Neuroscience reagents: Novus Biologicals

NB300-221

GAPDH Antibody (1D4) - BSA Free

(19 Reviews)

(455 Publications)

0.1 ml

NB300-221

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

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

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

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

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

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

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

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

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

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

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

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

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

Reactivity:

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

Species Glossary

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

Applications:

, , , , , , ,

Applications: , , , , , , ,

Host:

Mouse Monoclonal

Host: Mouse Monoclonal

Sizes:

Sample Size Available

Sizes: Sample Size Available

Conjugate:

Unconjugated

Available Formulations

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BSA Free	NB300-221SS

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NB100-2323

IRE1 alpha [p Ser724] Antibody - BSA Free

(9 Reviews)

(372 Publications)

0.1 ml

NB100-2323

P-Ire1a activation correlates with WFS1 cell expression. Cryosections of retina from 12 month old Wfs1+/+ and Wfs1-/- mouse were immunostained with anti-P-Ire1a antibody (red). DAPI was used for staining of cell nuclei (blue). RPE, retinal pigment epithelium; ONL, outer nuclear layer; INL, inner nuclear layer, RGC, retinal ganglion cells. Scale bars=50 um. Image collected and cropped by CiteAb from the following publication (//doi.org/10.1371/journal.pone.0097222) licensed under a CC-BY license.

Hepatic ER stress markers with cachexia progression. ER stress markers Bip, IRE1a, ATF6p50 and CHOP were examined in the liver of non, pre and severely cachectic mice. (n = 6-8 per group, p < 0.05) Dotted line indicates levels of Non-cachectic mice. Non = Non-Cachectic Apc Min/+ Sev = severely cachectic Apc Min/+; * denotes significantly different from Non-cachectic Apc Min/+ Image collected and cropped by CiteAb from the following publication (//doi.org/10.1371/journal.pone.0119888) licensed under a CC-BY license.

IRF-1 plays a central role in ER stress-mediated modulation of VCAM-1 expression by TGRL. HAEC were conditioned for 4 hr with TNFa (0.3 ng/ml) E: CHOP knockdown decreased TNFa-induced VCAM-1 expression. n=4. **P<0.01 vs. siCtrl+TNFa. Shown are representative blots from 3 independent experiments with similar results. Image collected and cropped by CiteAb from the following publication (//doi.org/10.1371/journal.pone.0078322) licensed under a CC-BY license.

Analysis using HRP conjugate of NB100-2323. Detection of phosphorylated IRE-1 alpha using NB100-2323. Lane 1: COS-7 untransfected Lane 2: COS-7 expressing wild-type IRE1 alpha Lane 3: COS-7 expressing kinase-dead IRE1 alpha. Theoretical molecular weight: 110 kDa.

<b>Biological Strategies Validation. </b>Analysis of anti-IRE1 alpha (pSer724) using Lot AN and AO of NB100-2323. HeLa cells were treated (+) or untreated (-) with 10 mM DTT for 60 min to activate the UPR. Total protein was separated on a 7.5% gel by SDS-PAGE, transferred to PVDF membrane and blocked in 5% BSA in TBST. The membrane was probed with 2.0 ug/ml antibody in 5% BSA, and detected with an anti-rabbit HRP secondary antibody using chemiluminescence. Theoretical molecular weight: 110 kDa.

Regulation of the unfolded protein response by KLF15. Western analysis of UPR activity in WT versus KLF15-/- primary hepatocytes. Hepatocytes were isolated from standard chow-fed 4-month-old male WT and KLF15 -/- mice. Two individual experiments were performed in triplicate; each lane indicates a technical replicate. Image collected and cropped by CiteAb from the following publication (//doi.org/10.1371/journal.pone.0077851) licensed under a CC-BY license.

HeLa cell lysate, 20 ug. Antibody at 1:1000, 1% skim milk in TBST, overnight incubation at 4C. WB image submitted by a verified customer review.

<b>Biological Strategies Validation. </b>Detection in Min6 cells which were treated with different concentrations of glucose for 3 hours prior to lysates preparation.

IRE1 (pS724) was detected in immersion fixed paraffin-embedded sections of human spleen using Rabbit Anti-Human IRE1 (pS724) polyclonal Antibody (Catalog # NB100-2323) at 1:300 for 1 hour at room temperature followed by incubation with the Anti-Rabbit IgG VisUCyte™ HRP Polymer Antibody (Catalog # VC003). Tissue was stained using DAB (brown) and counterstained with hematoxylin (blue). Specific staining was localized to the perinuclear cytoplasm in splenocytes.

Hepatic ER Stress.Representative hepatic western blots of BiP, phosphorylated (Ser51), total EIF2 alpha and phosphorylated:total EIF2 alpha , phosphorylated (Ser724), total IRE1 alpha and phosphorylated:total IRE1 alpha , and CHOP (n = 9). Diets not sharing a common letter differ significantly from one another (P≤.05).

Morphine suppressed 6-OHDA-induced ER stress through activation of UPR. (A,B) Morphine induced UPR in SH-SY5Y cells. Protein levels of GRP78, p-IRE1 alpha , IRE1 alpha , p-PERK, PERK, ATF6, CHOP and Tubulin in SH-SY5Y cells were analyzed (A) and quantified (B) by western blot. ∗P < 0.05, ∗∗P < 0.01, ∗∗∗P < 0.001 vs. control.

Effect of cancer on ER stress markers.Bip1, IRE-1, ATF-6 p50 and CHOP expression in the liver of non—cachectic ApcMin/+ mice (N = 6 per group), compared to healthy C57BL/6 mice. Dotted line on the western blot indicates two different sections of the same gel. Values are expressed as Mean ± SE. * denotes significantly different from the healthy C57BL/6 mice as analyzed by a pre—planned t—test. p < 0.05.

