| Formulation | Catalog # | Availability | Price | |
|---|---|---|---|---|
| BSA Free | NB100-2323SS | |||
| Formulation | Catalog # | Availability | Price | |
|---|---|---|---|---|
| BSA Free | NB300-144SS | |||
| Formulation | Catalog # | Availability | Price | |
|---|---|---|---|---|
| BSA Free | NB100-2324SS | |||
| Formulation | Catalog # | Availability | Price | |
|---|---|---|---|---|
| BSA Free | NB300-164SS | |||
| Azide and BSA Free | NBP2-80593 | |||
| Formulation | Catalog # | Availability | Price | |
|---|---|---|---|---|
| BSA Free | NB100-1936SS | |||
| Azide and BSA Free | NBP2-80955 | |||
| Formulation | Catalog # | Availability | Price | |
|---|---|---|---|---|
| BSA Free | NB110-55376SS | |||
| Formulation | Catalog # | Availability | Price | |
|---|---|---|---|---|
| BSA Free | NB100-2216SS | |||
| Formulation | Catalog # | Availability | Price | |
|---|---|---|---|---|
| BSA Free | NBP1-92695SS | |||
| Formulation | Catalog # | Availability | Price | |
|---|---|---|---|---|
| BSA Free | NB300-167SS | |||
![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.](http://images.novusbio.com/fullsize/nb100-2323_rabbit-polyclonal-ire1-alpha-p-ser724-antibody-310202415175222.jpg)
![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.](http://images.novusbio.com/fullsize/nb100-2323_rabbit-polyclonal-ire1-alpha-p-ser724-antibody-310202415384120.jpg)
![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.](http://images.novusbio.com/fullsize/nb100-2323_rabbit-polyclonal-ire1-alpha-p-ser724-antibody-31020241536371.jpg)
![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.](http://images.novusbio.com/fullsize/nb100-2323_rabbit-polyclonal-ire1-alpha-p-ser724-antibody-310202415175214.jpg)
![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.](http://images.novusbio.com/fullsize/nb100-2323_rabbit-polyclonal-ire1-alpha-p-ser724-antibody-310202415291930.jpg)
![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.](http://images.novusbio.com/fullsize/nb100-2323_rabbit-polyclonal-ire1-alpha-p-ser724-antibody-310202415171313.jpg)
![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.](http://images.novusbio.com/fullsize/nb100-2323_rabbit-polyclonal-ire1-alpha-p-ser724-antibody-310202415284519.jpg)
![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.](http://images.novusbio.com/fullsize/nb100-2323_rabbit-polyclonal-ire1-alpha-p-ser724-antibody-31020241535662.jpg)
![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.](http://images.novusbio.com/fullsize/nb100-2323_rabbit-polyclonal-ire1-alpha-p-ser724-antibody-310202415175288.jpg)
![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.](http://images.novusbio.com/fullsize/nb100-2323_rabbit-polyclonal-ire1-alpha-p-ser724-antibody-310202415175287.jpg)
![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.](http://images.novusbio.com/fullsize/nb100-2323_rabbit-polyclonal-ire1-alpha-p-ser724-antibody-31020241529334.jpg)
![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.](http://images.novusbio.com/fullsize/nb100-2323_rabbit-polyclonal-ire1-alpha-p-ser724-antibody-310202415371925.jpg)
![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.](http://images.novusbio.com/fullsize/nb100-2323_rabbit-polyclonal-ire1-alpha-p-ser724-antibody-310202415392557.jpg)
![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.](http://images.novusbio.com/fullsize/nb100-2323_rabbit-polyclonal-ire1-alpha-p-ser724-antibody-310202415304295.jpg)
![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.](http://images.novusbio.com/fullsize/nb100-2323_rabbit-polyclonal-ire1-alpha-p-ser724-antibody-310202415334944.jpg)
![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.](http://images.novusbio.com/fullsize/nb100-2323_rabbit-polyclonal-ire1-alpha-p-ser724-antibody-310202415384182.jpg)
