Neuronal Cell Markers reagents: Novus Biologicals

NB300-221

GAPDH Antibody (1D4)

(19 Reviews)

(425 Publications)

0.1 ml

NB300-221

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

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

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

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

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

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

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

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

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

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

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

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

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

Reactivity:

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

Species Glossary

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

Applications:

, , , , , , ,

Applications: , , , , , , ,

Host:

Mouse Monoclonal

Host: Mouse Monoclonal

Sizes:

Sample Size Available

Sizes: Sample Size Available

Conjugate:

Unconjugated

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BC100-494

PINK1 Antibody - BSA Free

(13 Reviews)

(274 Publications)

0.1 ml

BC100-494

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

Reactivity:

Hu, Mu, Rt, Rb

Species Glossary

Reactivity: Hu, Mu, Rt, Rb

Applications:

, , , , , , , , ,

Applications: , , , , , , , , ,

Host:

Rabbit Polyclonal

Host: Rabbit Polyclonal

Sizes:

Sample Size Available

Sizes: Sample Size Available

Conjugate:

Unconjugated

Available Conjugates:

Validated by:

Validated by:

Conjugate	Catalog #	Availability	Size	Price
Alexa Fluor 350	BC100-494AF350
Alexa Fluor 405	BC100-494AF405
Alexa Fluor 488	BC100-494AF488
Alexa Fluor 532	BC100-494AF532
Alexa Fluor 594	BC100-494AF594
Alexa Fluor 647	BC100-494AF647
Alexa Fluor 700	BC100-494AF700
Alexa Fluor 750	BC100-494AF750
Allophycocyanin	BC100-494APC
Biotin	BC100-494B
CoraFluor 1	BC100-494CL1
DyLight 350	BC100-494UV
DyLight 405	BC100-494V
DyLight 488	BC100-494G
DyLight 550	BC100-494R
DyLight 594	BC100-494DL594
DyLight 650	BC100-494C
DyLight 680	BC100-494FR
DyLight 755	BC100-494IR
FITC	BC100-494F
HRP	BC100-494H
Janelia Fluor 525	BC100-494JF525
Janelia Fluor 549	BC100-494JF549
Janelia Fluor 585	BC100-494JF585
Janelia Fluor 635	BC100-494JF635
Janelia Fluor 646	BC100-494JF646
Janelia Fluor 669	BC100-494JF669
PE	BC100-494PE
PerCP	BC100-494PCP
mFluor Violet 450 SE	BC100-494MFV450
mFluor Violet 500 SE	BC100-494MFV500
mFluor Violet 610 SE	BC100-494MFV610

Available Formulations

Formulation	Catalog #	Availability	Price
BSA Free	BC100-494SS

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NB300-109

Tyrosine Hydroxylase Antibody

(7 Reviews)

(230 Publications)

0.1 ml

NB300-109

Tyrosine hydroxylase immunoreactivity in the central complex and the lateral accessory lobe. A-D: Frontal sections (immunoperoxidase preparations, dorsal to the top). E: Horizontal section (immunofluorescent preparation, posterior to the top). Scale bars = 100 um. Image collected and cropped by CiteAb from the following publication (//dx.plos.org/10.1371/journal.pone.0160531), licensed under a CC-BY license.

Dopamine neurons in the mouse substantia nigra. ICC/IF image submitted by a verified customer review.

Simple Western lane view shows a specific band for Tyrosine Hydroxylase in 0.2 mg/mL of PC-12 lysate. This experiment was performed under reducing conditions using the 12-230 kDa separation system.

Western blot of 10 ug of rat striatal lysate showing specific immunolabeling of the ~60 kDa tyrosine hydroxylase protein.

10x Magnification cryo-sections mouse: primary antibody: anti-rb TH: 1:500; o.n. secondary antibody: 1:500 dk-anti-rb DyLight488. IHC-Fr image submitted by a verified customer review.

Tyrosine hydroxylase immunoreactivity in the mushroom body. All panels show a right brain hemisphere (dorsal to the top, medial to the right), except panels M-O (posterior to the top). Tyrosine hydroxylase (TH) immunoreactivity is shown in magenta (A, D, G, J, M) and synapsin immunoreactivity in green (B, E, H, K, N). Corresponding merged images in C, F, I, L, O. Scale bars = 100 um. Image collected and cropped by CiteAb from the following publication (//dx.plos.org/10.1371/journal.pone.0160531), licensed under a CC-BY license.

Western blot analysis confirms activation of UPR following Hotel protein lysates from the right adrenal medulla of saline (2RS) and RH groups (2RH) were subjected to Western blot analyses as described in methods. Proteins were separated by SDS-PAGE, electroblotted and the membranes were sequentially probed with antibodies specific to Grp78, Derlin1, TH and GAPDH. Similar results were obtained in two separate replicate experiments. Image collected and cropped by CiteAb from the following publication (//dx.plos.org/10.1371/journal.pone.0172789), licensed under a CC-BY license.

Impact of extrinsic and intrinsic hypoxia on catecholamine biosynthesis. Immunohistochemical staining showed an increased expression of Tyrosine Hydroxylase (red) in the necrotic and hypoxic core of the spheroid (DAPI, blue). Scale bar: 200 um. Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31035382/) licensed under a CC-BY license.

Immunohistochemical analysis of a formalin fixed and paraffin embedded rat brain tissue section using Tyrosine Hydroxylase antibody at 1:5000 dilution. The primary antibody binding to its antigen was detected using HRP anti-Polyvalent ready-to-use kit (Ultratek, 35368) with DAB (brown) and the sections were further counterstained using hematoxylin. Isotype control section was incubated with Rabbit IgG Isotype Control antibody and was processed under the same assay conditions. Tyrosine hydroxylase staining (brown) was observed in the test samples only and the signal was specifically localized to the neuronal cells.

Immunostaining of whole-mount Drosophila brains using NB300-109 at 1:500 dilution. The tyrosine hydroxylase antibody worked really well and produced a bright staining with almost no background. Data courtesy of Dr. Olga Alekseenko, Neurobiology Dept. Harvard Medical School.

Immunohistochemical analysis of tyrosine hydroxylase in rat mesenteric artery-whole. ICC/IF image submitted by a verified customer review.

Western blot analysis confirms activation of UPR following RH.Total protein lysates from the right adrenal medulla of saline (2RS) and RH groups (2RH) were subjected to Western blot analyses as described in methods. Proteins were separated by SDS-PAGE, electroblotted and the membranes were sequentially probed with antibodies specific to Grp78, Derlin1, TH and GAPDH. Similar results were obtained in two separate replicate experiments.

Image showing differentiation of neurospheres as evidenced morphologically (A) and through staining by Tyrosine Hydroxylase (B) to show the ability to derive dopaminergic neurons from the rat progenitor cells.