Western Blot: IRE1 alpha [p Ser724] Antibody - BSA Free [NB100-2323] - ABT-263 induces ER stress & activation of the unfolded protein response.a Western blot of ER stress molecules in uveal melanoma cells treated with ABT-263 5 μM for 24 h & 48 h. HSP90 is used as a loading control. Representative western blots are shown. b XBP1 splicing in uveal melanoma cells exposed to ABT-263 5 μM for 15 h. *P-value < 0.05, **P-value < 0.01. c Kinetic analysis of ER stress proteins in Mel270 cells treated with ABT-263 5 μM in the absence or presence of qVD-OPh 20 μM. HSP90 is used as a loading control. Representative western blots are shown. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/32337074), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: IRE1 alpha [p Ser724] Antibody - BSA Free [NB100-2323] - Effect of cancer on ER stress markers.Bip1, IRE-1, ATF-6 p50 & CHOP expression in the liver of non—cachectic ApcMin/+ mice (N = 6 per group), compared to healthy C57BL/6 mice. Dotted line on the western blot indicates two different sections of the same gel. Values are expressed as Mean ± SE. * denotes significantly different from the healthy C57BL/6 mice as analyzed by a pre—planned t—test. p < 0.05. Image collected & cropped by CiteAb from the following publication (//dx.plos.org/10.1371/journal.pone.0119888), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: IRE1 alpha [p Ser724] Antibody - BSA Free [NB100-2323] - ER stress is induced by acidosis activated OGR1-mediated signalling. Caco-2 cells subjected to different pH medium, following 4–6 h incubation in pH 7.6 serum free medium.(B) After 24 h pH shift, total protein was isolated & WB was performed. The results representative of 3 independent experiments. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31996710), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: IRE1 alpha [p Ser724] Antibody - BSA Free [NB100-2323] - Expression of ER stress markers in mouse & human skeletal muscle(a) TA muscle lysates from high fat fed mice were used to determine the expression of ER stress markers by Western blot analysis (n=6). (b-g) Western blot analysis was done to measure proteins involved in ER stress in vastus lateralis muscle from lean, obese, or diabetic subjects (n=6-13). Data are the means ± S.E.M. * indicates p<0.05 & ** indicates p<0.01 vs. chow or lean controls, using Student’s t-test (a) & One way ANOVA. Image collected & cropped by CiteAb from the following publication (//www.nature.com/articles/ncomms2851), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: IRE1 alpha [p Ser724] Antibody - BSA Free [NB100-2323] - The inositol-requiring enzyme 1 alpha (IRE1 alpha )/ X-box-binding-protein 1 spliced isoform (XBP1s) arm of unfolded protein response (UPR) is induced by angiotensin II in VSMCs. (A–C) The rat aortic VSMCs infected with adenovirus encoding GRP78 or control GFP (100 moi) for 48 h were stimulated with 100 nM AngII (AII) for 1–6 h & immunoblotting was performed as indicated. (A) Representative blots from 4 independent experiments. (B) Signal intensity was used to calculate the expression ratio of XBP1s to GAPDH. (C) Signal intensity was used to calculate the IRE1 alpha Ser724 phosphorylation ratio to the total IRE1 alpha . The bars in the graphs show the mean ± SD from 4 independent experiments. * indicates p < 0.05. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/32679678), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: IRE1 alpha [p Ser724] Antibody - BSA Free [NB100-2323] - Morphine suppressed 6-OHDA-induced ER stress through activation of UPR. (A,B) Morphine induced UPR in SH-SY5Y cells. Protein levels of GRP78, p-IRE1 alpha , IRE1 alpha , p-PERK, PERK, ATF6, CHOP & Tubulin in SH-SY5Y cells were analyzed (A) & quantified (B) by western blot. ∗P < 0.05, ∗∗P < 0.01, ∗∗∗P < 0.001 vs. control. (C,D) Protein levels of GRP78, CHOP & Actin in SH-SY5Y cells were analyzed (C) & quantified (D) by western blot in the indicated groups. ∗P < 0.05, ∗∗P < 0.01 vs. control & #P < 0.05, ##P < 0.01 vs. 6-OHDA-treated group. All data are expressed as mean ± SEM. Image collected & cropped by CiteAb from the following publication (//journal.frontiersin.org/article/10.3389/fnmol.2018.00120/full), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: IRE1 alpha [p Ser724] Antibody - BSA Free [NB100-2323] - Hepatic ER Stress.Representative hepatic western blots of BiP, phosphorylated (Ser51), total EIF2 alpha & phosphorylated:total EIF2 alpha , phosphorylated (Ser724), total IRE1 alpha & phosphorylated:total IRE1 alpha , & CHOP (n = 9). Diets not sharing a common letter differ significantly from one another (P≤.05). Image collected & cropped by CiteAb from the following publication (//dx.plos.org/10.1371/journal.pone.0167979), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: IRE1 alpha [p Ser724] Antibody - BSA Free [NB100-2323] - Effect of Insig-1 overexpression on nSREBP-1c & proteins related to ER stress pathway in INS-1 cells. INS-1 & INS-1-Insig-1 cells were stimulated with 11.2 mM & 25.0 mM glucose for 0, 24 & 72 h. A) nSREBP-1c & p-IRE1 alpha pathway of ER stress related proteins were detected by Western blot. GAPDH was used as control for protein loading. Equal amount of proteins (50 μg) were loaded. B) Relative protein expression compared to GAPDH, data are the means ± SE of three independent experiments; *, P < 0.05, **, P < 0.01 VS INS-1 cells at the same time point. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/21843373), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: IRE1 alpha [p Ser724] Antibody - BSA Free [NB100-2323] - cCK-18 is formed following activation of the UPR. A. Immunoblots for phospho-IRE1 (p-IRE1), total IRE1 (IRE1), & cleaved cytokeratin 18 (cCK-18) showing time-dependent increase of cCK-18 in A549 cells exposed to 0.5 μM of thapsigargin (TG, +) for various lengths of time. Immunoblots showing an increase in total & phospho-IRE1 confirm thapsigargin activates the UPR in A549 cells compared to vehicle controls (−). B. Immunoblots for cCK-18 showing time-dependent appearance of cCK-18 in annexin V– or V+ A549 cells exposed to 0.5 μM of thapsigargin for various lengths of time. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/23167970), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: IRE1 alpha [p Ser724] Antibody - BSA Free [NB100-2323] - Protein expression of downstream markers of ER stress in islets from lean, obese & high-fat-diet-fed fZDF rats. Protein lysates from islets isolated from three age-matched fZDF rats (obese), HF-fZDF (HFD) rats & their heterozygous lean littermates (lean) were separated by SDS-PAGE & analysed by western blotting. As controls, lysates from the islets isolated from Wistar rats or MIN6 cells treated with 1 μM thapsigargin for 2 h or sorbitol for 1 h were run alongside. Proteins were detected using antisera against (a) Calreticulin, HYOU1, GRP78, p-IRE1 alpha , p-eIF2 alpha & CHOP & as protein loading control rpS6 & (b) p-JNK & total JNK1/2 as loading control. Western blots were quantified using Image-J software. Image collected & cropped by CiteAb from the following publication (//www.nature.com/articles/nutd201335), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: IRE1 alpha [p Ser724] Antibody - BSA Free [NB100-2323] - CETP inhibition reduces endoplasmic reticulum stress. HAECs transfected with CETP or control scrambled siRNA. (A) Western blot analysis of PERK (n = 3, * p < 0.01) & qPCR analysis of ATF6 mRNA. (B) Phosphorylated & total IRE (n = 3, ns). (C) Representative microscopic images of HAECs stained with GADD153, n = 5, & (D) Grp78/BIP, & DAPI. Scale bar, 10 μm. Mean ± SEM, n = 5, * p < 0.05. HAECs, human aortic endothelial cells. CETP, cholesteryl ester transfer protein. NS, non-silenced. siCETP, silenced CETP. PERK, protein kinase RNA-like ER kinase. ATF6, Activating transcription factor 6. IRE, inhibitor resistant esterase. BIP, binding immunoglobulin protein. GADD153, growth arrest- & DNA damage-inducible gene 153. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/33430172), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: IRE1 alpha [p Ser724] Antibody - BSA Free [NB100-2323] - Activation of UPR signaling pathways after UIRI. a & b The expression of p-PERK & t-PERK in kidneys of UIRI mice were evaluated with western blot analysis & quantified. c UIRI induces the activation of ATF6 as demonstrated by enhanced expression of cleaved ATF6 (cATF6). GAPDH was used as an internal control. d Fold-change expression of cATF6 in kidneys of UIRI mouse as compared with that of sham group mouse. e & f The expression of p-IRE1 & t-IRE1 in mice kidneys were evaluated with western blotting & quantified. Data are expressed as means ± SEM, n = 3 ~ 6 in each group. *P < 0.05, **P < 0.01, & ***P < 0.001, as compared with sham group Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/35765067), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: IRE1 alpha [p Ser724] Antibody - BSA Free [NB100-2323] - Apoptosis mediated by Arl6ip5 interference is regulated by Chop. (a) Immunoblotting was used to detect the protein level for p-IRE1 alpha , IRE1, Chop, Arl6ip5 & beta -actin in the UAMS-32 cell with NC-siRNA or Arl6ip5-siRNA treatment for 72 h. Representative results were shown from three independent experiments. (b–e) UAMS-32 cells first received NC-siRNA or Chop-siRNA for 24 h, then the medium was changed & further received NC-siRNA or Arl6ip5-siRNA for 72 h. Q-PCR was used to analyze the mRNA levels of Chop (b), GADD34 (c) & Trib3 (d). The apoptotic cells were stained with Annexin-V & the proportion were calculated (e). n=4. In all panels, error bars represent the mean±S.E.M. **P<0.01, *P<0.05 based on ANOVA Image collected & cropped by CiteAb from the following publication (//www.nature.com/articles/cddis2014427), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: IRE1 alpha [p Ser724] Antibody - BSA Free [NB100-2323] - Downregulation of gamma -taxilin & alpha NAC, & ER stress responses in mouse brain slice cultured under hypoxic conditions. (a) Immunohistochemistry shows downregulation of gamma -taxilin & alpha NAC expression in brain slices cultured for 48 h under hypoxic conditions. Scale bar, 20 μm. (b) Western blot shows downregulation of gamma -taxilin & alpha NAC, phosphorylation of PERK & IRE1 alpha & induction of CHOP in mouse brain slices cultured for 48 h under normoxic (−) or hypoxic conditions (+) Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/25880086), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: IRE1 alpha [p Ser724] Antibody - BSA Free [NB100-2323] - Differential ER stress response pathways initiated by gamma -taxilin or alpha NAC depletion. Proteins involved in UPR sensor (PERK, IRE1 alpha ), eIF2 alpha , JNK, Bcl-2, & Bcl-2-related protein (Puma, Bim, Bak, & Bax) signaling pathways were analyzed by Western blotting of HeLa S3 cells that were depleted of gamma -taxilin or alpha NAC by RNA intereference for 72 & 96 h. Upper panels, taxilin & NAC proteins; middle panels, UPR proteins; lower panels; apoptotic proteins; & bottom panel, beta -actin Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/25880086), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: IRE1 alpha [p Ser724] Antibody - BSA Free [NB100-2323] - The UPR is activated in type II AECs isolated from IPF lungs. Phosphorylated IRE-1 alpha (panel A) & spliced XBP-1 (panel B) were present in increased amounts in AECs from 3 different IPF lungs, but not in the 3 control subjects (* P < 0.05, **P = 0.0495 by Wilcoxon rank sum test). # indicates amplicon of unspliced XBP1 digested with Pst1. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/23167970), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: IRE1 alpha [p Ser724] Antibody - BSA Free [NB100-2323] - ER stress is induced by OGR1 via IRE1 alpha /JNK signalling. (A) Caco-2 cells were subjected to different pH medium, with or without an OGR1 inhibitor (10 µM), following 4–6 h in pH 7.6 serum free medium. After 24 h pH shift, total protein was isolated & Western blot performed. Results are representative of two independent experiments. (B) Caco-2 cells were subjected to different pH medium After 24 h pH shift, total protein was isolated & Western blot performed. Results are representative of two independent experiments. (C) Caco-2 cells were subjected to different pH medium with or without a JNK inhibitor (10 µM) following 4–6 h in pH 7.6 serum free medium. After 24 h pH shift, total protein was isolated & Western blot performed. Results are representative of two independent experiments. (D) Caco-2 cells were starved & subjected to an acidic pH with or without a JNK inhibitor as described in (C). After 24 h pH shift, total RNA was isolated & mRNA expression was investigated by qPCR. Statistical analysis was performed using one-way ANOVA followed by Tukey’s post-test. Data are presented as means ± SE of three independent experiments (***p < 0.001). (E) Caco-2 cells were starved & subjected to different pH medium following 4–6 h in pH 7.6 serum free medium. After 24 h pH shift, total protein was isolated & co-IP using IRE1 alpha antibody & JNK antibody was performed, followed by immunoblotting. Results are representative of two independent experiments. pH conditions: High pH 7.5–7.8; Normal pH 7.2–7.4; Low pH 6.6–6.8. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31996710), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

