group are shown. Paired, two‐tailed Student's t‐test was used to calculate the significant change in signals between liver tissues at the time of resection (0 h) compared to 40 h post‐PH.Percentage of Ki67‐positive hepatocytes in aged and aged + siMST 40 h post‐resection. Representative results from a single experiment with n = 6 independent aged animals for group are shown. Two‐tailed Student's t‐test was used to calculate the significance of percentage of positive hepatocytes of siMST‐treated animals compared to non‐treated controls.Endpoint liver weight was taken of the remnant lobe and expressed as a percentage to total body weight. Representative results from a single experiment with n = 6 independent animals for group expect for control group where n = 6 are shown. Estimated liver‐to‐body weight ratio before PH in mice = 3.85 ± 0.05 (SD). Unpaired, two‐tailed Student's t‐test was used to calculate the significance of each aged group in comparison with the control young group.Hepatocyte geometric diameter was determined (see Materials and Methods). Representative results from a single experiment with n = 3 independent animals per group. Unpaired, two‐tailed Student's t‐test was used to calculate the significant change in hepatocyte size in liver tissue with and without siMST 40 h post‐PH.Data information: Bars represent mean ± SD. Scale bars, 50 μm. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/27940445), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

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
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 549	BC100-494JF549
Janelia Fluor 646	BC100-494JF646
PE	BC100-494PE
PerCP	BC100-494PCP
mFluor Violet 450 SE	BC100-494MFV450
mFluor Violet 500 SE	BC100-494MFV500
mFluor Violet 610 SE	BC100-494MFV610

Available Formulations

Formulation	Catalog #	Availability	Price
BSA Free	BC100-494SS

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NBP2-12446

NLRP3/NALP3 Antibody - BSA Free

(4 Reviews)

(223 Publications)

0.2 ml

NBP2-12446

C-AR inhibited NLRP3 inflammasome activation in synovial tissue. NLRP3 protein expression in succinate-stimulated synovial fibroblasts. The results were derived from four independent experiments for immunohistochemistry staining and Western blot and expressed as the mean +/- SD. *p 0.05 versus the OA + Allopurinol group. Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/29358971), licensed under a CC-BY licence.

Lycium barbarum polysaccharides lessened the changes in expression of pyroptosis markers (NOD-like receptors protein 3 (NLRP3), caspase-1, and membrane N-terminal cleavage product of GSDMD (GSDMD-N)) in Abeta1-40 oligomers-exposed ARPE-19 cells. (A) Representative immunofluorescence images of NLRP3 (green fluorescence) and DAPI (blue fluorescence) in ARPE-19 cells under different treatments. Abeta1-40 oligomers exposure increased the cellular expressions of NLRP3 (second row). However, the increased expression was subsequently decreased by LBP treatment with both low (3.5 mg/L) and high (14 mg/L) concentration (third row and the fourth row). Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/32629957), licensed under a CC-BY licence.

Hippocampal AMPK/Sirt1 and NFkappaB/NLRP3/IL-1beta signaling pathways in diabetic rats and the effects of aerobic exercise. Type 2 diabetes significantly decreases the activation of hippocampal AMPK (a) and the level of Sirt1 (c), leading to increased Ac-NFkappaB (d) and NFkappaB (e); diabetic rats contain more NLRP3 inflammasomes (f) and IL-1beta (g). Aerobic exercise intervention significantly increases AMPK activity and Sirt1 concentration; aerobic exercise downregulates the Ac-NFkappaB and NFkappaB, leading to decreased levels of the NLRP3 inflammasome and IL-1beta. **p < 0.01, DM group vs. C group; #p < 0.05, TDM group vs. DM group. Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/30911292), licensed under a CC-BY licence.

Exercise training prevents HFD-induced upregulation of cardiac pyroptosis. Western blotting was performed to determine the components of inflammasome complex and pyroptosis in the left ventricle of mice hearts. (A) HFD-fed obese mice show upregulation of the NLRP3 inflammasome in the left ventricle, which is prevented by exercise training. Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31835893), licensed under a CC-BY licence.

NLRP3 deficiency in non-hematopoietic cells exacerbates GVHD and is not rescued by propionate. B6 WT and Gpr43-/- mice received BMT from either syngeneic B6 or allogeneic BALB/c donors. a) Representative immunoblots and densitometric analysis of NLRP3 normalized to the presence of beta-actin in IECs (CD326+) from allogeneic recipients 14 days after BMT (n = 3 each, two-tailed Mann-Whitney U test). Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/30201970), licensed under a CC-BY licence.