Immunohistochemistry: Tyrosine Hydroxylase Antibody [NB300-109] - D409H GBA1 expression promotes reduction of dopaminergic fiber densities & motor deficit in the striatum of hA53T alpha -synuclein transgenic mice. a, The striatal TH-immunopositive fiber density was assessed in the striatum of the indicated genotypes at 6 months of age (n = 6 per each group). The scale bar is 250 μm. b, The optical densities of TH positive signals were quantified. c & d, Rotarod & Pole test were assessed at 6 months of age with the indicated genotypes (n = 7 per each group). e, the body weight of mice were measured with the indicated genotypes (n = 15 per each group). DATA are expressed as mean ± SEM Image collected & cropped by CiteAb from the following publication (//actaneurocomms.biomedcentral.com/articles/10.1186/s40478-018-0538-9), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: Tyrosine Hydroxylase Antibody [NB300-109] - Dysregulation of RNF146-PARP1 pathways in PD pathogenesis. (C) Expression of PARsylated proteins, RNF146, TH & phosphorylated alpha -synuclein (pS129-a-syn) in postmortem striatum from PD patients & age-matched control subjects (Ctrl) determined by WBs using designated antibodies. Image collected & cropped by CiteAb from following publication (//www.oncotarget.com/lookup/doi/10.18632/oncotarget.21828), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Immunocytochemistry/ Immunofluorescence: Tyrosine Hydroxylase Antibody [NB300-109] - Image showing differentiation of neurospheres as evidenced morphologically (A) & through staining by Tyrosine Hydroxylase (B) to show the ability to derive dopaminergic neurons from the rat progenitor cells. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/30042680), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: Tyrosine Hydroxylase Antibody [NB300-109] - Immunoblots of tyrosine hydroxylase in the cricket & cockroach brain.Protein extracts (8 μl & 16 μl) from the male cricket, Gryllus bimaculatus & male cockroach, Periplaneta americana were electrophoresed, transferred to a membrane & reacted with anti-tyrosine hydroxylase (TH). The anti-TH recognized a single band of protein of ~ 66 kDa (arrow heads) in both the cricket (left two lanes) & cockroach (right two lanes). M, molecular marker. Image collected & cropped by CiteAb from the following publication (//dx.plos.org/10.1371/journal.pone.0160531), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Immunohistochemistry: Tyrosine Hydroxylase Antibody [NB300-109] - D409H GBA1 expression shortens lifespan & leads to dopaminergic degeneration in the hA53T alpha -synuclein transgenic mice. a, Survival was monitored from littermates with the following genotypes: hA53Ta-Syn/GBA1+/+ (n = 15), hA53T alpha -Syn/GBA1+/D409H(n = 16), hA53T alpha -Syn/GBA1D409H/D409H (n = 18) mice. GBA1 mutation induces the lethal phenotype & TH-positive neuronal loss in the SNpc of A53T mutant alpha -synuclein transgenic mice. b & c, The number of TH-positive neurons in the SNpc was counted using stereological analysis with the indicated genotypes at 6 months of age. The scale bar is 200 μm. DATA are expressed as mean ± SEM (n = 6 for the each group) Image collected & cropped by CiteAb from the following publication (//actaneurocomms.biomedcentral.com/articles/10.1186/s40478-018-0538-9), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Immunocytochemistry/ Immunofluorescence: Tyrosine Hydroxylase Antibody [NB300-109] - Tyrosine hydroxylase immunoreactivity in the deutocerebrum & medial antennal lobe tract.Tyrosine hydroxylase (TH) immunoreactivity is shown in magenta (A, D, G, J) & synapsin immunoreactivity in green (B, E, H, K). Corresponding merged images (C, F, I, L). A-C: Frontal sections through the antennal lobe (AL). Insets indicate single optical slice ( 0.05. b Heatmaps of proteins significantly enriched under toxic stress (10 µM CCCP; 20 nM rotenone) & their validation by western blot (Input, total levels & S-HSP90 bait isolate, chaperome network associated). Mean ± SEM, n = 3 individual values from the different experiments shown as points, t-test, ***p < 0.001; *p < 0.05. c Western blot & quantification of rotenone stress increase in the p-TH:TH ratio & its reduction by PU-H71 (200 nM). p-ERK/ERK, cell viability control; beta -actin, protein loading control. Mean ± SEM, n = 3 individual values from the different experiments shown as points, One-way ANOVA with Tukey’s post-hoc, ***p < 0.001; **p < 0.01. d Total intracellular dopamine levels in PD mDA neurons in conditions of toxic stress & under PU-H71 rescue; Mean ± SEM, n = 4–5 individual values from the different experiments shown as points, t-test, *p < 0.05. e PU-H71 treatment of rotenone- or CCCP-stressed mDA neurons significantly increases their viability, as measured by total ATP levels; means ± SEM, n = 3–8 from independent differentiations, t-test, ***p < 0.001; **p < 0.01; *p < 0.05 Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/30341316), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Immunocytochemistry/ Immunofluorescence: Tyrosine Hydroxylase Antibody [NB300-109] - ErbB4 protein expression in mesencephalic nuclei.The overview on the mesencephalon (B) shows dense ErbB4 expression (mAb-10, green channel) in the dopaminergic nuclei SNc & VTA that is clearly above background levels, whereas expression in the red nucleus is weaker. Higher magnification shows abundant immunoreactivity on neuropil (C–E, C'–E'). At 100x magnification, a dense network of ErbB4-positive neuropil surrounding a neuron (asterisk) is evident in the VTA (E”). The red channel shows neurofilament H-immunofluorescence in panels (B–E) & TH-immunofluorescence in (F–G). Co-immunolabeling reveals that subsets of TH-positive dopaminergic somata express ErbB4 in the VTA (F) & SNc (G); coexpressing neurons are indicated by arrowheads (F–G), whereas lack of ErbB4 signal is indicated by arrows (G). The location of the overview image within the monkey brain is indicated by a red rectangle in (A). The location of the profiles through mesencephalic nuclei is indicated by yellow boxes in (A) & by rectangles in (B). Images were obtained with a confocal microscope. Scale bar = 3 mm (B), 400 µm (C–E), 175 µm (C'–E', F–G), 70 µm (E”). Abbreviations: cerebral peduncle (cp), oculomotor nerve (3n), substantia nigra pars reticulata (SNr). Image collected & cropped by CiteAb from the following publication (//dx.plos.org/10.1371/journal.pone.0027337), licensed under a CC0-1.0 license. Not internally tested by Novus Biologicals.

Immunocytochemistry/ Immunofluorescence: Tyrosine Hydroxylase Antibody [NB300-109] - Tyrosine hydroxylase immunoreactivity in mushroom body.All panels show a right brain hemisphere, except panels M-O (posterior to top). Tyrosine hydroxylase (TH) immunoreactivity shown in magenta (A, D, G, J, M) & synapsin immunoreactivity (green: B, E, H, K, N). Corresponding merged images in C, F, I, L, O. A-C: Frontal sections through lateral protocerebrum. 2 groups of TH-positive cell bodies (DCa1 & 2) labeled. DCa2 appears to send axons ventrally (arrowhead). Superior lateral protocerebrum (SLP) as well as medial & lateral calyces (MCA & LCA) innervated by TH-positive fibers. D-F: Frontal sections through vertical lobe (VL) & parts of medial calyx (MCA), which receive many fine TH-positive fibers. G-I: Horizontal sections through a tip of vertical lobe & dorsal parts of calyces. Both calyces & vertical lobe innervated by fibrous TH-positive fibers. Note TH-immunoreactive fibers exclusively innervate synapsin-positive neuropil layers (NLs) of calyx where dendrites of Kenyon cells receive synaptic inputs from antennal-lobe projection neurons. J-L: Horizontal sections through calyces, ventral to panels G-I. Here, 3clusters of TH-positive cell bodies (DCa1, DCa2, & DSP1) visible. Immunoreactive fibers mainly invade anterior layers including gamma layer ( gamma ) in vertical lobe. M-O: Horizontal sections through distal portions of medial lobes (MLs), invaded by fine TH-positive fibers exhibiting moderate immunolabeling (arrows). in inferior medial protocerebrum (IMP) anterior to medial lobe, a pair of DIP1 clusters (triangles) is situated. D, dorsal; KFL, Kenyon fiber layer; LCA, lateral calyx; LO, lobula; M, medial; P, posterior; PED, pedunculus; SMP, superior medial protocerebrum. Scale bars = 100 μm. Image collected & cropped by CiteAb from following publication (//dx.plos.org/10.1371/journal.pone.0160531), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Immunohistochemistry: Tyrosine Hydroxylase Antibody [NB300-109] - Characterization of the nigrostriatal pathway of LRRK2 conditional transgenic mice. A, Representative TH immunohistochemistry of the midbrain coronal sections of 22-month-old LRRK2 GS & GSDA transgenic & age-matched littermate controls. B, C, Stereological assessment of TH-positive (B) & Nissl-positive (C) neurons in the SNpc (control, n = 9; GS, n = 9; GS/DA, n = 9). Data are the mean number of cells per region ± SEM, n = 9 mice per group. Statistical significance was determined by two-tailed unpaired Student’s t test. D, Representative images of TH immunostaining of nerve terminals in the striatum of LRRK2 conditional transgenic mice at 22 months of age. E, Quantitation of TH immunostaining in the striatum using ImageJ software (NIH; control, n = 7; GS, n = 7; GS/DA, n = 7). Differences between groups were assessed by two-way ANOVA. Bars represent the mean ± SEM (n ≥ 5 animals/genotype). n.s., Nonsignificant. Image collected & cropped by CiteAb from the following publication (//www.eneuro.org/lookup/doi/10.1523/ENEURO.0004-17.2017), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Reactivity:

Hu, Mu, Rt, Ch, Dr, I, Ma

Species Glossary

Reactivity: Hu, Mu, Rt, Ch, Dr, I, Ma

Applications:

, , , , , ,

Applications: , , , , , ,

Host:

Rabbit Polyclonal

Host: Rabbit Polyclonal

Sizes:

Sample Size Available

Sizes: Sample Size Available

Conjugate:

Unconjugated

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H00023435-M01

TDP-43/TARDBP Antibody (2E2-D3)

(3 Reviews)

(211 Publications)

0.1 mg

H00023435-M01

Western Blot: TDP-43/TARDBP Antibody (2E2-D3) [H00023435-M01] - PDI co-precipitates with TDP-43/TARDBP and is increased in mutant TDP-43 transgenic mouse spinal cords. Co-immunoprecipitation of wildtype and mutant Q331K TDP-43-mCherry from Neuro2a cell lysates using an anti-PDI antibody followed by TDP-43 immunoblot. Control immunoprecipitations were performed using untransfected (Untrans) or mCherry expressing cell lysates, buffer only with coprecipitating antibodies or TDP-43 Q331K cell lysates using an irrelevant, isotype-matched control antibody (IgG). Input control (2%) shows expression of mCherry-TDP43 in wildtype and Q331K cell lysates. Image collected and cropped by CiteAb from the following publication (//dx.plos.org/10.1371/journal.pone.0081170) licensed under a CC-BY license.

Immunocytochemistry/Immunofluorescence: TDP-43/TARDBP Antibody (2E2-D3) [H00023435-M01] - Analysis of monoclonal antibody to TARDBP on HeLa cell. Antibody concentration 10 ug/ml.

Immunohistochemistry-Paraffin: TDP-43/TARDBP Antibody (2E2-D3) [H00023435-M01] - TARDBP on formalin-fixed paraffin-embedded human leiomyosarcoma. [antibody concentration 3 ug/ml]

Western Blot: TDP-43/TARDBP Antibody (2E2-D3) [H00023435-M01] - Analysis of TARDBP expression in transfected 293T cell line by TARDBP monoclonal antibody (M01), clone 2E2-D3.Lane 1: TARDBP transfected lysate(44.7 KDa).Lane 2: Non-transfected lysate.

Immunohistochemistry-Paraffin: TDP-43/TARDBP Antibody (2E2-D3) [H00023435-M01] - Analysis of monoclonal antibody to TARDBP on formalin-fixed paraffin-embedded human leiomyosarcoma tissue Antibody concentration 3 ug/ml.

<b>Genetic Strategies Validation. </b>Knockdown Validated: TDP-43/TARDBP Antibody (2E2-D3) [H00023435-M01] - Analysis of TARDBP over-expressed 293 cell line, cotransfected with TARDBP Validated Chimera RNAi ( Cat # H00023435-R01V ) (Lane 2) or non-transfected control (Lane 1). Blot probed with TARDBP monoclonal antibody (M01), clone 2E2-D3 (Cat # H00023435-M01 ). GAPDH ( 36.1 kDa ) used as specificity and loading control.

ELISA: TDP-43/TARDBP Antibody (2E2-D3) [H00023435-M01] - Detection limit for recombinant GST tagged TARDBP is 0.3 ng/ml as a capture antibody.

Western Blot: TDP-43/TARDBP Antibody (2E2-D3) [H00023435-M01] - PDI co-precipitates with TDP-43 & is increased in mutant TDP-43 transgenic mouse spinal cords.(A) Co-immunoprecipitation of wildtype & mutant Q331K TDP-43-mCherry from Neuro2a cell lysates using an anti-PDI antibody followed by TDP-43 immunoblot. Control immunoprecipitations performed using untransfected (Untrans) or mCherry expressing cell lysates, buffer only with coprecipitating antibodies or TDP-43 Q331K cell lysates using an irrelevant, isotype-matched control antibody (IgG). Input control (2%) shows expression of mCherry-TDP43 in wildtype & Q331K cell lysates. Image collected & cropped by CiteAb from the following publication (//dx.plos.org/10.1371/journal.pone.0081170), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: TDP-43/TARDBP Antibody (2E2-D3) [H00023435-M01] - CLIP shows that TDP-43 directly interacts with translational target mRNAs. (A) Schematic diagram of the CLIP experiment. (B) Immunoblot showing specific IP of TDP-43 from MN1 cells under CLIP conditions. A TDP-43 band is specifically observed in the input & TDP-43 IP lanes from both untreated & UV-treated cells, but not in the IgG or anti-RBP X control lanes. RBP X is an IP of a different RNA-binding protein, which serves as an additional specificity control here. (C and D) Plots showing percentage of input mRNA in the TDP-43 IP for the mRNAs indicated in three separate CLIP assays from MN1 cells. Performing CLIP from UV-treated cells leads to significant recovery & enrichment relative to Gapdh for all mRNAs examined (C). In the absence of UV treatment, much less mRNA is recovered & no significant enrichment relative to Gapdh mRNA is observed. Note that the Y-axis scale in D is 1000× smaller than in C, indicating strong crosslinking dependence of mRNA co-immunoprecipitation (n = 3, s.e.m. error bars, P-values indicated in the plot, unpaired two-tailed t-test). Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/30357366), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: TDP-43/TARDBP Antibody (2E2-D3) [H00023435-M01] - SINE compounds partially rescue motor deficits in an animal model of ALS/FTD. (a) Schematic timeline for in vivo experiments. (b) Western blot demonstrating the expression of human TDP43 within the brains of AAV9-injected animals, which we have previously shown is largely restricted to neuronal cell types (Jackson et al.59). Full-length blots appear in Fig. S1. (c) The hang test measures the time it takes for animals to fall from grid-like scaffold when it is lifted & tilted. A single representative animal administered AAV9-TDP43 is shown; note the inability of the hind limbs to clasp the wire mesh. (d) TDP43 expression impaired motor performance on the hang test at 3 weeks, an effect that could be mitigated by 7.5 mg kg-1 KPT-350. (e) Rotarod testing at 4 weeks of age showed prominent deficits associated with TDP43 expression that were resistant to treatment with SINE compounds. n, number of animals per condition. ns, not significant, mean ± s.e.m. *p < 0.05, **p < 0.01, ***p < 0.001, one-way ANOVA with Bonferroni correction. Image collected & cropped by CiteAb from the following publication (//www.nature.com/articles/s41598-018-22858-w), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Reactivity:

Hu, Mu, Rt, Ba, I, Pm, Pp

Species Glossary

Reactivity: Hu, Mu, Rt, Ba, I, Pm, Pp

Applications:

, , , , , ,

Applications: , , , , , ,

Host:

Mouse Monoclonal

Host: Mouse Monoclonal

Conjugate:

Unconjugated

Validated by:

Validated by:

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NB100-56875

GAPDH Antibody

(5 Reviews)

(122 Publications)

0.1 mg

NB100-56875

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

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

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

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

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

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

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

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

Western Blot: GAPDH Antibody [NB100-56875] - ABCA1, ABCG1 & SR-BI protein expressions. a & b Hepatic protein expressions of ABCA1, ABCG1 & SR-BI were significantly decreased in COMT−/− mice at GD 18.5, compared to C57BL/6 J mice. Decreased hepatic ABCA1 expression was also observed at 10 days postpartum. ATI-5261 increased ABCA1 & ABCG1 expression in the liver at 10 days postpartum. c Placental protein expressions of ABCA1 & ABCG1 was reduced in COMT−/− mice, compared to C57BL/6 J mice. ATI-5261 treatment significantly increased ABCA1 levels in the placenta of COMT−/− mice. d Representative immunoblots of the corresponding proteins in the placenta with mouse RAW264.7 cell lysate included as positive control. Similar results were obtained when the experiment was repeated with lysates prepared from three batches of tissues. Data are presented as mean ± SEM. Groups (n = 8 in all groups) were compared using one-way ANOVA with post-hoc analysis (Tukey’s procedure). *, p < 0.05 Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/30237900), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