$Western Blot: IRE1 alpha [p Ser724] Antibody - BSA Free [NB100-2323] - Downregulation of gamma -taxilin & alpha NAC & ER stress responses in hypoxic cells. (a) Phase-contrast micrographs of SK-N-SH cells cultures in hypoxic conditions for 0–48 h. Floating cells were evident by 37 h after the beginning of hypoxic treatment. (b) FACS (fluorescence-activated cell sorting) analysis of apoptosis in hypoxic SK-N-SH cells. Bars in the FACS profiles (left panel) indicate the fraction locations of annexin-positive cells. Bar graph indicates the relative numbers of annexin-positive cells (right panel). Bar graph data are shown as means±S.D. (n=3). *Significantly different from controls (0 h) (P<0.001, Tukey–Kramer test). (c) DAPI (4',6-diamidino-2-phenylindole) staining shows fragmented nuclei of apoptotic SK-N-SH cells after hypoxic treatment. Scale bar, 10 μm. (d) Downregulation of gamma -taxilin & alpha NAC & induction of ER stress responses in hypoxic SK-N-SH cells. Western blot analysis was performed 0 to 48 h after hypoxic treatment of cells. Upper panels, taxilin & NAC proteins; middle panels, UPR proteins; lower panels, apoptotic proteins; & bottom panels, cleaved caspase-9 & beta -actin proteins. (e) MG-132 treatment restore the gamma -taxilin & alpha NAC protein level in hypoxic (16 h) HeLa S3 cells. MG-132 (−), DMSO; MG-132 (+), 20 μM. (f) Caspase inhibition does not affect the hypoxia-induced downregulation of gamma -taxilin & alpha NAC in HeLa S3 cells. (g) Colocalization of gamma -taxilin & alpha NAC in normoxic (0 h) & hypoxic (8 h) HeLa S3 cells. Note that the colocalization fraction increases with the appearance of apoptotic phenotypes. Scale bars, 10 μm Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/25880086), licensed under a CC-BY license. Not internally tested by Novus Biologicals.$

$Western Blot: IRE1 alpha [p Ser724] Antibody - BSA Free [NB100-2323] - gamma -Taxilin ablation causes ER stress responses & apoptosis in normoxic cells. (a) Knockdown of gamma -taxilin expression by small interfering RNA (siRNA) in HeLa S3 cells. Two different siRNA constructs are equally effective. HeLa S3 cells were treated with solvent alone (Mock), control siRNA (Co), or gamma -taxilin siRNA ( gamma -tax-1 or -2) for 96 h. (b) Induction of apoptosis by gamma -taxilin ablation in HeLa S3 cells. gamma -Taxilin ablation causes apoptosis in HeLa S3 cells, but Mock or Co treatment did not. Bar graph shows fractions of annexin-positive cells (means±S.D., n=3). *Significantly different from Mock- or Co treatment (P <0.001, Tukey–Kramer test). (c) Confocal microscopy demonstrates coincidence of gamma -taxilin depletion & apoptotic nuclei in HeLa S3 cells treated with gamma -taxilin siRNA. Scale bar, 10 μm. (d) gamma -Taxilin depletion triggers ER stress responses in HeLa S3 cells. Upper panels, taxilin & NAC proteins; middle panels, UPR proteins; & lower panel, beta -actin. (e) gamma -Taxilin ablation induces accumulation of ubiquitinated proteins in HeLa S3 cells. Cell lysates were analyzed on 7.5% SDS-PAGE, followed by immunoblotting with antibodies specific for anti-mono- & polyubiquitinated conjugates (upper panel) & beta -actin (lower panel) Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/25880086), licensed under a CC-BY license. Not internally tested by Novus Biologicals.$

$Western Blot: IRE1 alpha [p Ser724] Antibody - BSA Free [NB100-2323] - Localization of the WT & mutant Wrn proteins in different subcellular fractions.(A) Example of western blots showing the presence of the Wrn WT protein in the nuclear fraction & the presence of the Wrn delta hel mutant protein mainly in the cytosolic fraction. Fractionations were performed on WT, Wrn delta hel/ delta hel, & Wrn-/- MEFs. Topoisomerase I & beta -tubulin are nuclear & cytoplasmic markers, respectively. As expected the molecular weight of the Wrn delta hel mutant protein was lower than the Wrn WT protein. No band was detected in Wrn-/- MEFs fractions with the anti-Wrn polyclonal antibody. (B) Example of western blots showing only the presence of the Wrn delta hel mutant protein in total ER & the peroxisomal fractions. Fractionations were performed on WT, Wrn delta hel/ delta hel, & Wrn-/- liver tissues. Catalase & calreticulin are used as peroxisomal & ER specific markers. This experiment was repeated three times. (C) Protein levels of GRP78, phosphorylated IRE alpha , & beta -actin (top panels) & of total IRE alpha , & beta -actin (bottom panels) in the spleen of three animals of each genotype. (D) Ratio of GRP78 signal over beta -actin signal from western blots. (E) Ratio of IRE alpha over beta -actin signal from western blots. (F) Ratio of phosphorylated IRE alpha signal over beta -actin signal from western blots. Experiments were performed in triplicates. Bars in all histograms represent SEM. Tukey post ANOVA test P-values are shown (*P < 0.05 & **P < 0.01). Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/26447695), licensed under a CC-BY license. Not internally tested by Novus Biologicals.$