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), and 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, and Mfn1 mRNA. (B) Levels of LC3B, PINK1, Parkin, and Mfn1 protein by Western blot. (C) Relative expression of LC3B-II/LC3B-I and PINK1 protein. (D) Relative expression of Parkin and Mfn1 protein. (E) Levels of TLR9 and COX4 mRNA. (F) Levels of MyD88 and nuclear factor-kappa B (NF-kappa B) mRNA. (G) Levels of TLR9, COX4, MyD88, and NF-kappa B protein by Western blot. (H) Relative expression of TLR9 and COX4 protein. (I) Relative expression of MyD88 and 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; and cP < 0.05 vs. AmA group. Image collected and cropped by CiteAb from the following open publication (//www.frontiersin.org/article/10.3389/fimmu.2018.01477/full), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Cellular and embryonic localisation of CL-L1.A. Immunostaining of ATDC5 cells with the golgi marker 58K and CL-L1. CL-L1 shows localisation with golgi apparatus (white arrow). B. Laminin and CL-L1 coimmunolocalisation. Laminin shows partial cellular immunolocalisiton with CL-L1 around the golgi area (arrows). Scale bar 50 μm C. Laminin and CL-K1 coimmunolocalisation. CL-K1 staining shows a very strong golgi localisation with partial cytoplasmatic laminin colocalisation. D. CL-L1 immunohistochemistry of a 18.5 days postfertilisation mouse embryo. CL-L1 is expressed in the liver (long arrow) and submucosal patal region (short arrows). E. Immunofluorescence showing co-localisation of CL-L1 and Laminin in E13.5 mouse embryos sections. CL-L1 is expressed in the basal membrane of the ephithelium in the palate shelf of the maxilla (arrows). In contrast Laminin expression is present all around the ephitelium membrane. A faint but clear CL-L1 expression is also observed in the cytoplasm of the epithelium and in the mesenchyme of the palate. PSM; rostral extremity of right palatal shelf of maxilla. Scale bar 100 μm. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/28301481), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Role of NF-kappa B in glucose fluctuation-induced inflammasome-related myocardial fibrosis. (A) Immunofluorescence staining of NF-kappa B/p65 nucleation (n = 3 per group). (B,C) The phosphorylation level of NF-kappa B/p65 in rat hearts of the three groups (n = 4 per group). (D) Immunofluorescence staining of intracellular NLRP3–ASC interaction in the GF and GF + TPCA-1 groups. The NRCFs were labeled with anti-NLRP3 (red), anti-ASC (green), and DAPI (blue) (n = 3 per group). (E–G) After application of TPCA-1 (0.5 μM), the protein expressions of cleaved caspase-1 and collagen I were measured by western blot (n = 3 per group). Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/35592403), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Effects of oltipraz on the expression of CD11b/c, PI3K, p-Akt, and p-IkB alpha in the hippocampus of the CCI-injured mice. The relative protein levels of (A) CD11b/c, (B) PI3K, (D) p-Akt, and (E) p-IKB alpha in the hippocampus of the CCI-injured mice treated with oltipraz (OLT) or vehicle. The sham-operated mice (SHAM) treated with vehicle were used as controls. Representative examples of blots for (C) CD11b/c (160 kDa), PI3K (130 kDa), and GAPDH (37 kDa); and (F) for p-Akt (60 kDa), Akt (60 kDa), p-IKB alpha (40 kDa), and IKB alpha (40 kDa). CD11b/c and PI3K are expressed relative to GAPDH levels whereas phosphorylated proteins are expressed relative to their corresponding total proteins. In all panels, * denotes significant differences vs. sham-operated mice treated with vehicle (p < 0.05; one-way ANOVA followed by the SNK test). Results are presented as the mean ± SEM; n = 5 samples per experimental group. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/31234342), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

LRRK2 regulation on alpha -synuclein levels. a Western blot analysis of basal alpha -synuclein and b p62 levels in neurons during mid and late differentiations. Blots show the alpha -synuclein soluble monomer of ~15 kDa. Bars represent the mean ± SEM of three to six values, including two different cell lines per group. beta III-tubulin was used as loading control (two-way ANOVA, ** P < 0.01, LRRK2G2019S v. control WT, late stage). cLRRK2 RNA levels 5 days after shRNA lentiviral transduction. The empty vector was used as the mock control. Lines represent the mean ± SEM of three to four independent silencing experiments. A representative immunoblot analysis of LRRK2 protein levels 5 days after transduction is also shown. beta III-tubulin was the loading control. d Immunoblots and corresponding quantification of alpha -synuclein 5 days after shLRRK2 transduction. Bars represent the mean ± SEM of at least three independent silencing experiments. LRRK2 silencing had a significant effect on alpha -synuclein protein levels (two-way ANOVA, *** P = 0.0002). Bonferroni post hoc test showed that this effect was limited to LRRK2 mutated mature neurons (**P < 0.05 for both LRRK2G2019S and LRRK2R1441G). e qRT-PCR analysis of SNCA after LRRK2 silencing. f Immunoblots and corresponding quantification of p62 5 days after shLRRK2 transduction. Bars represent the mean ± SEM of at least three independent silencing experiments. See Additional file 3 for uncropped blots Image collected and cropped by CiteAb from the following open publication (//jneuroinflammation.biomedcentral.com/articles/10.1186/s12974-016-0761-x), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