![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. (F) A specific small molecule OGR1 inhibitor (10 µM) was tested & the cells subjected to low pH for 24 h, following 4–6 h incubation in pH 7.6 serum free medium. After 24 h pH shift, total protein was isolated & WB performed. Results representative of two 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.](http://images.novusbio.com/fullsize/nb100-2323_rabbit-polyclonal-ire1-alpha-p-ser724-antibody-31020241529194.jpg)
![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.](http://images.novusbio.com/fullsize/nb100-2323_rabbit-polyclonal-ire1-alpha-p-ser724-antibody-31020241537195.jpg)
![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.](http://images.novusbio.com/fullsize/nb100-2323_rabbit-polyclonal-ire1-alpha-p-ser724-antibody-310202415535198.jpg)
![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.](http://images.novusbio.com/fullsize/nb100-2323_rabbit-polyclonal-ire1-alpha-p-ser724-antibody-310202415535172.jpg)
![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.](http://images.novusbio.com/fullsize/nb100-2323_rabbit-polyclonal-ire1-alpha-p-ser724-antibody-31020241682191.jpg)
![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.](http://images.novusbio.com/fullsize/nb100-2323_rabbit-polyclonal-ire1-alpha-p-ser724-antibody-31020241682134.jpg)
![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.](http://images.novusbio.com/fullsize/nb100-2323_rabbit-polyclonal-ire1-alpha-p-ser724-antibody-310202415525219.jpg)
![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.](http://images.novusbio.com/fullsize/nb100-2323_rabbit-polyclonal-ire1-alpha-p-ser724-antibody-31020241553727.jpg)
![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.](http://images.novusbio.com/fullsize/nb100-2323_rabbit-polyclonal-ire1-alpha-p-ser724-antibody-310202415541960.jpg)
![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.](http://images.novusbio.com/fullsize/nb100-2323_rabbit-polyclonal-ire1-alpha-p-ser724-antibody-31020241553725.jpg)
![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.](http://images.novusbio.com/fullsize/nb100-2323_rabbit-polyclonal-ire1-alpha-p-ser724-antibody-31020241554530.jpg)
![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.](http://images.novusbio.com/fullsize/nb100-2323_rabbit-polyclonal-ire1-alpha-p-ser724-antibody-3102024155527.jpg)
![Western Blot: TDP-43/TARDBP Antibody (2E2-D3) [H00023435-M01] - TARDBP monoclonal antibody (M01), clone 2E2-D3 Analysis of TARDBP expression in A-431.](http://images.novusbio.com/fullsize/TDP-43-TARDBP-Antibody-2E2-D3-Western-Blot-H00023435-M01-img0025.jpg "Western Blot: TDP-43/TARDBP Antibody (2E2-D3) [H00023435-M01] - TARDBP monoclonal antibody (M01), clone 2E2-D3 Analysis of TARDBP expression in A-431.")
![Immunohistochemistry-Paraffin: TDP-43/TARDBP Antibody (2E2-D3) [H00023435-M01] - TARDBP in rat tissue samples. Image courtsey of product review by Daniel Pirici.](http://images.novusbio.com/fullsize/TDP-43-TARDBP-Antibody-2E2-D3-Immunohistochemistry-Paraffin-H00023435-M01-img0011.jpg)
![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.](http://images.novusbio.com/fullsize/TDP-43-TARDBP-Antibody-2E2-D3-Western-Blot-H00023435-M01-img0028.jpg)
![Immunocytochemistry/Immunofluorescence: TDP-43/TARDBP Antibody (2E2-D3) [H00023435-M01] - Analysis of monoclonal antibody to TARDBP on HeLa cell. Antibody concentration 10 ug/ml.](http://images.novusbio.com/fullsize/TDP-43-TARDBP-Antibody-2E2-D3-Immunocytochemistry-Immunofluorescence-H00023435-M01-img0019.jpg)
![Immunohistochemistry-Paraffin: TDP-43/TARDBP Antibody (2E2-D3) [H00023435-M01] - TARDBP on formalin-fixed paraffin-embedded human leiomyosarcoma. [antibody concentration 3 ug/ml]](http://images.novusbio.com/fullsize/TDP-43-TARDBP-Antibody-2E2-D3-Immunohistochemistry-Paraffin-H00023435-M01-img0013.jpg)
![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.](http://images.novusbio.com/fullsize/TDP-43-TARDBP-Antibody-2E2-D3-Western-Blot-H00023435-M01-img0026.jpg)
![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.](http://images.novusbio.com/fullsize/TDP-43-TARDBP-Antibody-2E2-D3-Immunohistochemistry-Paraffin-H00023435-M01-img0021.jpg)