Western Blot: IRE1 alpha [p Ser724] Antibody - BSA Free [NB100-2323] - IER3IP1 suppression decreases the UPR activation(A) mRNA levels of IRE1 alpha , Perk & Atf6 in IER3IP1 KD cells. 4 days after infection with IER3IP1 shRNA lentivirus, mRNA levels of IRE1 alpha , Perk & Atf6 in IER3IP1 KD cells were determined by qRT-PCR. *P<0.05, **P<0.01 compared to control group. Values are mean ± SEM. (B) Effect of IER3IP1 suppression on the IRE1 alpha arm of the UPR. 4 days after IER3IP1 KD in MIN6 cells, phosphorylation of IRE1 alpha , Bip, sXBP-1 & uXBP-were determined by Western blot. The loaded proteins in the two “- or +” lines were the same but from the different plates. (C) mRNA levels of downstream targets of sXBP-1 in IER3IP1 KD cells. 4 days after IER3IP1 KD in MIN6 cells, mRNA levels of downstream targets of sXBP-1, Erdj4, p58IPK, EDEM & Sec61a, were determined by qRT-PCR. Values are mean ± SEM. (D) Effect of IER3IP1 suppression on the Perk arm of the UPR. 4 days after IER3IP1 KD in MIN6 cells, phosphorylation of Perk & eIF2a, & ATF4 were determined by Western blot. The loaded proteins in the two “- or +” lines were the same but from the different plates. (E) IER3IP1 KD decreases UPR activation induced by ER stress in MIN6. 4 days after IER3IP1 KD, MIN6 cells were treated with 10 μg/ml tunicamycin (TC) or 1 μM thapsigargin (TG) for 6 hours. Then the expression levels of Chop, sXBP-1, uXBP-1 & IER3IP1 were determined by Western blot. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/28915629), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: IRE1 alpha [p Ser724] Antibody - BSA Free [NB100-2323] - ATG5 & ATG7 influenced on autophagy, apoptosis & cell cycle through PERK/Nrf2 signaling. a The ER stress proteins were analysed by western blotting in Ad-GFP, Ad-ATG5 + Ad-ATG7,Ad-ATG5 + Ad-ATG7 + siPERK,Ad-ATG5 + Ad-ATG7 + siNrf2 & Ad-ATG5+ Ad-ATG7 + siPERK+siNrf2 induced chondrocytes. b The levels of ER stress proteins were normalized to beta -actin. c Determination of autophagy & apoptosis proteins expression by western blotting in Ad-GFP, Ad-ATG5 + Ad-ATG7, Ad-ATG5 + Ad-ATG7 + siPERK,Ad-ATG5 + Ad-ATG7 + siNrf2 & Ad-ATG5+ Ad-ATG7 + siPERK+ siNrf2 induced chondrocytes. dThe levels of related proteins were normalized to beta -actin. e FCM analysis was used to calculate the percentage of apoptotic cells at the time point of 24 h. The apoptosis rate were increased when combined treatment with silencing of PERK or Nrf2. Experiments were repeated 3 times, Representative images are shown. f Analysis of cell apoptosis. Data come from 3 independent experiments. g FCM analysis indicated that the S phase percentage were decreased compared to that of the control groups when combine infected with silencing of PERK or Nrf2 in C28I2 cells. Experiments were repeated 3 times, Representative images are shown. h Percentage of cells at each phase in different groups. *P < 0.05, **P < 0.01 compared with the controls. Values are means ± SD n = 3). (1:Ad-GFP, 2:Ad-ATG5 + Ad-ATG7, 3:Ad-ATG5 + Ad-ATG7 + siPERK, 4:Ad-ATG5 + Ad-ATG7 + siNrf2, 5:Ad-ATG5 + Ad-ATG7 + siPERK+ siNrf2) Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31060556), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: IRE1 alpha [p Ser724] Antibody - BSA Free [NB100-2323] - Thapsigargin treatment induces calpain activation & autophagy. (A) Control & shCAPNS1 cells were treated with 100 nM thapsigargin for 10, 20 & 30 min & the lysates subjected to western blot analysis to quantify the precursor & active form of CAPN1. The ratio between active CAPN1 & tubulin is reported below each lane. (B) Time course measurement of intracellular calcium concentration. The plot indicates the ratio of mean Indo Violet/Indo Blue emission values of each cell population at individual time points (minutes). The ratio corresponds to the relative calcium concentration of control & shCAPNS1 U2OS cells before & after addition of thapsigargin (100 nm final). Moving average was used as smoothing method. (C) shCAPNS1 cells were treated with 100 nM thapsigargin for 30, 60 & 120 min & the lysates subjected to western blot analysis to detect LC3, p62, pIRE, CAPNS1 & tubulin. (D) Levels of p62 & LC3 normalized to tubulin levels. Image collected & cropped by CiteAb from the following publication (//journals.biologists.com/bio/article/doi/10.1242/bio.022806/256614/Calpain-mobilizes-Atg9-Bif-1-vesicles-from-Golgi), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: IRE1 alpha [p Ser724] Antibody - BSA Free [NB100-2323] - Abnormal Paneth cells show ER stress.(A, B) Representative transmission electron microscopy images of Paneth cells at the base of ileal crypts in (A) ICR & (B) SAMP1/YitFc mice. Scale bars indicate 2 μm. (C, D) Quantitative analysis of (C) granule number & (D) ER lumen diameter in Paneth cells (n = 3/each week for SAMP1/YitFc mice). For the measurements, three Paneth cells were randomly selected from each mouse. (E) SDS–PAGE Western blot analysis of ER stress markers, pIRE1 alpha , ATF4, cleaved-ATF6, & GRP78 in ileal crypts (n = 4/each group). Total-IRE1 alpha & HPRT1 was used as loading control. (F) Relative expression level of ER stress markers calculated from the band intensity. Error bars represent mean ± SEM. (C, D, F) Statistical significance was evaluated by t test in (C, D), & one-way ANOVA followed by Tukey’s post hoc test in (F). P < 0.05 was considered statistically significant. *P < 0.05, †P < 0.01, §P < 0.001. E, ER; G, granules; N, nucleus; n.s., not significant. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/32345659), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: IRE1 alpha [p Ser724] Antibody - BSA Free [NB100-2323] - Hypoxia-induced downregulation of gamma -taxilin & alpha NAC & the subsequent ER responses are GSK-3 beta -dependent. (a) GSK-3 beta activation in hypoxia. Western blot analysis shows downregulation of phosphorylated (Ser 9) GSK-3 beta (phospho-GSK-3 beta ) in hypoxic (0–48 h) SK-N-SH & hypoxic (0–24 h) HeLa S3 cells. (b) Inhibition of GSK-3 beta activation by lithium chloride (LiCl, 100 mM) or CHIR-99021 (CHIR, 15 or 30 μM) maintained gamma -taxilin & alpha NAC protein levels in hypoxic SK-N-SH & HeLa S3 cells. (c) GSK-3 beta inhibition suppresses the expression of ER stress response proteins that are induced in hypoxic SK-N-SH cells. (d) GSK-3 beta RNA interference almost completely blocked the protein expression & restored the expression of gamma -taxilin & alpha NAC proteins in hypoxic HeLa S3 cells Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/25880086), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Reactivity:

Hu, Mu, Rt, Po, Dr, Gt, Ma, Pm, Pm, Rb, SyHa

Species Glossary

Reactivity: Hu, Mu, Rt, Po, Dr, Gt, Ma, Pm, Pm, Rb, SyHa

Applications:

, , , , , , , , ,

Applications: , , , , , , , , ,

Host:

Rabbit Polyclonal

Host: Rabbit Polyclonal

Sizes:

Sample Size Available

Sizes: Sample Size Available

Conjugate:

Unconjugated

Available Conjugates:

Validated by:

Validated by:

Conjugate	Catalog #	Availability	Size	Price
Alexa Fluor 350	NB100-2323AF350
Alexa Fluor 405	NB100-2323AF405
Alexa Fluor 488	NB100-2323AF488
Alexa Fluor 532	NB100-2323AF532
Alexa Fluor 594	NB100-2323AF594
Alexa Fluor 647	NB100-2323AF647
Alexa Fluor 700	NB100-2323AF700
Alexa Fluor 750	NB100-2323AF750
Allophycocyanin	NB100-2323APC
Biotin	NB100-2323B
CoraFluor 1	NB100-2323CL1
DyLight 350	NB100-2323UV
DyLight 405	NB100-2323V
DyLight 488	NB100-2323G
DyLight 550	NB100-2323R
DyLight 594	NB100-2323DL594
DyLight 650	NB100-2323C
DyLight 680	NB100-2323FR
DyLight 755	NB100-2323IR
FITC	NB100-2323F
HRP	NB100-2323H
Janelia Fluor 525	NB100-2323JF525
Janelia Fluor 549	NB100-2323JF549
Janelia Fluor 646	NB100-2323JF646
Janelia Fluor 669	NB100-2323JF669
PE	NB100-2323PE
PerCP	NB100-2323PCP
mFluor Violet 450 SE	NB100-2323MFV450
mFluor Violet 500 SE	NB100-2323MFV500
mFluor Violet 610 SE	NB100-2323MFV610

Available Formulations

Formulation	Catalog #	Availability	Price
BSA Free	NB100-2323SS

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BC100-494

PINK1 Antibody - BSA Free

(13 Reviews)

(300 Publications)

0.1 ml

BC100-494

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

Reactivity:

Hu, Mu, Rt, Rb

Species Glossary

Reactivity: Hu, Mu, Rt, Rb

Applications:

, , , , , , , , ,

Applications: , , , , , , , , ,

Host:

Rabbit Polyclonal

Host: Rabbit Polyclonal

Sizes:

Sample Size Available

Sizes: Sample Size Available

Conjugate:

Unconjugated

Available Conjugates:

Validated by:

Validated by:

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

Available Formulations

Formulation	Catalog #	Availability	Price
BSA Free	BC100-494SS

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NB300-109

Tyrosine Hydroxylase Antibody - Azide Free

(7 Reviews)

(252 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, Ch

Species Glossary

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

Applications:

, , , , , ,

Applications: , , , , , ,

Host:

Rabbit Polyclonal

Host: Rabbit Polyclonal

Sizes:

Sample Size Available

Sizes: Sample Size Available

Conjugate:

Unconjugated

Available Formulations

Formulation	Catalog #	Availability	Price
Azide Free	NB300-109-25ul

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H00023435-M01

TDP-43/TARDBP Antibody (2E2-D3) - Azide and BSA Free

(3 Reviews)

(212 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>Western Blot: 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

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NB300-605

iNOS Antibody - BSA Free

(3 Reviews)

(143 Publications)

200uL

NB300-605

Immunohistochemistry-Paraffin: iNOS Antibody [NB300-605] - Immunohistochemistry was performed on normal deparaffinized human Heart tissue.

Immunocytochemistry/Immunofluorescence: iNOS Antibody [NB300-605] - Analysis of iNOS in A549 Cells. Cells were grown on chamber slides and fixed with formaldehyde prior to staining. Cells were probed without (control) or with a iNOS polyclonal antibody at a dilution of 1:20 overnight at 4C, washed with PBS and incubated with a DyLight 488 conjugated secondary antibody. iNOS staining (green), F-Actin staining with Phalloidin (red) and nuclei with DAPI (blue) is shown.