ER stress is induced by acidosis activated OGR1-mediated signalling. Caco-2 cells were subjected to different pH medium, following 4–6 h incubation in pH 7.6 serum free medium. (A) Vector control Caco-2 (VC) and OGR1 overexpressing Caco-2 cells where treated with tunicamycin at the indicated concentrations for 24 h. Total protein was isolated and Western blotting was performed. The results are representative of two independent experiments. (B) After 24 h pH shift, total protein was isolated and Western blotting was performed. The results are representative of three independent experiments. (C) Densitometry after normalization of BiP to beta -actin and (D) p-IRE1 alpha to total IRE1 alpha . Statistical analysis was performed using one-way ANOVA followed by Tukey’s post-test. Data are presented as means ± SE of three independent experiments (*p < 0.05; **p < 0.01; ***p < 0.001; ****p < 0.0001). (E) After 24 h pH shift, total RNA was isolated and mRNA expression was investigated by qPCR. Statistical analysis was performed using one-way ANOVA followed by Tukey’s post-test. Data are presented as means ± SE of three independent experiments (*p < 0.05; **p < 0.01). (F) A specific small molecule OGR1 inhibitor (10 µM) was tested and the cells were subjected to low pH for 24 h, following 4–6 h incubation in pH 7.6 serum free medium. After 24 h pH shift, total protein was isolated and Western blot performed. Results are representative of two independent experiments. (G) Cells were treated as described in (F), then total RNA was extracted and analysed for expression of XBP1 (XBP1u) and spliced XBP1 (XBP1s) by conventional PCR. Results are representative of three independent experiments. (H) Quantification of the ratio of XBP1s/XBP1u was performed using ImageJ. Results are representative of two independent experiments. Statistical analysis was performed using one-way ANOVA followed by Tukey’s post-test. Data are presented as means ± SE of three independent experiments (*p < 0.05; **p < 0.01; ***p < 0.001; ****p < 0.0001). For all the panels, the experiments were repeated two to three times. pH conditions: High pH 7.5–7.8; Normal pH 7.2–7.4; Low pH 6.6–6.8. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/31996710), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Flow cytometry gating strategy for quantification of platelet-derived microparticles in equine platelet samples.A: Platelet events in citrate-anticoagulated platelet-rich plasma were identified and gated as CD41-positive cells (R1 region) in a CD41 fluorescence versus forward scatter (FSC) dotplot. The R1 region or gate was established on an isotype control for the CD41 antibody. Representative image from platelets exposed to the RacL11 strain of EHV-1 at 1 plaque forming unit (PFU)/cell. B: Platelet-derived microparticles (PDMPs) were defined as small events (<101 log FSC units) positive for Annexin V and CD41. The PDMP percentage was obtained from the lower right quadrant of an Annexin V fluorescence versus FSC dotplot of the R1 gate (CD41-positive events), with the quadrants being defined on a negative sample in which 1 mM EDTA was added to the buffer with Annexin V. The PDMP percentage was 0.1% in this representative image of platelets exposed to rabbit kidney 13 (RK) cell lysate at an equivalent volume to 1 PFU/cell (mock-infected negative control). The events in the upper left and right quadrants are platelets that are negative (94.0%) and positive for Annexin V (0.9%), respectively. C: Representative image of PDMP quantification in platelets exposed to RacL11 at 1 PFU/cell. In this sample, there are 12.1% PDMP (lower right quadrant) and 22.1% of platelets are weakly positive for Annexin V (upper right quadrant). Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/25905776), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Reactivity:

Hu, Mu, Rt, RM

Species Glossary

Reactivity: Hu, Mu, Rt, RM

Applications:

, , , , ,

Applications: , , , , ,

Host:

Rabbit Polyclonal

Host: Rabbit Polyclonal

Alt Catalog#

IMG-6668A

Alt Catalog# IMG-6668A

Sizes:

Sample Size Available

Sizes: Sample Size Available

Conjugate:

Unconjugated

Available Conjugates:

Conjugate	Catalog #	Availability	Size	Price
Alexa Fluor 350	NBP2-12446AF350
Alexa Fluor 405	NBP2-12446AF405
Alexa Fluor 488	NBP2-12446AF488
Alexa Fluor 532	NBP2-12446AF532
Alexa Fluor 594	NBP2-12446AF594
Alexa Fluor 647	NBP2-12446AF647
Alexa Fluor 700	NBP2-12446AF700
Alexa Fluor 750	NBP2-12446AF750
Allophycocyanin	NBP2-12446APC
Biotin	NBP2-12446B
DyLight 350	NBP2-12446UV
DyLight 405	NBP2-12446V
DyLight 488	NBP2-12446G
DyLight 550	NBP2-12446R
DyLight 594	NBP2-12446DL594
DyLight 650	NBP2-12446C
DyLight 680	NBP2-12446FR
DyLight 755	NBP2-12446IR
FITC	NBP2-12446F
HRP	NBP2-12446H
Janelia Fluor 549	NBP2-12446JF549
Janelia Fluor 646	NBP2-12446JF646
PE	NBP2-12446PE
PerCP	NBP2-12446PCP

Available Formulations

Formulation	Catalog #	Availability	Price
BSA Free	NBP2-12446SS

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NB100-56708

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

(2 Reviews)

(191 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).

$NFATc1 regulates DcR3 expression at a transcriptional level. (C) Immunoblot analysis of cytoplasmic and nuclear fractions of ACHN and 769-P cells after treatment with LY294002 (50 uM), Everolimus (1 uM), or Cyclosporine A (25 uM). Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/24107265), licensed under a CC-BY licence.$

Lipofection of top broccoletti-miR candidates does not influence basal and induced apoptosis. (B) Lipofected BxPc-3 and 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 x100 magnification are shown. The percentage of Ki-67- or caspase-3-positive cells was counted in 18 visual fields, and the means +/- SD are shown in the diagram below. (C) BxPc-3 and Bx-Gem were lipofected as described above, and 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 and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/32292571), licensed under a CC-BY licence.