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

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

Reactivity:

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

Species Glossary

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

Applications:

, , , ,

Applications: , , , ,

Host:

Rabbit Polyclonal

Host: Rabbit Polyclonal

Alt Catalog#

IMG-5143A

Alt Catalog# IMG-5143A

Sizes:

Sample Size Available

Sizes: Sample Size Available

Conjugate:

Unconjugated

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NB300-146

Sodium Potassium ATPase Alpha 1 Antibody (464.6)

(4 Reviews)

(114 Publications)

0.05 ml

NB300-146

Immunohistochemistry: Sodium Potassium ATPase Alpha 1 Antibody (464.6) [NB300-146] - Staining of human enodmetrial glands within the uterus using NB300-146. Note the absence of staining in the surrounding myometrial smooth muscle.

Flow Cytometry: Sodium Potassium ATPase Alpha 1 Antibody (464.6) [NB300-146] - An intracellular stain was performed on NIH3T3 cells with Sodium Potassium ATPase Alpha 1 Antibody (464.6) NB300-146 (blue) and a matched isotype control MAB002 (orange). Cells were fixed with 4% PFA and then permeabilized with 0.1% saponin. Cells were incubated in an antibody dilution of 1 ug/mL for 30 minutes at room temperature, followed by Mouse IgG (H+L) Cross-Adsorbed Secondary Antibody, Dylight 550 (84540, Thermo Fisher).

Western Blot: Sodium Potassium ATPase Alpha 1 Antibody (464.6) [NB300-146] - Analysis detecting Na, K-ATPase (alpha) in porcine proximal tubule protein.

Immunocytochemistry/Immunofluorescence: Sodium Potassium ATPase Alpha 1 Antibody (464.6) [NB300-146] - Hek293 cells were fixed for 10 minutes using 10% formalin and then permeabilized for 5 minutes using 1X TBS + 0.5% Triton X-100. The cells were incubated with anti-Sodium Potassium ATPase Alpha 1 (464.6) at 10 ug/ml overnight at 4C and detected with an anti-mouse DyLight 488 (Green) at a 1:500 dilution. Actin was detected with Phalloidin 568 (Red) at a 1:200 dilution. Nuclei were counterstained with DAPI (Blue). Cells were imaged using a 40X objective.

Immunocytochemistry/Immunofluorescence: Sodium Potassium ATPase Alpha 1 Antibody (464.6) [NB300-146] - HeLa cells were fixed for 10 minutes using 10% formalin and then permeabilized for 5 minutes using 1X TBS + 0.5% Triton X-100. The cells were incubated with anti-Sodium Potassium ATPase Alpha 1 (464.6) at 10 ug/ml overnight at 4C and detected with an anti-mouse DyLight 488 (Green) at a 1:500 dilution. Actin was detected with Phalloidin 568 (Red) at a 1:200 dilution. Nuclei were counterstained with DAPI (Blue). Cells were imaged using a 40X objective.

Immunocytochemistry/Immunofluorescence: Sodium Potassium ATPase Alpha 1 Antibody (464.6) [NB300-146] - Detection of ATPA1 (Green) in HepG2 cells using NB300-146. Nuclei (Blue) were counterstained using Hoechst 33258.

Immunocytochemistry/Immunofluorescence: Sodium Potassium ATPase Alpha 1 Antibody (464.6) [NB300-146] - ARPE-19 cells cultured on transwell inserts for 4 weeks are not completely polarized. ARPE-19 cells were cultured up to 4 weeks on transwell inserts covered with laminin. The expression of Na+, K+-ATPase using anti-alpha1 antibody was observed mostly at the basolateral membrane. Scale bar: 10 um. Image collected and cropped by CiteAb from the following publication (//journal.frontiersin.org/article/10.3389/fphys.2016.00450/full), licensed under a CC-BY license.

Flow Cytometry: Sodium Potassium ATPase Alpha 1 Antibody (464.6) [NB300-146] - An intracellular stain was performed on A549 cells with NB300-146 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 1 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).

Flow Cytometry: Sodium Potassium ATPase Alpha 1 Antibody (464.6) [NB300-146] - An intracellular stain was performed on A549 cells with NBP2-61137AF647 (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. Image using the Alexa Fluor 647 form of this antibody.

Flow Cytometry: Sodium Potassium ATPase Alpha 1 Antibody (464.6) [NB300-146] - An intracellular stain was performed on A549 cells with - Purified NBP2-61137 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 1 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). Image using the Purified form of this antibody.

Flow Cytometry: Sodium Potassium ATPase Alpha 1 Antibody (464.6) [NB300-146] - An intracellular stain was performed on RCC4 cells with Sodium Potassium ATPase Alpha 1 Antibody (464.6) NB300-146 (blue) and a matched isotype control MAB002 (orange). Cells were fixed with 4% PFA and then permeabilized with 0.1% saponin. Cells were incubated in an antibody dilution of 1 ug/mL for 30 minutes at room temperature, followed by Mouse IgG (H+L) Cross-Adsorbed Secondary Antibody, Dylight 550 (84540, Thermo Fisher).

Flow Cytometry: Sodium Potassium ATPase Alpha 1 Antibody (464.6) [NB300-146] - An intracellular stain was performed on SK-MEL-28 cells with Sodium Potassium ATPase Alpha 1 Antibody (464.6) NB300-146 (blue) and a matched isotype control MAB002 (orange). Cells were fixed with 4% PFA and then permeabilized with 0.1% saponin. Cells were incubated in an antibody dilution of 1 ug/mL for 30 minutes at room temperature, followed by Mouse IgG (H+L) Cross-Adsorbed Secondary Antibody, Dylight 550 (84540, Thermo Fisher).

Sodium Potassium ATPase Alpha 1 Antibody (464.6) [NB300-146] - ARPE-19 cells cultured on transwell inserts for 4 weeks are not completely polarized. ARPE-19 cells were cultured up to 4 weeks on transwell inserts covered with laminin. The expression of Na+, K+-ATPase using anti-alpha1 antibody was observed mostly at the basolateral membrane. Scale bar: 10 um. Image collected and cropped by CiteAb from the following publication (//journal.frontiersin.org/article/10.3389/fphys.2016.00450/full), licensed under a CC-BY license.

Western Blot: Sodium Potassium ATPase Alpha 1 Antibody (464.6) [NB300-146] - Endothelial-mesenchymal transformation (EMT) of RCECs using specific endothelial-mesenchymal transformation medium (SEMTM). (A) Immunohistochemistry of the fibroblastic markers alpha -SMA & vimentin were characteristic of fibroblasts in EMT-RCECs compared to the hexogonal morphology of Fresh RCECs (Scale bar upper panel = 100 µm, Scale bar middle & bottom panel = 50 µm). (B) RT-PCR showed that both Fresh RCECs & EMT-RCECs expressed alpha -Sma. Original gel is shown in Supplemental Fig. S2. However, qRT-PCR in the lower panel shows alpha -Sma was significantly upregulated in EMT-RCECs. (C) Western blots showed that Fresh RCECs & EMT-RCECs expressed Vimentin, Atp1a1, a marker of differentiated endothelial cells, & b-actin. Original gel & blots are shown in Supplemental Figs S3, 4. Semiquantitative analysis shows significant upregulation of the protein levels of Vimentin (p = 0.048) & downregulation of the protein level of Atp1a1 (p = 0.0043). Data expressed as mean ± SD of three replicate experiments. Student’s t test (*p < 0.05, **p < 0.01). (n = 3). RCECs: rabbit corneal endothelial cells, alpha -SMA: smooth muscle alpha -actin. Atp1a1: Na,K‐ATPase alpha ‐subunit. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/30442918), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: Sodium Potassium ATPase Alpha 1 Antibody (464.6) [NB300-146] - SDS–PAGE western blot validation of the increased abundance of Annexin V, Na/K ATPase & alpha -tubulin in the EVs derived from TIS Cal51 cells compared with EVs derived from non-senescent non-treated controls. EVs isolated from TIS & control cells were immunoblotted to validate the protein expression of annexin V, Na/K ATPase & alpha -tubulin from the MS data. CD63 & HSP70 were used as loading controls. Densitometry was completed using Image J software (Fiji). All values are expressed as the mean of three independent experiments±s.e.m. The limit of ±1 skewness was set as normal distribution. Skewed data were transformed to Y=Log(Y) to fit a normal distribution. Results were analysed using the Student’s t-test with significant differences having a *P⩽0.05, **P⩽0.01, ***P⩽0.001. Image collected & cropped by CiteAb from the following publication (//www.nature.com/articles/oncsis201782), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Reactivity:

Hu, Mu, Rt, Po, Bv, Ca, Dr, Gp, Pm, Rb, Sh, Xp, Ye

Species Glossary

Reactivity: Hu, Mu, Rt, Po, Bv, Ca, Dr, Gp, Pm, Rb, Sh, Xp, Ye

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	NBP2-61137AF350
Alexa Fluor 405	NBP2-61137AF405
Alexa Fluor 488	NBP2-61137AF488
Alexa Fluor 532	NBP2-61137AF532
Alexa Fluor 594	NBP2-61137AF594
Alexa Fluor 647	NBP2-61137AF647
Alexa Fluor 700	NBP2-61137AF700
Alexa Fluor 750	NBP2-61137AF750
Allophycocyanin	NBP2-61137APC
Biotin	NBP2-61137B
CoraFluor 1	NBP2-61137CL1
DyLight 350	NBP2-61137UV
DyLight 405	NBP2-61137V
DyLight 488	NBP2-61137G
DyLight 550	NBP2-61137R
DyLight 594	NBP2-61137DL594
DyLight 650	NBP2-61137C
DyLight 680	NBP2-61137FR
DyLight 755	NBP2-61137IR
FITC	NBP2-61137F
HRP	NBP2-61137H
Janelia Fluor 525	NBP2-61137JF525
Janelia Fluor 549	NBP2-61137JF549
Janelia Fluor 585	NBP2-61137JF585
Janelia Fluor 635	NBP2-61137JF635
Janelia Fluor 646	NBP2-61137JF646
Janelia Fluor 669	NBP2-61137JF669
PE	NBP2-61137PE
PerCP	NBP2-61137PCP
mFluor Violet 450 SE	NBP2-61137MFV450
mFluor Violet 500 SE	NBP2-61137MFV500
mFluor Violet 610 SE	NBP2-61137MFV610

Available Formulations

Formulation	Catalog #	Availability	Price
BSA Free	NBP2-61137
Azide and BSA Free	NBP2-80956

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NB300-143

GAP-43 Antibody

(1 Review)

(101 Publications)

0.1 ml

NB300-143

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

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

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

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

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

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

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

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

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

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

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

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

Reactivity:

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

Species Glossary

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

Applications:

, , ,

Applications: , , ,

Host:

Rabbit Polyclonal

Host: Rabbit Polyclonal

Sizes:

Sample Size Available

Sizes: Sample Size Available

Conjugate:

Unconjugated

Available Conjugates:

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

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NB100-355

RPE65 Antibody (401.8B11.3D9) - BSA Free

(7 Reviews)

(97 Publications)

0.2 ml

NB100-355

Immunohistochemistry-Paraffin: RPE65 Antibody (401.8B11.3D9) - BSA Free [NB100-355] - Analysis of FFPE human glioblastoma tissue section using 1:500 dilution of RPE65 [401.8B11.3D9] antibody on a Bond Rx autostainer (Leica Biosystems). The assay involved 20 minutes of heat induced antigen retrieval (HIER) with 10mM sodium citrate buffer (pH 6.0) and endogenous peroxidase quenching using peroxide block. The sections were incubated with primary antibody for 30 minutes. Bond Polymer Refine Detection (Leica Biosystems) and DAB were used for signal detection which followed counterstaining with hematoxylin. Whole slide scanning and capturing of representative images (20X) were performed using Aperio AT2 (Leica Biosystems).

$Western Blot: RPE65 Antibody (401.8B11.3D9) - BSA Free [NB100-355] - WB analysis of RPE65 in 20ug lysate of COS7 cells expressing recombinant Human RPE65 (Lane 1) and 5ug of Bovine retinal pigment epithelium membrane fraction (Lane 2). Blot processed for detection with alkaline phosphatase conjugated goat-anti Mouse IgG secondary antibody and NBT/BCIP substrate.$

Immunocytochemistry/Immunofluorescence: RPE65 Antibody (401.8B11.3D9) - BSA Free [NB100-355] - ICC-IF analysis of cultured ARPE19 cells, a spontaneously arising human retinal pigment epithelia cell line - 10 minutes fixation in 4% PFA, 10 minutes permeabilization in PBS containing 0.2% Triton X-100 (PBS-T), 1 hour blocking in 10% normal goat serum containing 1% BSA in PBS-T, 1:100 primary antibody dilution in PBS, ON 4C incubation.

Immunohistochemistry-Frozen: RPE65 Antibody (401.8B11.3D9) - BSA Free [NB100-355] - Staining of RPE65 in a cryosection of mouse retina tissue using RPE65 antibody (clone 401.8B11.3D9).

Immunohistochemistry: RPE65 Antibody (401.8B11.3D9) - BSA Free [NB100-355] - Zebrafish brain ventricular area labeled with mouse anti-RPE65 (1:100). This image was submitted through a verified customer review.

Simple Western: RPE65 Antibody (401.8B11.3D9) - BSA Free [NB100-355] - iPSC-RPE from all donors express RPE marker proteins. iPSC-RPE from the patient, the patients mom, the patients dad, and the three unrelated, unaffected controls all expressed RPE65. The negative control (iPSCs) had no detectable RPE65 protein expression. Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/29540715/) licensed under a CC-BY license.

<b>Genetic Strategies Validation. </b>Knockout Validated: RPE65 Antibody (401.8B11.3D9) - BSA Free [NB100-355] - Immunoblotting showing the expression of RPE-specific proteins BEST1 (NB300-164), RPE65 (NB100-355), CRALBP, and the loading control beta-Actin in iPSC-RPE cells. Two gels/blots in the same panel were prepared from the same cell lysate of each PSC-RPE to detect BEST1 + beta-Actin, and RPE65 + CRALBP, respectively. Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/34061021/) licensed under a CC-BY license.