<b>Biological Strategies Validation. </b>Western Blot: iNOS Antibody [NB300-605] - iNOS in stimulated astrocytes. Western blot image submitted by a verified customer review.

<b>Biological Strategies Validation. </b>Western Blot: iNOS Antibody [NB300-605] - LCA-induced oxidative stress in 4T1 breast cancer cells. The 4T1 cells were treated with LCA for 48 h, then the indicated measurements were performed. The level of iNOS protein was detected by western blotting (n = 3). Image collected and cropped by CiteAb from the following publication (//www.mdpi.com/2072-6694/11/9/1255), licensed under a CC-BY license.

Immunocytochemistry/Immunofluorescence: iNOS Antibody [NB300-605] - Analysis of iNOS in NIH-3T3 Cells. Cells were grown on chamber slides and fixed with formaldehyde prior to staining. Cells were probed without (control) or with a iNOS polyclonal antibody at a dilution of 1:20 overnight at 4C, washed with PBS and incubated with a DyLight 488 conjugated secondary antibody. iNOS staining (green), F-Actin staining with Phalloidin (red) and nuclei with DAPI (blue) is shown.

Western Blot: iNOS Antibody - BSA Free [NB300-605] - Stimulation of IMA 2.1 cells had no effect on relative survival after viral infection. IMA 2.1 cells were stimulated with LPS (10 µg/ml), IFN-gamma , (10 ng/ml) LPS + IFN-gamma , IL-4 (10 ng/ml), FGF (5 ng/ml) or FGF + LPS for 24 h in medium with 2% FBS. Polarization of cells was analyzed by Griess assay (a), Western blot (b) & FACS analysis by detection of MHCII+ cells (c). d MTT assay was performed to detect the relative percentage of VACV-mediated cell death in the presence of stimulating factors. e Viral replication was analyzed by standard plaque assay in the presence of stimulating factors. All experiments were performed in triplicate. Image collected & cropped by CiteAb from the following publication (//www.translational-medicine.com/content/13/1/216), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Immunocytochemistry/ Immunofluorescence: iNOS Antibody - BSA Free [NB300-605] - Nfix is mainly expressed by anti-inflammatory MPs. (a) Percentage of F4/80+ MPs positive for Nfix in Tibialis Anterior muscles (TA) of WT mice injected by CTX at D2, D4 & D7, post-injury. Immunostaining for F4/80 (green), Nfix (red) & DAPI (blue) at D4 & D7 after CTX injection; (b) Percentage of Ly6C+ & Ly6C- sorted MPs positive for Nfix in TA muscles of WT mice injected by CTX at D2, D4 & D7 post-injury; (c) Percentage of Nfix+ MPs after M1 & M2c polarization (with IFN gamma & IL10, respectively). * p < 0.05; *** p < 0.001; for (b) * p < 0.05 Ly6C+ vs. Ly6C+ at D4 & D7; # p < 0.05 Ly6C− D7 vs. D2. Results are means ± SEM of at least three independent experiments. Scale bar = 50 μm. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/32183151), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: iNOS Antibody - BSA Free [NB300-605] - Indolepropionic acid (IPA) induced oxidative stress, cellular energy stress, & decreased the proportions of cancer stem cells. 500,000 cells/well 4T1 cells were treated with IPA in the concentrations indicated for 24 h; then, (A) lipid peroxidation was measured by TBARS assay, & (B) 4HNE expression was assessed by Western blotting (representative figure, n = 3). In the same cells (C), the protein expression of NRF2 (at 68 kDa) & iNOS were determined by Western blotting (n = 3), while (D) the mRNA expression of catalase (cat) was determined by RT-qPCR (n = 3). (E) The expression of the indicated proteins (pACC, ACC, FOXO1, & PGC-1 beta ) were determined by Western blotting (n = 3, except for PGC-1 beta , where n = 2). (F) 100,000 cells/well 4T1 cells were treated with the indicated concentration of IPA for 24 h; then, the proportions of aldehyde dehydrogenase-positive cells were determined in Aldefluor assays using flow cytometry (n = 3). For Western blots, a typical experiment was displayed. Fold data were log2 transformed to achieve normal distribution. Statistical significance was determined using the ANOVA test followed by Dunnett’s post-hoc test, except for panel F, where Student’s t-test was used. * & *** indicate statistically significant difference between control & treated samples at p < 0.05 & p < 0.001, respectively. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/32854297), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: iNOS Antibody - BSA Free [NB300-605] - NRF2 activation modulated LCA-induced oxidative stress responses in 4T1 breast cancer cells. The 4T1 cells were treated with 0.3 μm LCA & the NRF2 activator RA839 or tBHQ in the concentrations indicated for 48 h. Lipid peroxidation was determined by measuring (A) TBARS (n = 4) & (B,C) 4-HNE levels using western blotting (n = 3). (D) The 4T1 cells were treated with LCA (0.3 μm) and/or GSH & NAC (both at 5 mm) antioxidants for 48 h, then total protein concentration was determined using the sulforhodamine B assay (n = 3). For statistical analysis ANOVA test was used followed by the Dunnett post-hoc test, where all groups were compared to the LCA-treated cohort. Data are plotted as mean ± SEM. ** p < 0.01, LCA vs. LCA/NRF2-activator-treated groups (GSH, reduced glutathione; LCA, lithocholic acid; NAC, N-acetylcysteine; TBARS, thiobarbituric acid reactive substances; 4HNE, 4-hydroxynonenal). Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31461945), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: iNOS Antibody - BSA Free [NB300-605] - Impaired amount of virus progeny after stimulation of BV-2 cells with IFN-gamma or IFN-gamma & LPS. BV-2 cells were stimulated with LPS (10 µg/ml), IFN-gamma , (10 ng/ml), LPS + IFN-gamma or IL-4 (10 ng/ml) for 24 h in medium with 2% FBS. Polarization of cells was analyzed by Griess assay (a), Western blot (b) & by detection of the percentage of MHCII+ cells by FACS analysis (c). The amount of virus progeny (pfu/ml) was analyzed by standard plaque assay in the presence of stimulating factors & in normal growth medium in cells & supernatants (d). Statistical analysis was performed related to infection medium. To analyze the recovery of viral replication, normal growth medium was applied after infection of pre-stimulated cells. Standard plaque assay was performed to determine viral progeny in cells & supernatant after 24, 48, 72 & 96 hpi (e). To analyze the relative survival of the cells in the presence of stimulating factors a MTT assay was performed (f). The cellular density of stimulated cells relative to unstimulated (w/o) cells was detected via optical density measurement after 24 & 48 h of cultivation (g). Two-sided t test with unequal variances was used for statistics *p < 0.05, **p < 0.01, ***p < 0.001. Active replication was defined as virus titer above the virus titer of the infection medium (red line). All experiments were performed in triplicate & repeated in an independent experiment. Image collected & cropped by CiteAb from the following publication (//www.translational-medicine.com/content/13/1/216), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: iNOS Antibody - BSA Free [NB300-605] - Inhibitory effect of MMPP on amyloidogenesis & STAT3 translocation in astrocytes & microglia cells. The expression of APP, BACE1 & C99 was detected by Western blotting using specific antibodies in astrocytes (a) & microglia cells (b). Each blot is representative of three experiments. The activity of beta -secretase was investigated using assay kit in astrocytes (c) & microglia cells (d). Values are presented as mean ± S.D. of the three independent experiments performed in triplicate. #p < 0.05 compared to control, *p < 0.05 compared to LPS. Iba-1, COX-2, & iNOS proteins were detected by Western blotting using specific antibodies in astrocytes (e) & microglia cells (f). NO level was measured in astrocytes (g) & microglia cells (h). Activation of STAT3 was investigated using EMSA in astrocytes (i) microglial cells (j) were determined & the expression of STAT3 & phopho-STAT3 was also detected by Western blotting using specific antibodies (k), (l). For the cropped images, samples were run in the same gels under same experimental conditions & processed in parallel. Each band is representative for three experiments Image collected & cropped by CiteAb from the following publication (//link.springer.com/10.1007/s12017-017-8469-3), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

TSA, PXD, or MGCD restore osteoimmune balance and reduce osteolytic activity. A Histological examination by H&E staining revealed differences in calvarial bone morphology between groups. Immunohistochemical staining demonstrated that treatment with TSA, PXD, or MGCD reduced osteoclast activity, as shown by decreased CTSK expression (B), suppressed M1 macrophage polarization indicated by reduced iNOS expression (D), enhanced M2 macrophage polarization indicated by increased ARG1 expression (F), and promoted osteogenesis as reflected by elevated RUNX2 expression (H). Quantification of CTSK- (C), iNOS- (E), ARG1- (G), and RUNX2- (I) positive cells. Data are presented as mean +/- SD (n = 6 per group). *P < 0.05, **P < 0.01, and ***P < 0.001. Scale bar = 100 μm Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/41174647), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Reactivity:

Hu, Mu, Rt, Po

Species Glossary

Reactivity: Hu, Mu, Rt, Po

Applications:

, , , , ,

Applications: , , , , ,

Host:

Rabbit Polyclonal

Host: Rabbit Polyclonal

Sizes:

Sample Size Available

Sizes: Sample Size Available

Conjugate:

Unconjugated

Available Conjugates:

Validated by:

Validated by:

Conjugate	Catalog #	Availability	Size	Price
Alexa Fluor 405	NB300-605AF405
Alexa Fluor 488	NB300-605AF488
Alexa Fluor 647	NB300-605AF647
Alexa Fluor 700	NB300-605AF700
Biotin	NB300-605B
DyLight 350	NB300-605UV
DyLight 405	NB300-605V
DyLight 488	NB300-605G
DyLight 550	NB300-605R
DyLight 594	NB300-605DL594
DyLight 650	NB300-605C
DyLight 680	NB300-605FR
DyLight 755	NB300-605IR
FITC	NB300-605F
HRP	NB300-605H
Janelia Fluor 549	NB300-605JF549
Janelia Fluor 646	NB300-605JF646

Available Formulations

Formulation	Catalog #	Availability	Price
BSA Free	NB300-605SS

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NB300-144

Laminin Antibody - BSA Free

(8 Reviews)

(140 Publications)

0.1 ml

NB300-144

MxIF analysis of mouse submandibular salivary gland morphogenesis. MxIF of a developmental TMA including embryonic stages (E14, E16, E18) and postnatal stages (P5 and P20) was performed using sequential application of directly conjugated antibodies to detect multiple markers of tissue structures and cell types on the same tissue sections. Tissue compartments. The epithelium, mesenchyme, neurons, and basement membranes was detected using antibodies directed towards E-cadherin (ECAD, red), platelet-derived growth factor (PDGFR, green), beta III tubulin (bIII, magenta), and Laminin Antibody [NB300-144] (LMN, cyan), respectively. Image collected and cropped by CiteAb from the following publication (//bio.biologists.org/cgi/doi/10.1242/bio.20134309), licensed under a CC-BY license.

Staining of mouse section of cortex stained with Laminin Antibody [NB300-144] (red). Blue is DAPI staining of DNA. This antibody reveals strong staining in the basement membranes of blood vessels.

Staining of rat spinal cord and dorsal root paraformaldehyde/paraffin-embedded tissue using Laminin Antibody [NB300-144]. Pepsin antigen retrieval was performed on this tissue sample.

Analysis of rat heart cells lysates (lane 1) and 0.2 ug of purified laminin protein from mouse EHS sarcoma (lane 2) Laminin Antibody [NB300-144] recognizes 3 laminin isotypes: alpha 1 (440 kDa), beta 1 (220 kDa) and gamma 1 (220 kDa). Also recognized is a laminin binding protein at 120 kDa in both rat heart lysates and purified laminin protein. Since this protein always coexpresses with laminin this crossreactivity is irrelevant. Theoretical molecular weight of LAMA1 is 337 kDa.

IF Confocal analysis of HeLa cells using Laminin Antibody [NB300-144] (1:5). An Alexa Fluor 488-conjugated Goat to rabbit IgG was used as secondary antibody (green, A). Actin filaments were labeled with Alexa Fluor 568 phalloidin (red, B). DAPI was used to stain the cell nuclei (blue, C).

Western blot analysis of the effects of IP6, Ins, IP6 + Ins and normal saline on the levels of collagen IV, Laminin and Fibronectin, with Laminin Antibody [NB300-144]. IP6 or Ins treatment decreased the protein expression of LN and FN, and the combined IP6 + Ins treatment resulted in significantly greater effects compared with treatment with either compound alone. The Western blot membranes were stripped and reprobed for beta-actin as an internal control to confirm equal loading. (A) representative blots from one of three separate experiments; (B) relative band intensities based on densitometry. The results are expressed as the mean +/- standard deviation from three independent experiments. * p < 0.05 compared to the IP6 + Ins group; #p < 0.05 compared to the normal saline group. Image collected and cropped by CiteAb from the following publication (//www.mdpi.com/2072-6643/8/5/286), licensed under a CC-BY license.

Immunofluorescence staining for extracellular matrix proteins in day 1 and day 7 HWJSC spheroids. HWJSC spheroids were cultured for either 1 day or 7 days (with 6 days of osteogenic differentiation), fixed, and stained for extracellular matrix protein: laminin (C) and counter-staining with Hoechst. Scale bars represent 100 um. Image collected and cropped by CiteAb from the following publication (journals.plos.org/plosone/article?id=10.1371/journal.pone.0184155), licensed under a CC-BY license. Using the Alexa Fluor 488 format of this antibody.

Laminin staining on an E12.5 mouse Right Ventricle. IHC-Fr image submitted by a verified customer review.

A surface stain was performed on HeLa cells with the Alexa Fluor 647 conjugate of Laminin Antibody [NB300-144AF647] (blue) and a matched isotype control (orange). Cells were incubated in an antibody dilution of 2.5 ug/mL for 20 minutes at room temperature. Both antibodies were conjugated to Alexa Fluor 647.

Analysis of Laminin-1 expression in mouse EHS tumor crude extracts (left) and Laminin-2 expression in rat heart crude extracts (right), using Laminin Antibody [NB300-144]. The Laminin polyclonal antibody was used at 1 ug/mL. Theoretical Molecular Weight of NB300-144 is 337 kDa.

VSOP observed in perivascular-restricted spinal cord lesions with intact BBB. Immunostaining for laminin (brown) using Laminin Antibody [NB300-144] shows vascular endothelium and glia limitans of a perivascular lesion, along with infiltrating cells and VSOP (blue). Image collected and cropped by CiteAb from the following publication (//asn.sagepub.com/lookup/doi/10.1042/AN20120081), licensed under a CC-BY license.

SOX17 regulates adult muscle regeneration after injury in Pax7CreERT2/+;Sox17fl/fl mutant mice. Representative images of cryosections from regenerating adult TA muscles d28 after injury, showing immunofluorescence for PAX7+ (quiescent, arrows) cells. Scale bar, 25 Aum. Image collected and cropped by Citeab from the following publication (SOXF factors regulate murine satellite cell self-renewal and function through inhibition ofI2-catenin activity. Elife (2018)) licensed under a CC-BY license.

WNT11 regulates MMPs activities.(A–C) (Top panels): Serum-free medium was conditioned for 24 hrs by the indicated cells, concentrated 20-fold & assayed by gelatin zymography. Gelatinolytic activity is indicated by clear zones against a dark background of stained substrate. (Bottom): Whole cell extracts were immunoblotted with indicated antibodies. (A) Overexpression of Wnt11 in EMSC or BT473 cells enhances activity of MMP-9 & MMP-2. (B) Impaired activity of MMP-9 & MMP-2 in MDA-MB-231 cells (left) or EMSCs (right) stably expressing Wnt11 shRNAs & treated with DMOG. (C) WNT11 is required for MMP-9 & MMP-2 activity in MDA-MB-231 cells (left) or EMSCs (right) under normoxic & hypoxic culture conditions. (D) WNT11 regulates MMP2 protein in media. (Top): conditioned media from indicated cells & treatments. (Bottom): whole cell lysates were immunoblotted with indicated antibodies. (E) Recombinant WNT11 induces both MMP-2 protein & MMP-2 activity in media. (Top panels): Gelatin zymography & immunoblot of serum-free medium conditioned for the indicated times after recombinant WNT11 (r-WNT11) treatment. (Bottom): Whole cell lysates were immunoblotted with indicated antibodies. (F) MMP-2 inhibitor attenuated induced migration by WNT11. MDA-MB-231 cells infected with lentiviruses for stable expression of Wnt11 or GFP (n = 4) were incubated with either vehicle or 1 μM of ARP100. Media in the lower compartment had same concentration of DMSO or inhibitor. Values are mean ± s.e.m. *p < 0.05, **p < 0.01. For panels (A–D), HIF-1 alpha & HIF-2 alpha were shown as a marker of hypoxia, WNT11 normalized to alpha -Tubulin was shown. Image collected & cropped by CiteAb from the following publication (//www.nature.com/articles/srep21520), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Hypoxia induces expression of WNT11 through VHL.(A,B) Higher basal levels of WNT11 protein in Vhl-deleted cells (lenti-Cre infected Vhlf/f). EMSCs isolated from Vhlf/f mouse were infected with lentivirus carrying either GFP gene (for control) or Cre recombinase (for knockout). Non-infected cells were also used as a control. Immunoblot analysis of control or Vhl KO EMSCs treated with 0.1 mM DMOG (A), & EMSCs exposed to air (21% O2) or hypoxia (1% O2) for 24 hrs (B). Laminin, alpha -tubulin, & lamin A/C were used as loading controls, WNT11 normalized to alpha -Tubulin was shown. (C,D) Inactivation of the Vhl gene results in increased Wnt11 mRNA. Wnt11 & Vegf mRNA levels in liver (C) or duodenum (D) were measured by qPCR in Liver-VhlcKO or duodenum-VhlcKO & control mice (n = 5 per group). Values normalized to Tbp mRNA are expressed relative to tissues from control mice. For panels (C,D), values are mean ± s.e.m. *p < 0.05, **p < 0.01. Image collected & cropped by CiteAb from the following publication (//www.nature.com/articles/srep21520), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