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.

APE1 acetylation enhances its stability on chromatin and its interaction with downstream BER proteins. (A) Colocalization of ligase III and AcAPE1 in A549 cells. Cells were immunostained with anti-ligase III and anti-AcAPE1 Abs. (B) WT or K5R mutant APE1-overexpressing HEK293T cells were treated with TSA-nicotinamide (NAM) for 6 h or not treated, and the nuclear extract was immunoprecipitated using anti-FLAG Ab and immunoblotted with anti-XRCC1 and anti-FLAG Abs. (C) A549 cells were fixed with paraformaldehyde before (top) or after treatment with Triton X-100 (0.5%) (middle) or Triton X-100 plus salt (100 mM KCl) (bottom) and immunostained with anti-APE1 or anti-AcAPE1 Abs and counterstained with DAPI. (D) Acetylation of APE1 induces a conformational change in APE1. The distinct intrinsic fluorescence emission spectra of APE1 and AcAPE1 at 280 nm are shown. A.U., absorbance units. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/27994014), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Reduced expression levels of IFI16 protein in human normal diploid fibroblasts after treatment with histone deacetylase inhibitor are associated with increased expression of hTERT and increased telomerase activity.(A) Total RNA isolated from untreated (control, lane 1) or CGK1026 (10 µM for 24 h, lane 2) treated young WI-38 fibroblasts was subjected cDNA synthesis followed by semi-quantitative PCR using a pair of primer specific to the IFI16, hTERT, or actin. As a positive control, we used RNA from human HT1080, a human fibrosarcoma cell line. (B) Total RNA isolated from untreated (control) or CGK1026 (10 µM for 24 h; treated) treated young WI-38 fibroblasts was subjected cDNA synthesis, followed by quantitative real-time PCR using the TaqMan assay for the hTERT gene. Results are mean values of triplicate experiments and error bars represent standard deviation (**p<0.005). (C and D) Total protein extracts prepared from untreated (lane 1) or CGK1026 (10 µM for 24 h; treated) treated young WI-38 fibroblasts were subjected to immunoblotting using antibodies specific to the indicated proteins. Image collected and cropped by CiteAb from the following open publication (//dx.plos.org/10.1371/journal.pone.0008569), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

HIF-1 alpha overexpression rescues oxygen-induced radioresistance in RAH-treated cells, but not GCH-treated cells.Results are shown for the anchorage-independent colony forming assays for U87 cells transfected with either an empty vector or HIF-1 alpha expression vector and then exposed to GCH or RAH protocols without (–) or with (+) reoxygenation. Continuously normoxic cells (NOx) were irradiated as a positive control. To allow for ease of comparisons among conditions, raw values are presented as a percentage of that cell type’s negative (non-irradiated) control and the means and SEMs are plotted. Each result represents at least three independent samples, plated in triplicate. Holm-Sidak comparisons for multiple groups were used for statistical comparisons of raw values (*p<0.05, **p<0.01). Western blotting analysis of nuclear HIF-1 alpha at the time of irradiation is shown for each cell type below clonogenic results. Corresponding Western blots of lamin A/C are shown as a loading control and blots for hemagglutinin (HA) are shown below HIF-1 alpha overexpression vector results to demonstrate transfection efficacy. All lanes shown that are non-adjacent to the negative control (NOx) are denoted with a separating black line. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/25350400), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Differential roles of caspase-1 and caspase-11 in response to infection with Aspergillus fumigatus.(A) Immunoblot analysis of pro-caspase-1 (Pro-Casp-1) and the caspase-1 subunit p20 (Casp-1 p20) and GAPDH (loading control) in unprimed WT or mutant bone marrow-derived dendritic cells left untreated (medium alone [Med]) or assessed 20 h after infection with A. fumigatus (MOI, 10). (B) Release of IL-1 beta and IL-18 after treatment as in (A). (C) Survival of 8-week-old WT and mutant mice infected with 5 × 105 A. fumigatus conidia after immunosuppression with cyclophosphamide and cortisone acetate. *P < 0.05, ****P < 0.0001 (log-rank test). Data are representative of two (C) or three independent experiments (A and B; mean and s.e.m. are representative of values from three independent experiments in B). Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/28345580), 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
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 549	NB100-56708JF549
Janelia Fluor 646	NB100-56708JF646
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

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NB100-56875

GAPDH Antibody

(5 Reviews)

(114 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.

Particle-induced Changes in Apoptosis are Restored by Firoin.Peripheral blood neutrophils from healthy donors (n = 7), 2 h pre-treated with indicated amounts of firoin (F) or 1 mM ectoine (E) before CNP exposition (33 ug/ml). A: After 16 h of CNP treatment, cells were stained with Annexin V and analysed flow cytometrically. Normalized values of % Annexin V-positive cells are shown. Natural apoptosis of untreated cells was considered as 1. Dark bars, CNP-treated, light bars, untreated. * Significantly different from CNP alone (Mann-Whitney U Test after Bonferroni correction for multiple testing p<0.05). B: 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 licence.