Western Blot: RPE65 Antibody (401.8B11.3D9) - BSA Free [NB100-355] - Expression of RPE-specific marker proteins in hPSC-RPE & iPSC-RPE cells.(a–b) Immunoblotting showing the expression of RPE-specific proteins BEST1, RPE65, CRALBP, & the loading control beta -Actin in hPSC-RPE (a) & iPSC-RPE (b) cells. Two gels/blots in the same panel were prepared from the same cell lysate of each PSC-RPE to detect BEST1 + beta -Actin, & RPE65 + CRALBP, respectively. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/34061021), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Immunocytochemistry/ Immunofluorescence: RPE65 Antibody (401.8B11.3D9) - BSA Free [NB100-355] - BMP5 induces ectopic RPE development in the central NR at optic cup stages. (A,B) Peripheral, untreated chick eye at E8 showing pigmentation & MITF expression being restricted to the outer layer of the eye. The arrowheads indicate the peripheral NR. (C-F) Higher magnification of the central chick eye at E8 showing the pigmented RPE, where RPE65 protein is detected (arrows). Faint Wnt2b & strong Vsx2 expression is detected in the central NR. The arrows indicate the RPE. (G,H) Following BMP5 application at E3.5/4, the NR detached (arrowhead) & MITF protein is now detected in the central NR (cNR). Note that a part of the cNR has RPE-like morphology (eRPE). (I-L) Higher magnification images of the eRPE. Ectopic pigment granulae, RPE65 protein & strong Wnt2b expression are detected in this region, whereas Vsx2 expression is downregulated (arrowheads). (M-O) Untreated chick eye at E8 showing pigmentation & MITF (arrow) & VSX2 protein distribution, restricted to the RPE & NR, respectively. (P-R) Following BMP5 application at E3.5/4, ectopic pigmentation & nuclear MITF protein are detected in the inner optic cup (arrowheads), whereas VSX2 protein is only weakly or not detected. The arrows indicate the RPE. (S) Graphical representation of the average thickness of the inner layer of the untreated (control) & BMP5-treated eye at E8. All expression pattern studies included n≥5. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/28546339), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Reactivity:

Hu, Mu, Rt, Po, Bv, Ca, Ch, Pm, Xp

Species Glossary

Reactivity: Hu, Mu, Rt, Po, Bv, Ca, Ch, Pm, Xp

Applications:

, , , , , , , , ,

Applications: , , , , , , , , ,

Host:

Mouse Monoclonal

Host: Mouse Monoclonal

Sizes:

Sample Size Available

Sizes: Sample Size Available

Conjugate:

Unconjugated

Available Conjugates:

Validated by:

Validated by:

Conjugate	Catalog #	Availability	Size	Price
Alexa Fluor 350	NB100-355AF350
Alexa Fluor 405	NB100-355AF405
Alexa Fluor 488	NB100-355AF488
Alexa Fluor 532	NB100-355AF532
Alexa Fluor 594	NB100-355AF594
Alexa Fluor 647	NB100-355AF647
Alexa Fluor 700	NB100-355AF700
Alexa Fluor 750	NB100-355AF750
Allophycocyanin	NB100-355APC
Biotin	NB100-355B
DyLight 350	NB100-355UV
DyLight 405	NB100-355V
DyLight 488	NB100-355G
DyLight 550	NB100-355R
DyLight 594	NB100-355DL594
DyLight 650	NB100-355C
DyLight 680	NB100-355FR
DyLight 755	NB100-355IR
FITC	NB100-355F
HRP	NB100-355H
Janelia Fluor 525	NB100-355JF525
Janelia Fluor 549	NB100-355JF549
Janelia Fluor 585	NB100-355JF585
Janelia Fluor 635	NB100-355JF635
Janelia Fluor 646	NB100-355JF646
Janelia Fluor 669	NB100-355JF669
PE	NB100-355PE
PerCP	NB100-355PCP

Available Formulations

Formulation	Catalog #	Availability	Price
BSA Free	NB100-355SS
Azide and BSA Free	NBP2-80931

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NB300-110

Tyrosine Hydroxylase Antibody

(5 Reviews)

(92 Publications)

0.1 ml

NB300-110

Immunocytochemistry/Immunofluorescence: Tyrosine Hydroxylase Antibody [NB300-110] - Alpha-Synuclein overexpression or intracerebral seeding impacts the dopaminergic system. Increased levels of ser129-phosphosynuclein in the substantia nigra (arrows) indicate alpha-syn stress in PFF injected animals. Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/30050065/) licensed under a CC-BY license.

Immunohistochemistry: Tyrosine Hydroxylase Antibody [NB300-110] - Mouse cryo-sections. Antibody at 1:500. Secondary antibody: dk-anti-sp Alexa Fluor488 at 1:500; 1 h. IHC image submitted by a verified customer review.

Immunocytochemistry/Immunofluorescence: Tyrosine Hydroxylase Antibody [NB300-110] - Nmnat by itself does not protect dopaminergic neurons from MPP+ toxicity. Similar transduction efficiencies of the different lentiviruses were confirmed by quantifying the number of TH+ and GFP+ cells following transduction of dopaminergic cultures. Quantification of TH+ cell bodies and (E) TH+ neurites show that only WldS-transduced cultures protected neurites against MPP+. Data are normalized to control cultures and denote the mean +/- SEM of representative determinations made in three separate cultures. *p 99.8% posterior probability); green, expressed above baseline in human (>99.8% posterior probability); gray, not expressed above baseline.(F) Validation of LMO3 expression by immunohistochemistry in a subset of TH+ neurons in the E18.5 mouse ventral midbrain (scale bar left, 100 μm; right, 20 μm).(G) Validation of BNC2 expression by immunohistochemistry in TH+ neurons in the E18.5 mouse ventral midbrain (scale bar left, 100 μm; right, 20 μm). Image collected & cropped by CiteAb from the following publication (//linkinghub.elsevier.com/retrieve/pii/S0092867416313095), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Immunocytochemistry/ Immunofluorescence: Tyrosine Hydroxylase Antibody [NB300-110] - Developmental song exposure & social context affect cFOS expression in TH neurons of the caudal VTA. Sagittal drawings (A,C) & photomicrographs of tyrosine hydroxylase (TH; green label) expression (B,D) in the ventral tegmental area (VTA) & periaqueductal gray (PAG; panels A,B), & the substantia nigra pars compacta (SNc) & locus coeruleus (LC; panels C,D). (E) Examples of co-localized expression of TH (green) & cFOS (red) in the caudal VTA of a normally-reared bird that heard silence (left panel), UD song (middle panel; UD song) & FD song (FD; right panel). White arrows indicate examples of colocalized expression. (F) Percent of TH neurons co-localized with cFOS in the caudal VTA (cVTA), rostral VTA (rVTA) & SNc. Box-and-whisker plots for normally-reared (yellow colors) & song-naïve (green colors) hearing UD (UD; lighter colors) or female-directed (FD; darker colors) songs. Each box spans the interquartile range, horizontal white lines indicate the median & whiskers show the minima & maxima. Levels of cFOS expression in TH neurons for silence controls are plotted as the mean (gray dashed line) +/− standard error (gray boxes). *Indicates a significant difference at p 99.8% posterior probability); green, expressed above baseline in human (>99.8% posterior probability); gray, not expressed above baseline.(F) Validation of LMO3 expression by immunohistochemistry in a subset of TH+ neurons in the E18.5 mouse ventral midbrain (scale bar left, 100 μm; right, 20 μm).(G) Validation of BNC2 expression by immunohistochemistry in TH+ neurons in the E18.5 mouse ventral midbrain (scale bar left, 100 μm; right, 20 μm). Image collected & cropped by CiteAb from the following publication (//linkinghub.elsevier.com/retrieve/pii/S0092867416313095), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Immunocytochemistry/ Immunofluorescence: Tyrosine Hydroxylase Antibody [NB300-110] - Conversion of hNES cells into hPRogFPM & their differentiation into midbrain dopaminergic neurons. a Schematic representation of the conversion & differentiation protocols. b, cRT-qPCR analysis at day 8, showing the expression of midbrain-hindbrain TFs, such as OTX2, GBX2, LMX1A, & FOXA2 (b), as well as the dopaminergic neuron markers, NR4A2, TH, SLC18A22, & SLC6A3 (c). d Immunocytochemistry analysis of the presence of OTX2 & TH in control unconverted NES cultures, compared with NES cells converted with SAF+Dkk1 & differentiated until day 8. e, f Percentage of OTX2+ & TH+ cells in the conditions in d. P = 0.02673 (e), P = 0.03233 (f), n = 3. g–i Expression of the key midbrain TFs, LMX1A, NR4A2, & PBX1, in TH+cells derived from SAI2-NES cells after conversion & differentiation. j, k TH+ cells express the mature neuronal marker, MAP2 (j), & some acquire mature neuronal morphologies, with long processes & varicosities at day 8 (k). Scale 50μm. Box plots (b, c, e, f): Center line, median; hinges, 25% & 75% quartiles; whiskers, 1.5 interquartile range. Statistics: (b, c) ANOVA, followed by pair-wise t-test with Bonferroni correction for multiple testing. (e, f). Two sample t-test; *P ≤ 0,05; **P ≤ 0,01; ***P ≤ 0,001. N = 3 (GBX2, FOXA2, TH, SLC6A3), n = 4 (LMX1A, OTX2, NR4A2, SLC18A2) Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/29968757), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Immunocytochemistry/ Immunofluorescence: Tyrosine Hydroxylase Antibody [NB300-110] - Comparison of Mouse & Human Dopaminergic Neuronal Development(A) WNT1 compartments marking lateral population of the floor plate in human & mouse tissue (scale bar, 100 μm).(B) Bar plot of cell types of the human & mouse dopaminergic lineage, showing the expression of key genes. Bars show average mRNA expression, scaled to the absolute molecule counts indicated on the right axis. Error bars show SEM.(C) Validation of mNbM by in situ hybridization for Igfbpl1 & Nhlh1 (scale bar, 50 μm).(D) Neuroblasts in human & mouse ventral midbrain (scale bar, 100 μm; magnification, 20 μm).(E) Selected genes showing similar (left) or distinct (right) expression in mouse & human ventral midbrain. Blue, expressed above baseline in mouse (>99.8% posterior probability); green, expressed above baseline in human (>99.8% posterior probability); gray, not expressed above baseline.(F) Validation of LMO3 expression by immunohistochemistry in a subset of TH+ neurons in the E18.5 mouse ventral midbrain (scale bar left, 100 μm; right, 20 μm).(G) Validation of BNC2 expression by immunohistochemistry in TH+ neurons in the E18.5 mouse ventral midbrain (scale bar left, 100 μm; right, 20 μm). Image collected & cropped by CiteAb from the following publication (//linkinghub.elsevier.com/retrieve/pii/S0092867416313095), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Reactivity:

Hu, Mu, Rt, Am, Av, Ma, Rb, Re, Ch

Species Glossary

Reactivity: Hu, Mu, Rt, Am, Av, Ma, Rb, Re, Ch

Applications:

, , , ,

Applications: , , , ,

Host:

Sheep Polyclonal

Host: Sheep Polyclonal

Alt Catalog#

IMG-5070

Alt Catalog# IMG-5070

Sizes:

Sample Size Available

Sizes: Sample Size Available

Conjugate:

Unconjugated

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NBP2-27103

GAPDH Antibody (13H12) - BSA Free

(3 Reviews)

(34 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.

Western Blot: GAPDH Antibody (13H12) - BSA Free [NBP2-27103] - Effect of AAT on Mcl-1 phosphorylation, the activity of MAP kinases & caspases.Neutrophils from healthy volunteers (2.5 × 106/ml) were cultured in medium supplemented with patient serum (3 mg protein/ml; 1%) & those containing low levels of AAT (AAT-reduce serum; 1%) in the presence of STS (0.2 μM). After 3 h, the expression of pMcl-1 (A, n = 7), pAkt (B, n = 8) & pERK1/2 (C, n = 10) were analyzed by western blot. Expression levels of the phosphorylated proteins were normalized to that of the unphosphorylated forms. GAPDH was used as loading control. One representative blot is displayed. *p<0.05; **p<0.01; n.s. = not significant. D. After 4 h of incubation the activities of caspase-9 & caspase-3/-7 were quantified. Results are presented as means ± SEM of eight independent experiments. No significant differences were found (one-way ANOVA with Newman keuls post-hoc test). Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/28493974), 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
CoraFluor 1	NBP2-27103CL1
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 525	NBP2-27103JF525
Janelia Fluor 549	NBP2-27103JF549
Janelia Fluor 585	NBP2-27103JF585
Janelia Fluor 635	NBP2-27103JF635
Janelia Fluor 646	NBP2-27103JF646
Janelia Fluor 669	NBP2-27103JF669
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)

(87 Publications)

0.2 mg

NB600-502

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

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

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

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

Reactivity:

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

Species Glossary

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

Applications:

, , , , ,

Applications: , , , , ,

Host:

Mouse Monoclonal

Host: Mouse Monoclonal

Conjugate:

Unconjugated

Available Conjugates:

Conjugate	Catalog #	Availability	Size	Price
Alexa Fluor 350	NB600-502AF350-0.2ml
Alexa Fluor 405	NB600-502AF405-0.2ml
Alexa Fluor 488	NB600-502AF488-0.2ml
Alexa Fluor 532	NB600-502AF532-0.2ml
Alexa Fluor 594	NB600-502AF594-0.2ml
Alexa Fluor 647	NB600-502AF647-0.2ml
Alexa Fluor 700	NB600-502AF700-0.2ml
Alexa Fluor 750	NB600-502AF750-0.2ml
Biotin	NB600-502B-0.2ml
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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NB300-232

SCP3/SYCP3 Antibody - BSA Free

(2 Reviews)

(82 Publications)