WNT11 is induced by hypoxia or hypoxic mimetics in different cell types.(A) Increased Wnt11 mRNA in EMSC adipocytes (Day 12) after hypoxia-mimetic treatments. EMSC adipocytes were treated with CoCl2 (0.1 mM), DFO (0.1 mM) or DMOG (0.1 mM) for 24 hrs. Values were normalized to Tbp mRNA & are expressed relative to control (n = 3). (B,C) Increased Wnt11 mRNA by hypoxia in EMSC preadipocytes & adipocytes (Day 0–12 after differentiation) (B), & C2C12 myoblast & myocyte (Day 0 & 8 after differentiation) (C). Wnt11 mRNA was assessed by quantitative PCR in cells exposed to air (21% O2) or hypoxia (1% O2) for 24 hrs. (n = 4). Values were normalized to Tbp mRNA & are expressed relative to 21% O2 samples (left panel). (D) Immunoblot analyses of HeLa cells under normal air or hypoxia for 24 hrs. (E,F) Induction of Wnt11 by increasing concentrations of DMOG in MDA-MB-231 cells (E) & 4T1 cells (F). (G) EMSCs treated with 0.1 mM DMOG for the indicated times. Wnt11 & Vegf mRNA expression was measured by qPCR & normalized to Tbp mRNA (n = 4). (H) WNT11 protein levels after DMOG treatment normalized to alpha -Tubulin (upper panel; n = 4). Representative immunoblots of EMSCs treated with 0.1 mM DMOG for the indicated times (Lower panel). (I) Protein expression in MDA-MB-231 cells treated with 0.1 mM DMOG. (J) Induction of Wnt11 promoter activity by hypoxia or hypoxia mimetics. pGL3-Wnt11 promoter plasmid was transfected into C2C12 cells. Cells were incubated with DMOG (left panel, n = 4) or under 21% O2 or 1% O2 (right panel, n = 8) for 24 hrs. For panels (A–C,G,H,J), values are mean ± s.e.m. *p < 0.05, **p < 0.01. For panels of immunoblotting, laminin, alpha -tubulin, & ERK were used as loading controls, WNT11 normalized to alpha -Tubulin was shown. Image collected & cropped by CiteAb from the following publication (//www.nature.com/articles/srep21520), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Immunocytochemistry/ Immunofluorescence: Laminin Antibody [NB300-144] - hS/PCs sequentially secrete basement membrane proteins during microstructure reorganization & function. Encapsulated hS/PCs in HA-PEGDA hydrogels initially produce laminin (red) (A–C) & collagen IV (green) (D–F) even at the single-cell state (A,D). Perlecan (green) (G–I) secretion follows to stabilize the laminin & collagen IV networks. Scalebar = 20 μm in all confocal micrographs. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31750298), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: Laminin Antibody [NB300-144] - Western blot analysis of the effects of IP6, Ins, IP6 + Ins & normal saline on the levels of collagen IV, Lamininand Fibronectin. IP6 or Ins treatment decreased the protein expression of collagen IV, LN & FN, & the combined IP6 + Ins treatment resulted in significantly greater effects compared with treatment with either compound alone. The samples were probed with antibodies against p-collagen IV, p-LN, & p-FN. The Western blot membranes were stripped & reprobed for beta -actin as an internal control to confirm equal loading. (A) representative blots from one of three separate experiments; (B) relative band intensities based on densitometry. The results are expressed as the mean ± standard deviation from three independent experiments. * p < 0.05 compared to the IP6 + Ins group; #p < 0.05 compared to the normal saline group. Image collected & cropped by CiteAb from the following publication (//www.mdpi.com/2072-6643/8/5/286), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Reactivity:

Hu, Mu, Rt, ChHa, In, Ma, Rb, Sh

Species Glossary

Reactivity: Hu, Mu, Rt, ChHa, In, Ma, Rb, Sh

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	NB300-144AF350
Alexa Fluor 405	NB300-144AF405
Alexa Fluor 488	NB300-144AF488
Alexa Fluor 532	NB300-144AF532
Alexa Fluor 594	NB300-144AF594
Alexa Fluor 647	NB300-144AF647
Alexa Fluor 700	NB300-144AF700
Alexa Fluor 750	NB300-144AF750
Allophycocyanin	NB300-144APC
Allophycocyanin/Cy7	NB300-144APCCY7
Biotin	NB300-144B
CoraFluor 1	NB300-144CL1
DyLight 350	NB300-144UV
DyLight 405	NB300-144V
DyLight 488	NB300-144G
DyLight 550	NB300-144R
DyLight 594	NB300-144DL594
DyLight 650	NB300-144C
DyLight 680	NB300-144FR
DyLight 755	NB300-144IR
FITC	NB300-144F
HRP	NB300-144H
Janelia Fluor 525	NB300-144JF525
Janelia Fluor 549	NB300-144JF549
Janelia Fluor 646	NB300-144JF646
Janelia Fluor 669	NB300-144JF669
PE	NB300-144PE
PE/Atto594	NB300-144PEATT594
PE/Cy5.5	NB300-144PECY55
PE/Cy7	NB300-144PECY7
PerCP	NB300-144PCP
mFluor Violet 450 SE	NB300-144MFV450
mFluor Violet 500 SE	NB300-144MFV500
mFluor Violet 610 SE	NB300-144MFV610

Available Formulations

Formulation	Catalog #	Availability	Price
BSA Free	NB300-144SS

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NB100-56875

GAPDH Antibody - BSA Free

(5 Reviews)

(131 Publications)

0.1 mg

NB100-56875

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

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

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

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

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

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

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

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

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

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

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

Reactivity:

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

Species Glossary

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

Applications:

, , , ,

Applications: , , , ,

Host:

Rabbit Polyclonal

Host: Rabbit Polyclonal

Alt Catalog#

IMG-5143A

Alt Catalog# IMG-5143A

Sizes:

Sample Size Available

Sizes: Sample Size Available

Conjugate:

Unconjugated

Available Formulations

Formulation	Catalog #	Availability	Price
BSA Free	NB100-56875SS

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NB300-213

MAP2 Antibody - BSA Free

(5 Reviews)

(132 Publications)

0.05 ml

NB300-213

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

Reactivity:

Hu, Mu, Rt, Fe

Species Glossary

Reactivity: Hu, Mu, Rt, Fe

Applications:

, , ,

Applications: , , ,

Host:

Chicken Polyclonal

Host: Chicken Polyclonal

Conjugate:

Unconjugated

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NB100-355

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

(7 Reviews)

(105 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>Western Blot: 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.

Altered RPE structure and cell morphology in JR5558 mice. Immunofluorescence imaging of JR5558 retinal sections with antibodies against GFAP (green) and RPE65 (red) revealed subretinal Müller cell gliosis and altered RPE structure around the lesion area (A), corresponding to the altered outer retina and RPE structure noted in OCT image (B). Arrow and arrowhead highlighting subretinal gliosis and altered RPE, respectively. Phalloidin staining of JR5558 retinal flatmounts revealed the normal morphology of RPE cells at 4 (C) and 8 weeks (D) is changed from 12 weeks onwards (E–F). Dashed box represents area imaged in panel A. Scale bars: 50 μm. Image collected and cropped by CiteAb from the following open publication (//www.nature.com/articles/s41598-024-66068-z), 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
CoraFluor 1	NB100-355CL1
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 646	NB100-355JF646
Janelia Fluor 669	NB100-355JF669
PE	NB100-355PE
PerCP	NB100-355PCP
mFluor Violet 450 SE	NB100-355MFV450
mFluor Violet 500 SE	NB100-355MFV500
mFluor Violet 610 SE	NB100-355MFV610

Available Formulations

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

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NB100-664

VEGF Antibody (VG1) - BSA Free

(1 Review)

(100 Publications)

0.1 mg

NB100-664

U87 cells were fixed in 4% paraformaldehyde for 10 minutes and permeabilized in 0.05% Triton X-100 in PBS for 5 minutes. The cells were incubated with anti- NB100-664 at 1 ug/ml overnight at 4C and detected with an anti-mouse Dylight 488 (Green) at a 1:1000 dilution for 60 minutes. Nuclei were counterstained with DAPI (Blue). Cells were imaged using a 40X objective.