Analysis of non-canonical inflammasome pathway. D) Western blotting for the cleaved forms of CASP1 (p20), CASP4 (p20), and GSDMD (N-terminal). S: SCGB3A2, N: nigericin. Experiments were repeated more than twice and same results were obtained. Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/33452234), licensed under a CC-BY licence.

No dystrophin expression was detected in cardiac and skeletal muscles of Dmdmdx rats.(A) Male 7 month-old rats of line 61, wild-type littermate controls (WT) and Dmdmdx were sacrificed and biopsies from tibialis cranialis muscles (TC) and hearts (H) were harvested. Western-blot of total proteins (50 ug) was incubated with NCL-DYS2 and Manex1011C monoclonal antibodies (C-terminal and 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 and samples from WT rats were used as positive controls. Staining with an anti-GAPDH polyclonal antibody validated equal protein loadings. Image collected and cropped by CiteAb from the following publication (//dx.plos.org/10.1371/journal.pone.0110371), licensed under a CC-BY licence.

Antigen uptake is reduced in K14E7 mice.Epidermal cell suspensions from C57BL/6 and K14E7 mice were cultured with Alexa-555-labelled OVA overnight at 37°C, stained and analysed by flow cytometry (A). The Alexa-555-OVA+ LC (CD45.2+, MHC Class II+, CD207+) as a percentage of total LC (B) and the level of expression of Alexa-555-OVA on the positive stained LC is shown (C). **P < 0.01; *P < 0.05 (Mann-Whitney U test). Confocal imaging of CD207+, MHCII+ LC that have taken up Alexa-555-OVA (D). Image collected and cropped by CiteAb from the following open publication (//dx.plos.org/10.1371/journal.pone.0127155), 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

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NBP2-27103

GAPDH Antibody (13H12) - BSA Free

(3 Reviews)

(32 Publications)

0.1 mg

NBP2-27103

Immunohistochemistry-Paraffin: GAPDH Antibody (13H12) [NBP2-27103] - IHC-P detection GAPDH protein in a formalin-fixed paraffin-embedded section of human rectal carcinoma tissue using GAPDH antibody (clone 13H12) at 5 ug/ml concentration.

Western Blot: GAPDH Antibody (13H12) [NBP2-27103] - Characterization of lncR492.(B) Northern blot of lncR494 using increasing amounts of loaded total. Black arrow signifies lncR492-specific signal at approximately 1400 bp. A probe targeting Gapdh mRNA served as the loading control. (D) RT-PCR analysis of lncR492 and Gapdh expression. RNA extract was treated with a 5'-phosphate-dependent exonuclease, resulting in a degradation of f.ex. ribosomal RNA.Citation: Winzi M, Casas Vila N, Paszkowski-Rogacz M, Ding L, Noack S, Theis M, et al. (2018) The long noncoding RNA lncR492 inhibits neural differentiation of murine embryonic stem cells. PLoS ONE 13(1): e0191682. //doi.org/10.1371/journal.pone.0191682

Western Blot: GAPDH Antibody (13H12) [NBP2-27103] - Serum from trauma patients induces intrinsic apoptosis resistance by up-regulating AAT expression in neutrophils. AAT protein expression was analyzed in neutrophils after 18 h of culture by western blot analysis. Relative expression was quantified vs. GAPDH expression. One representative blot of five independent experiments is depicted. **p<0.01 (one-way ANOVA with Newman keuls post-hoc test). Image collected and cropped by CiteAb from the following publication (//dx.plos.org/10.1371/journal.pone.0177450), licensed under a CC-BY license.

Western Blot: GAPDH Antibody (13H12) [NBP2-27103] - WB detection of GAPDH protein (theoretical molecular weight 36 kDa) in lysates of Mouse cell lines (A) NIH 3T3 (B) RAW 264.7 using GAPDH antibody (clone 13H12) at a concentration of 0.25 ug/ml.

Western Blot: GAPDH Antibody (13H12) [NBP2-27103] - analysis of GAPDH in HeLa and HEK 293 cells (25ug/lane) using anti-GAPDH antibody. Image from verified customer review.

Immunohistochemistry-Paraffin: GAPDH Antibody (13H12) [NBP2-27103] - IHC-P detection GAPDH protein in a formalin-fixed paraffin-embedded tissue section of human esophageal squamous cell carcinoma (SCC) using GAPDH antibody (clone 13H12) at 5 ug/ml concentration.

Simple Western: GAPDH Antibody (13H12) [NBP2-27103] - GAPDH/G3PDH Antibody (13H12) [NBP2-27103] - Simple Western lane view shows a specific band for GAPDH in 0.1 mg/ml of HeLa lysate. This experiment was performed under reducing conditions using the 12-230 kDa separation system.