0.1 ml

NB300-232

Immunocytochemistry/Immunofluorescence: SCP3/SYCP3 Antibody [NB300-232] - Exposure to DEHP impairs meiotic progression of oocytes from pachytene to diplotene. Immunolabeling of the oocyte chromosomes with anti-SYCP3 antibody (red) and Hoechst 33342 (blue). All experiments were repeated at least three times independently. (* P600 spermatocytes in each stage. b, c The immunostaining of SYCP3 in the testicular sections (b) & surface-spread chromatin preparations of Uhrf1 deletion & control mice (c); d the percentage of spermatocytes with abnormal SYCP3 location. e Double immunofluorescence of testicular spread preparations of the adult mice, SYCP3 (green) & SYCP1 (red). f The percentage of spermatocytes with abnormal SYCP1 location. Lep leptotene, Zyg zygotene, Pac pachytene, Dip diplotene. Data are presented as mean ± SEM of three mice. ***p ≤ 0.001. Scale bar, 25 μm in b, 5 μm in c, e. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/32081844), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Immunocytochemistry/ Immunofluorescence: SCP3/SYCP3 Antibody - BSA Free [NB300-232] - Dynamic expression of germ cell markers in human fetal ovaries. (A) Histological sections of human ovaries at W10.5, W14, W17 & W21.5, immunostained for the early germ cell marker (nuclear) POU5F1 (red) & late germ cell marker (cytoplasmic) DDX4 (green). In zone 1, most germ cells are POU5F1+DDX4−/low; in zone 2 & 3, most germ cells are DDX4+. Several germ cells in zone 3 have developed into primordial follicles. Inserts are magnifications of the dotted boxes. (B) Histological sections of human ovaries at W10.5, W14, W17 & W21.5, immunostained for the meiotic markers H2AFX (red) & SYCP3 (green). Inserts are magnifications of the dotted boxes. Note the presence of autofluorescent red blood cells. Scale bars are 200 µm & in the magnified inserts 20 µm. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/26834021), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Immunocytochemistry/ Immunofluorescence: SCP3/SYCP3 Antibody - BSA Free [NB300-232] - CYP51 regulates the expression of the meiosis-specific cohesin subunits REC8 & STAG3. (A,B) RS21745 treatment decreased REC8 & STAG3 expression. Ovaries at 14.5 dpc were cultured with 10 μM RS21745 for 3 days in vitro. (A) Expression of the cohesin subunits following RS21745 treatment by qRT-PCR. All qRT-PCR values were normalized to beta -actin & were expressed as a relative ratio to the control; the means±s.e.m. of 3 values are shown. (B) Expression of REC8 & STAG3 following RS21745 treatment by western blotting GAPDH was used as internal reference. (C–F) Inhibition of CYP51 disturbed the distribution of both REC8 & STAG3 on the chromosomes. (C,E) In the control groups, REC8 & STAG3 expression was observed at high levels in zygotene oocytes. In the CYP51 inhibition groups, the cohesin signals were absent in zygotene cells. (D,F) The percentage of REC8-positive or STAG3-positive oocytes at the zygotene stage was recorded. Unidentified germ cells were not included in the analyses. Scale bars: 10 μm. The data are presented as the means±s.e.m. of 3–9 ovaries per group. Asterisk (*) denotes a statistically significant difference between the control & the treatment groups. ***P<0.001 (t-test). Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/30420384), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Immunocytochemistry/ Immunofluorescence: SCP3/SYCP3 Antibody - BSA Free [NB300-232] - Induction of meiosis is compromised in the cortical germ cells of D17 embryos subject to oestrogen level alterations. (A) D17 (HH43) left gonad sections immunostained for gamma H2AX (green) & P63 (red); nuclei are counterstained with DAPI (blue). (B) Sections from the D17 (HH43) left gonad shown in A immunostained for gamma H2AX (green) & SYCP3 (red). ZW-WT, ZW wild type; ZW-Fa, ZW treated with fadrozole from D7-7.5 (HH31); ZW-E2, ZW treated with beta -oestradiol at D7-7.5; ZZ-E2, ZZ treated with beta -oestradiol at D7-7.5; ZW-Fa(sr), ZW, partially sex-reversed gonad, treated with fadrozole at D4; ZZ-E2(sr), ZZ, partially sex-reversed gonad, treated with beta -oestradiol at D4. All gonadal models have a cortical domain containing germ cells. In ZW-Fa ovary & ZW-E2 ovary, most cortical germ cells express SYCP3 like the ZW-WT control. In ZW-Fa(sr) ovotestis, very few germ cells express gamma H2AX & SYCP3 (orange dotted circled areas). In ZZ-E2(sr) ovotestis & ZZ-E2 testis overlain by a cortex, some cortical germ cells express gamma H2AX but none expresses SYCP3. White dotted line highlights the cortical domain borders. See Fig. S4 for the medullary structure of the ZZ-E2, ZW-Fa(sr) & ZZ-E2(sr) models. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/32001442), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Immunocytochemistry/ Immunofluorescence: SCP3/SYCP3 Antibody - BSA Free [NB300-232] - Exposure to DEHP impairs meiotic progression of oocytes from pachytene to diplotene. (a) Immunolabeling of the oocyte chromosomes with anti-SYCP3 antibody (red) & Hoechst 33342 (blue). (b) Effect of DEHP on meiotic progression of oocytes throughout prophase I stages; percentage of each group is presented as mean±SD. Control: 36.27±0.80% pachytene & 54.99±0.66% diplotene; 10 μM & 100 μM DEHP 57.79±4.22% & 56.62±6.62% pachytene & 39.79±4.22% & 36.62±6.62% diplotene, respectively. (c) Representative WB showing the effect of DEHP on the expression of germ cell (DAZL) & meiotic (STRA8 & SCP3) specific proteins. (d) Effect of DEHP on the levels of mRNA in the ovarian tissues of germ cell (Mvh & Dazl), meiotic (Stra8, Rec8, Scp1 & Scp3). All experiments were repeated at least three times independently. (* P<0.05; ** P<0.01) Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/28771232), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Immunocytochemistry/ Immunofluorescence: SCP3/SYCP3 Antibody - BSA Free [NB300-232] - Loss of lamin C2 has no effect on meiotic telomere attachment.(A) 3D-preserved swab preparations showing wildtype (A) & knockout (A′) spermatocytes simultaneously labelled with anti-TRF1 & SUN1 antibodies. As in the wildtype, in lamin C2−/− spermatocytes virtual all telomeres appear to be attached to the NE as indicated by co-localisation of TRF1 & SUN1 signals. Scale bars 5 µm. (B) Quantifications of co-localised & non-co-localised TRF1/SUN1 signals (see A) revealed that ratios of co-localised to non-co-localised spots comparing wildtype & knockout spermatocytes show no significant difference (wildtype n = 33; lamin C2−/− n = 45; Pearson's Chi2 test p-value: 0.799). (C,D) Chromosome spread preparations of pachytene-like lamin C2−/− spermatocytes showing that all telomeres are associated with SUN1. In (C) TeloFISH & in (D) anti-SUN1 staining in co-localisation with SYCP3. Scale bars 10 µm. Image collected & cropped by CiteAb from the following publication (//dx.plos.org/10.1371/journal.pgen.1003261), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Immunohistochemistry: SCP3/SYCP3 Antibody - BSA Free [NB300-232] - FANCM expression in human fetal ovaries.(A) Relative FANCM mRNA abundance was measured by RT-qPCR in human fetal ovaries from 5 to 32 weeks post-fertilization (wpf). (B) Germ cells (D2-40+) & somatic cells (D2-40-) were sorted from three ovaries ranging from 8 to 12 wpf & FANCM expression was measured. ACTB was used to normalize FANCM expression in all samples. Dots represent different ovaries & the mean is indicated by the line. (C) Immunohistochemistry of FANCM in human fetal & adult ovaries. Fetal ovaries at 8 & 22 wpf & adult ovaries were studied. FANCM positive cells appear in yellow/brown color (monoclonal FANCM CV5.1 antibody, Novus Biologicals, Abingdon, UK). Ovarian sections were counterstained with hematoxylin (blue staining). Oo, oogonia; Pa, oocyte at the pachytene stage of meiosis I, D, oocyte at the diplotene stage of meiosis I; Pr, oocyte in primordial follicle. (D) Co-staining in 22 wpf ovaries, for FANCM (purple) & DDX4 (brown) confirmed the germ cell identity of FANCM-positive cells (left). Successive staining for FANCM & SYCP3 in the same section (panels a & b). Negative control performed with non-immune mouse IgG (right). Scale bar: 10 μm. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/29231814), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Reactivity:

Hu, Mu, Rt, Po, Bv, Ch, Fe, Pa

Species Glossary

Reactivity: Hu, Mu, Rt, Po, Bv, Ch, Fe, Pa

Applications:

, , , ,

Applications: , , , ,

Host:

Rabbit Polyclonal

Host: Rabbit Polyclonal

Sizes:

Sample Size Available

Sizes: Sample Size Available

Conjugate:

Unconjugated

Available Conjugates:

Conjugate	Catalog #	Availability	Size	Price
Alexa Fluor 350	NB300-232AF350
Alexa Fluor 405	NB300-232AF405
Alexa Fluor 488	NB300-232AF488
Alexa Fluor 532	NB300-232AF532
Alexa Fluor 594	NB300-232AF594
Alexa Fluor 647	NB300-232AF647
Alexa Fluor 700	NB300-232AF700
Alexa Fluor 750	NB300-232AF750
Allophycocyanin	NB300-232APC
Biotin	NB300-232B
CoraFluor 1	NB300-232CL1
DyLight 350	NB300-232UV
DyLight 405	NB300-232V
DyLight 488	NB300-232G
DyLight 550	NB300-232R
DyLight 594	NB300-232DL594
DyLight 650	NB300-232C
DyLight 680	NB300-232FR
DyLight 755	NB300-232IR
FITC	NB300-232F
HRP	NB300-232H
Janelia Fluor 525	NB300-232JF525
Janelia Fluor 549	NB300-232JF549
Janelia Fluor 585	NB300-232JF585
Janelia Fluor 635	NB300-232JF635
Janelia Fluor 646	NB300-232JF646
Janelia Fluor 669	NB300-232JF669
PE	NB300-232PE
PerCP	NB300-232PCP
mFluor Violet 450 SE	NB300-232MFV450
mFluor Violet 500 SE	NB300-232MFV500
mFluor Violet 610 SE	NB300-232MFV610

Available Formulations

Formulation	Catalog #	Availability	Price
BSA Free	NB300-232SS

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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)

PINK1 Antibody - BSA Free

Tyrosine Hydroxylase Antibody

TDP-43/TARDBP Antibody (2E2-D3)

GAPDH Antibody

Sodium Potassium ATPase Alpha 1 Antibody (464.6)

GAP-43 Antibody

RPE65 Antibody (401.8B11.3D9) - BSA Free

Tyrosine Hydroxylase Antibody

GAPDH Antibody (13H12) - BSA Free

GAPDH Antibody (6C5cc)

SCP3/SYCP3 Antibody - BSA Free