VEGF-Antibody-VG1-BSA-Free-Immunohistochemistry-NB100-664-img0015.jpg

An intracellular stain was performed on U-937 cells with NB100-664 (blue) and a matched isotype control (orange). Cells were fixed with 4% PFA and then permeabilized with 0.1% saponin. Cells were incubated in an antibody dilution of 1.0 ug/mL for 30 minutes at room temperature, followed by Mouse IgG (H+L) Cross-Adsorbed Secondary Antibody, Dylight 550 (35503, Thermo Fisher).

VEGF-Antibody-VG1-BSA-Free-Western-Blot-NB100-664-img0019.jpg

HUVEC and 293T cells transfected with a plasmid expressing human VEGF165 at 1:1000. Image provided by verified customer review.

FFPE human angiosarcoma tissue section using VEGF antibody (clone VG1). The endothelial cells of the blood vessels and most of the cancer cells showed strong positivity for VEGF protein.

Analysis of PerCP conjugate of NB100-664. An intracellular stain was performed on HUVEC cells with VEGF (VG1) antibody NB100-664PCP (blue) and a matched isotype control NBP2-27287PCP (orange). Cells were fixed with 4% PFA and then permeablized with 0.1% saponin. Cells were incubated in an antibody dilution of 10 ug/mL for 30 minutes at room temperature. Both antibodies were conjugated to PerCP.

An intracellular stain was performed on U-937 cells with NB100-664F (blue) and a matched isotype control (orange). Cells were fixed with 4% PFA and then permeablized with 0.1% saponin. Cells were incubated in an antibody dilution of 10 ug/mL for 30 minutes at room temperature. Both antibodies were conjugated to FITC.

Western Blot: VEGF Antibody (VG1) - BSA Free [NB100-664] - Regorafenib reduced TNBC cell migration & targeted p-STAT3/VEGF-A signaling.(A) Chemical structure of regorafenib. (B,C), Transwell assay (B) & wound-healing assay (C) were performed in TNBC cell lines after regorafenib treatment for 24 h. *p 160) or low VEGF-A (H score < = 160) levels for the indicated time of follow up. Chi-square test indicated a significant difference between VEGF-A high (N = 21) & low (N = 76) patients. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/27364975), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: VEGF Antibody (VG1) - BSA Free [NB100-664] - Regorafenib transcriptionally inhibited VEGF-A expression through decreasing binding of STAT3 on promoter of VEGF-A.(A) Top, MDA-MB-231 cells co-transfected w/ a Renilla control vector & plasmids containing firefly luciferase gene driven by wild-type or STAT3 binding site-mutated VEGF-A promoter. After transfection for 48 h, cells treated w/ regorafenib for 24 h. Promoter activity analyzed by luciferase assay after regorafenib treatment. Bottom, MDA-MB-231 cells transfected w/ vector-control or STAT3-overexpression plasmid for 48 h. After , cells further co-transfected w/ Renilla & wild-type VEGF-A promoter & detect promoter activity as mentioned above. *p < 0.05, **p < 0.01. (B) After regorafenib treatment for 24 h, STAT3 binding site fragment detected by PCR in ChIP samples precipitated w/ STAT3 & rabbit IgG control antibodies in MDA-MB-231 cells. (C,D), MDA-MB-231 cells transfected, respectively, w/ control vector or VEGF-A overexpression plasmid (C) or STAT3 overexpression plasmid (D) for 48 h. After transfection, cells treated w/wo regorafenib for 24 h & subjected to WB assay or seeded to Transwell to analyze migration ability. *p < 0.05, **p < 0.01. (E) Cells treated w/ regorafenib at indicated dosages for 24 h & cell lysates analyzed by SHP-1 phosphatase activity assay. *p < 0.05, **p < 0.01. (F) MDA-MB-231 cells pretreated w/ pan-phosphatase inhibitor (left), or specific SHP-1 inhibitor (Middle) for 1 h before regorafenib treatment. Right, MDA-MB-231 cells transfected, respectively, w/ control siRNA or SHP-1 siRNA for 48 h. After transfection, cells treated w/wo regorafenib (10 μM) for 24 h. The protein levels analyzed by WB assay or cells seeded to Transwell to analyze migration ability. *p < 0.05, **p < 0.01. Image collected & cropped by CiteAb from following publication (//pubmed.ncbi.nlm.nih.gov/27364975), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

VEGF expression in mouse liver tissues. Dilution: 2 ug/ml in 1X TBST. Image from a verified customer review.

Analysis of a FFPE tissue section of human liver using 1:200 dilution of VEGF antibody [VG1]. The staining was developed using HRP labeled anti-rabbit secondary antibody and DAB reagent, and nuclei of cells were counter-stained with hematoxylin.

Analysis of a FFPE tissue section of mouse liver using 1:200 dilution of VEGF antibody [VG1]. The staining was developed using HRP labeled anti-rabbit secondary antibody and DAB reagent, and nuclei of cells were counter-stained with hematoxylin.

HPG induces less VEGF production, less myofibroblast differentiation and lower macrophage activation. The expression of VEGF, alpha -SMA and MAC387 in the peritoneal tissue sections was examined using a routine immunohistochemical method. Data were a typical microscopic view of the peritoneal tissue sections in each group. a VEGF was detected using mouse monoclonal anti-VEGF antibody from Novus. Left graph a typical microscopic view, Dark brown stain VEGF-expressing cells (pointed by red arrows), Bv blood vessels, M muscle, black small bar 10 um. Right graph VEGF-expressing cells per 200 μm PM length in cross sections. Data were presented as mean +/- SD (n = 6) and were analyzed using t test. b alpha -SMA (a myofibroblast marker) was detected using mouse monoclonal anti-alpha -SMA antibody from Sigma-Aldrich. Left graph a typical microscopic view, Dark brown stain alpha -SMA-expressing cells or myofibroblasts (pointed by red arrows), Bv blood vessels, M muscle, black small bar 10 um. Right graph alpha -SMA-expressing cells per 200 μm PM length in cross sections. Data were presented as mean +/- SD (n = 6) and were analyzed using t test. c Macrophages were detected using mouse monoclonal anti-MAC387 antibody from Santa Cruz Biotech. Left graph a typical microscopic view, Dark brown stain MAC387-expressing cells or macrophages (pointed by red arrows), M muscle, black small bar 10 um. Right graph MAC387-expressing cells per 200 μm PM length in cross sections. Data were presented as mean +/- SD (n = 6) and were analyzed using t test Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/27964722), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Comparison of Col I and VEGF expression. (A) Representative images of Col I and VEGF immunohistochemical staining (30× magnification). Col I was stained with a reddish color. The black arrows indicate the location of VEGF staining. (B) Quantification of Col I and VEGF expression by immunohistochemical staining (mean +/- SD). Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/37151660), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Reactivity:

Hu, Mu, Rt, Po, Ca

Species Glossary

Reactivity: Hu, Mu, Rt, Po, Ca

Applications:

, , , , , ,

Applications: , , , , , ,

Host:

Mouse Monoclonal

Host: Mouse Monoclonal

Sizes:

Sample Size Available

Sizes: Sample Size Available

Conjugate:

Unconjugated

Available Conjugates:

Conjugate	Catalog #	Availability	Size	Price
Alexa Fluor 350	NB100-664AF350
Alexa Fluor 405	NB100-664AF405
Alexa Fluor 488	NB100-664AF488
Alexa Fluor 532	NB100-664AF532
Alexa Fluor 594	NB100-664AF594
Alexa Fluor 647	NB100-664AF647
Alexa Fluor 700	NB100-664AF700
Alexa Fluor 750	NB100-664AF750
Allophycocyanin	NB100-664APC
Biotin	NB100-664B
CoraFluor 1	NB100-664CL1
DyLight 350	NB100-664UV
DyLight 405	NB100-664V
DyLight 488	NB100-664G
DyLight 550	NB100-664R
DyLight 594	NB100-664DL594
DyLight 650	NB100-664C
DyLight 680	NB100-664FR
DyLight 755	NB100-664IR
FITC	NB100-664F
HRP	NB100-664H
Janelia Fluor 525	NB100-664JF525
Janelia Fluor 549	NB100-664JF549
Janelia Fluor 646	NB100-664JF646
Janelia Fluor 669	NB100-664JF669
PE	NB100-664PE
PerCP	NB100-664PCP
mFluor Violet 450 SE	NB100-664MFV450
mFluor Violet 500 SE	NB100-664MFV500
mFluor Violet 610 SE	NB100-664MFV610

Available Formulations

Formulation	Catalog #	Availability	Price
BSA Free	NB100-664SS
Azide and BSA Free	NBP2-81007

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NB300-110

Tyrosine Hydroxylase Antibody - Azide Free

(5 Reviews)

(104 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

Available Formulations

Formulation	Catalog #	Availability	Price
Azide Free	NB300-110SS

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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

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Applications

Reactivity

Citation

Antibody Validation

Reviews

Host

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Clone

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Species Glossary

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