5-FU-produced ROS involved in histone methyltransferase-mediated Nrf2 expressionSNUC5/5-FUR cells were pre-treated with 500 μM NAC, plated, and incubated for 48 h. Then, cells were treated with 10 μM DHR123 and incubated for 30 min at 37°C. The intracellular ROS were detected by A. flow cytometry and B. confocal imaging. FI indicates the fluorescence intensity of DHR-123. *Significantly different from SNUC5 cells (p<0.05), and #significantly different from SNUC5/5-FUR cells (p<0.05). C. Expression pattern of Nrf2 mRNA was determined by RT-PCR analysis. *Significantly different from SNUC5 cells (p<0.05), and #significantly different from SNUC5/5-FUR cells (p<0.05). D. Expression pattern of nuclear and cytosolic Nrf2 protein was determined by Western analysis. E. Expression patterns of TET1, OGT, HCF1, and MLL in NAC pre-treated SNUC5/5-FUR cells determined by Western blot analysis. *Significantly different from SNUC5 cells (p<0.05), and #significantly different from SNUC5/5-FUR cells (p<0.05). Also, SNUC5 cells were pre-treated with 500 μM of NAC and incubated for an additional 1 h at 37°. Cells were then treated with 140 μM 5-FU for 48 h. 10 μM of DHR123 was added to plate and incubated for an additional 30 min at 37°C. F. The intracellular ROS level was detected by flow cytometry and G. confocal imaging. FI indicates the fluorescence intensity of DHR123. *Significantly different from SNUC5 cells (p<0.05), and #significantly different from 5-FU-treated SNUC5 cells (p<0.05). H. Expression pattern of Nrf2 mRNA was determined by RT-PCR analysis. *Significantly different from SNUC5 cells (p<0.05), and #significantly different from 5-FU-treated SNUC5 cells (p<0.05). I. Expression pattern of nuclear and cytosolic Nrf2 protein was determined by Western analysis. J. The expression of TET1 and interaction proteins detected by Western blot analysis. *Significantly different from SNUC5 cells (p<0.05), and #significantly different from 5-FU-treated SNUC5 cells (p<0.05). Image collected and cropped by CiteAb from the following open publication (//www.oncotarget.com/lookup/doi/10.18632/oncotarget.9745), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Reactivity:

Hu, Mu, Rt, Dr, Pm, Pm, Sh, Po, Bv, Ca, Ma, Gp, Re, Sq

Species Glossary

Reactivity: Hu, Mu, Rt, Dr, Pm, Pm, Sh, Po, Bv, Ca, Ma, Gp, Re, Sq

Applications:

, , ,

Applications: , , ,

Host:

Mouse Monoclonal

Host: Mouse Monoclonal

Alt Catalog#

IMG-6665A

Alt Catalog# IMG-6665A

Sizes:

Sample Size Available

Sizes: Sample Size Available

Conjugate:

Unconjugated

Available Conjugates:

Conjugate	Catalog #	Availability	Size	Price
Alexa Fluor 350	NBP2-27103AF350
Alexa Fluor 405	NBP2-27103AF405
Alexa Fluor 488	NBP2-27103AF488
Alexa Fluor 532	NBP2-27103AF532
Alexa Fluor 594	NBP2-27103AF594
Alexa Fluor 647	NBP2-27103AF647
Alexa Fluor 700	NBP2-27103AF700
Alexa Fluor 750	NBP2-27103AF750
Biotin	NBP2-27103B
DyLight 350	NBP2-27103UV
DyLight 405	NBP2-27103V
DyLight 488	NBP2-27103G
DyLight 550	NBP2-27103R
DyLight 594	NBP2-27103DL594
DyLight 650	NBP2-27103C
DyLight 680	NBP2-27103FR
DyLight 755	NBP2-27103IR
FITC	NBP2-27103F
HRP	NBP2-27103H
Janelia Fluor 549	NBP2-27103JF549
Janelia Fluor 646	NBP2-27103JF646
mFluor Violet 450 SE	NBP2-27103MFV450
mFluor Violet 500 SE	NBP2-27103MFV500
mFluor Violet 610 SE	NBP2-27103MFV610

Available Formulations

Formulation	Catalog #	Availability	Price
BSA Free	NBP2-27103SS
Azide and BSA Free	NBP2-80749

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NB600-502

GAPDH Antibody (6C5cc)

(3 Reviews)

(81 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.

Representative picture of western blot in histopathologically unchanged tissue (N) and primary cancerous tissue (C) from patients with CRC. Immunodetection of bands was performed with Rp anti- PHD1, - PHD2, - PHD3 and - FIH Ab, followed by incubation with goat anti-rabbit HRP-conjugated Ab. The membrane was stripped and incubated with Rp anti-GAPDH Ab, followed by incubation with goat anti-rabbit HRP-conjugated Ab. Bands were revealed using SuperSignal West Femto Chemiluminescent Substrate, Thermo Fisher Scientific (Rockford, IL) and Biospectrum® Imaging System 500, UVP Ltd. (Upland, CA). Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/24195777), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Immunostaining of HN30 and MCF-12a cells for TRAF2 3 days post-transfectionMCF-12a NT (DAPI): non-treated MCF-12a DAPI stained, MCF-12a NT (TRAF2-FITC): non-treated MCF-12a FITC stained for TRAF2, MCF-12a pNSP 5a3a (DAPI): MCF-12a transfected with pcDNA 3.0 NSP 5a3a DAPI stained, MCF-12a pNSP 5a3a (TRAF2-FITC): MCF-12a transfected with pcDNA 3.0 NSP 5a3a FITC stained for Traf-2, HN30 NT (DAPI): non-treated HN30 DAPI stained, HN30 NT (TRAF2-FITC): non-treated HN30 FITC stained for TRAF2, HN30 pNSP 5a3a (DAPI): HN30 transfected with pcDNA 3.0 NSP 5a3a DAPI stained, HN30 pNSP 5a3a (TRAF2-FITC): HN30 transfected with pcDNA 3.0 NSP 5a3a FITC stained for TRAF2. White arrows indicate apoptotic bodies. Image collected and cropped by CiteAb from the following open publication (//www.oncotarget.com/lookup/doi/10.18632/oncotarget.306), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Baclofen reversed the changes of protein markers characteristic for autophagy in hippocampal CA1 area under chronic cerebral hypoperfusion.(a–c) Five weeks after induction of hypoperfusion, p-mTOR was significantly decreased, and LC3-II, Beclin 1, atg5 and atg7 were significantly increased, and baclofen could reverse the changes of these proteins expression. Treatment with baclofen at 12.5 mg/kg and 25 mg/kg in sham-operated rats did not change the expression of LC3-II, mTOR, p-mTOR, Beclin 1, atg5 and atg7 compared with sham-operated rats (n = 4 in each group). Blots shown have been cropped to fit space requirements and run under the same experimental conditions. *P < 0.05 and **P < 0.01 vs sham-operated rats; ##P < 0.01 vs 2VO rats. Image collected and cropped by CiteAb from the following open publication (//www.nature.com/articles/srep14474), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

The production of DSBs depends on Top1 degradation in CPT-treated quiescent cells. (A–C) Serum-starved WI38 hTERT cells were co-transfected with siRNAs against cullin 3 and cullin 4B or against a control sequence and then treated with DMSO (−CPT) or 25 μM CPT (+CPT) for 1 h. (A and B) Western blotting of the indicated proteins. alpha Tubulin: loading control. (C) Number of gamma H2AX foci per nucleus from one representative experiment (246–348 nuclei were analyzed for each treatment) out of three. ***P < 0.001. (D and E) Serum-starved WI38 hTERT cells were treated with DMSO or MG132 (50 μM) for 1 h before exposure to 0.8 Gy IR. One hour post-irradiation, cells were co-stained for gamma H2AX (green) and 53BP1 (red). (D) Representative pictures. (E) Number of gamma H2AX foci per nucleus from one representative experiment (162–180 nuclei were analyzed for each treatment) out of three. Ns: not significant. (F and G) U2OS EV28 cells were treated with DMSO or MG132 (10 μM) for 1 h before the addition of ethanol (untreated) or 300 nM 4-hydroxitamoxifen (4OHT) for 4 h to express AsiSI in the nucleus (42). (F) Representative pictures of cells co-stained for gamma H2AX (green) and 53BP1 (red). (G) ChIP analysis using an anti-gamma H2AX antibody (black) or a non-immune antibody (IgG, gray). Enrichment was assessed by QPCR amplification using primers proximal to two AsiSI sites located inside two genes (Gene I: SFRS6, Gene II: CCD47) and primers distal to an AsiSI site (Control). Enrichment was normalized to the maximum recovery for each experiment (means ± SEM, n = 3). Ns: not significant; *P < 0.05. In the microscopic images, nuclear contours, identified by DAPI staining (not shown), are indicated by dashed lines. Bars: 10 μm. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/26578593), 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
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 549	NB600-502JF549-0.2ml
Janelia Fluor 646	NB600-502JF646-0.2ml

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NB100-56113

Caspase-3 Antibody - (active/cleaved)

(70 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)

Pathology in DOX treated acute and recovery phase mice. Regions of myofiber loss and frank replacement fibrosis were noted, most commonly in atria (A, acute phase), and rarely in ventricles (D, recovery phase). These areas were accompanied by macrophage infiltration (B, E) and 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) and cleaved caspase -3 (G) Bar = 100um (A-C); 50um (D-F); 20um (G). Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31263061), licensed under a CC-BY licence.

Normoxic pre-treatment sensitizes glioma cells to radiation after graded chronic hypoxic (GCH) exposure.(A) The graded chronic hypoxia (GCH) protocol is shown, depicting the timing and severity of hypoxic exposure to four cell lines. Cells either remain in a continuous hypoxic environment (–) or are transiently (25 min) exposed to normoxia 25 min prior to radiation (+). Continuously normoxic cells (NOx) were irradiated as a positive control. (B) The results of anchorage-independent colony forming assays are shown for U87, U87-luc, GL261 glioma cells and 0308 GSCs after 5 Gy radiation exposure under varying oxygen conditions. To allow for ease of comparisons among cell types, raw values are expressed as a percentage of the corresponding cell type’s negative (non-irradiated) control and the means and SEMs are plotted. Each result represents at least three independent samples, plated in triplicate. Holm-Sidak comparisons for multiple groups were used for statistical comparisons of raw values (*p<0.05, **p<0.01). Also shown are Western blots of nuclear HIF-1 alpha at the time of irradiation for each cell type. Corresponding Western blots of lamin A/C are shown as a loading control. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/25350400), 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:

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NBP2-13075

beta Amyloid Antibody (MOAB-2) - BSA Free

(2 Reviews)

(63 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.

Abeta plaque load in neocortex and hippocampus in APP/PS1 mice exposed to differential housing. (F) 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 licence.

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
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 549	NBP2-13075JF549
Janelia Fluor 646	NBP2-13075JF646
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

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NB300-320

GAPDH Antibody

(2 Reviews)

(64 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.

stai Mutants Have Reduced Levels of alpha-Tubulin, Acetylated alpha-Tubulin, and Kinesin Heavy Chain Protein.(A) 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 (//pubmed.ncbi.nlm.nih.gov/23840848), licensed under a CC-BY licence.

PAR2 causes contraction of smooth muscle cells from human prostate. C) Representative western blot 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. Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31198907), licensed under a CC-BY licence.

MiR-34a affects stroke outcomes via interacting with cytochrome c. (A) WES system image showing CYC, VDAC and GAPDH expression from hemispheres of WT and miR-34a-/- mice at 6 h post-stroke. Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/32094435), licensed under a CC-BY licence.

Effects of resveratrol on the expression of SIRT1, PGC-1 alpha , HIF-1 alpha and apoptosis proteins in vivo. (A) Activation of the SIRT1–PGC-1 alpha –HIF-1 alpha signaling pathway in PC–AKI associated with DN in rabbits. Representative western blot images of proteins in the rabbits with DN treated with saline (Cont), resveratrol alone (Res), iohexol (PC–AKI), and co-treatment with resveratrol and iohexol (Res+PC–AKI). (B–H) Relative densitometry analysis of the ratios of SIRT1–PGC-1 alpha –HIF-1 alpha signaling proteins to beta -actin were expressed as mean ± standard error. *P < 0.05 vs. Cont; #P < 0.05 vs. PC–AKI. Cont, control; Res, resveratrol; PC–AKI, post-contrast acute kidney injury; SIRT1, silent information regulator l; HIF-1 alpha , hypoxia-inducible transcription factor-1 alpha ; DN, diabetic nephropathy; PGC-1 alpha , peroxisome proliferator-activated receptor gamma coactivator-1 alpha. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/31402864), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Reactivity:

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

Species Glossary

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

Applications:

, , , ,

Applications: , , , ,

Host:

Goat Polyclonal

Host: Goat Polyclonal

Alt Catalog#

IMG-3073

Alt Catalog# IMG-3073

Conjugate:

Unconjugated

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NBP1-49678

PINK1 Antibody - BSA Free

(1 Review)

(3 Publications)

0.1 ml

NBP1-49678

Immunohistochemistry-Paraffin: PINK1 Antibody [NBP1-49678] - Stain in paraffin embedded mouse brain.

Immunocytochemistry/Immunofluorescence: PINK1 Antibody [NBP1-49678] - PINK1 antibody was tested at 1:50 in HeLa cells with DyLight 488 (green). Nuclei and alpha-tubulin were counterstained with DAPI (blue) and DyLight 550 (red). Image objective 40x.

Reactivity:

Hu, Mu

Species Glossary

Reactivity: Hu, Mu

Applications:

, ,

Applications: , ,

Host:

Rabbit Polyclonal

Host: Rabbit Polyclonal

Sizes:

Sample Size Available

Sizes: Sample Size Available

Conjugate:

Unconjugated

Available Conjugates:

Conjugate	Catalog #	Availability	Size	Price
Alexa Fluor 350	NBP1-49678AF350
Alexa Fluor 405	NBP1-49678AF405
Alexa Fluor 488	NBP1-49678AF488
Alexa Fluor 532	NBP1-49678AF532
Alexa Fluor 594	NBP1-49678AF594
Alexa Fluor 647	NBP1-49678AF647
Alexa Fluor 700	NBP1-49678AF700
Alexa Fluor 750	NBP1-49678AF750
Allophycocyanin	NBP1-49678APC
Biotin	NBP1-49678B
DyLight 350	NBP1-49678UV
DyLight 405	NBP1-49678V
DyLight 488	NBP1-49678G
DyLight 550	NBP1-49678R
DyLight 594	NBP1-49678DL594
DyLight 650	NBP1-49678C
DyLight 680	NBP1-49678FR
DyLight 755	NBP1-49678IR
FITC	NBP1-49678F
HRP	NBP1-49678H
Janelia Fluor 549	NBP1-49678JF549
Janelia Fluor 646	NBP1-49678JF646
PE	NBP1-49678PE
PerCP	NBP1-49678PCP
mFluor Violet 450 SE	NBP1-49678MFV450
mFluor Violet 500 SE	NBP1-49678MFV500
mFluor Violet 610 SE	NBP1-49678MFV610

Available Formulations

Formulation	Catalog #	Availability	Price
BSA Free	NBP1-49678SS

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

Category

Protein/Target

Applications

Reactivity

Citation

Antibody Validation

Reviews

Host

Available Conjugates

Format

Marker

Modification

Clonality

Clone

Gene Symbol

Images Type

Isotype

Kit Type

Lysate Type

Preservative

Protein Or Peptide

Research Areas

Has Sample Size

Promotional Item

Species Glossary

GAPDH Antibody (1D4)

PGC1 alpha Antibody - BSA Free

PINK1 Antibody - BSA Free

NLRP3/NALP3 Antibody - BSA Free

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

GAPDH Antibody

GAPDH Antibody (13H12) - BSA Free

GAPDH Antibody (6C5cc)

Caspase-3 Antibody - (active/cleaved)

beta Amyloid Antibody (MOAB-2) - BSA Free

GAPDH Antibody

PINK1 Antibody - BSA Free