![<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.](http://images.novusbio.com/fullsize/TDP-43-TARDBP-Antibody-2E2-D3-Western-Blot-H00023435-M01-img0023.jpg)
![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.](http://images.novusbio.com/fullsize/TDP-43-TARDBP-Antibody-2E2-D3-ELISA-H00023435-M01-img0027.jpg)
![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.](http://images.novusbio.com/fullsize/h00023435-m01_mouse-monoclonal-tdp-43-tardbp-antibody-2e2-d3-310202415284521.jpg)
![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.](http://images.novusbio.com/fullsize/h00023435-m01_mouse-monoclonal-tdp-43-tardbp-antibody-2e2-d3-310202415483647.jpg)
![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.](http://images.novusbio.com/fullsize/h00023435-m01_mouse-monoclonal-tdp-43-tardbp-antibody-2e2-d3-310202415482260.jpg)
![Immunohistological analysis of brain stem section stained with rabbit polyclonal Laminin Antibody [NB300-144], dilution 1:1,000 in red, and costained with chicken pAb to Myelin Basic Protein (MBP), dilution 1:5,000 in green. The blue is DAPI staining of nuclear DNA. Following transcardial perfusion of rat with 4% paraformaldehyde, brain was post fixed for 24 hours, cut to 45 uM, and free-floating sections were stained with the above antibodies. The laminin antibody is an excellent marker of basement membranes surrounding blood vessels, while the MBP antibody stains the myelin sheathes around axons.](http://images.novusbio.com/fullsize/Laminin-Antibody-Immunohistochemistry-Free-Floating-NB300-144-img0018.jpg "Immunohistological analysis of brain stem section stained with rabbit polyclonal Laminin Antibody [NB300-144], dilution 1:1,000 in red, and costained with chicken pAb to Myelin Basic Protein (MBP), dilution 1:5,000 in green. The blue is DAPI staining of nuclear DNA. Following transcardial perfusion of rat with 4% paraformaldehyde, brain was post fixed for 24 hours, cut to 45 uM, and free-floating sections were stained with the above antibodies. The laminin antibody is an excellent marker of basement membranes surrounding blood vessels, while the MBP antibody stains the myelin sheathes around axons.")
![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.](http://images.novusbio.com/fullsize/Laminin-Antibody-Immunohistochemistry-NB300-144-img0022.jpg)
![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.](http://images.novusbio.com/fullsize/Laminin-Antibody-Immunohistochemistry-Free-Floating-NB300-144-img0014.jpg)
![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.](http://images.novusbio.com/fullsize/Laminin-Antibody-Immunohistochemistry-NB300-144-img0008.jpg)
![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.](http://images.novusbio.com/fullsize/Laminin-Antibody-Western-Blot-NB300-144-img0017.jpg)
![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).](http://images.novusbio.com/fullsize/Laminin-Antibody-Immunocytochemistry-Immunofluorescence-NB300-144-img0011.jpg)
![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.](http://images.novusbio.com/fullsize/Laminin-Antibody-Western-Blot-NB300-144-img0024.jpg)
![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.](http://images.novusbio.com/fullsize/Laminin-Antibody-Flow-Cytometry-NB300-144-img0020.jpg)
![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.](http://images.novusbio.com/fullsize/Laminin-Antibody-Western-Blot-NB300-144-img0010.jpg)
![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.](http://images.novusbio.com/fullsize/Laminin-Antibody-Immunohistochemistry-NB300-144-img0023.jpg)
![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.](http://images.novusbio.com/fullsize/nb300-144_rabbit-polyclonal-laminin-antibody-310202415171342.jpg)
![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.](http://images.novusbio.com/fullsize/nb300-144_rabbit-polyclonal-laminin-antibody-310202416212338.jpg)
![Immunohistochemistry: IRE1 alpha Antibody [NB100-2324] - XBP1 and TG2 deficiency promote increased IRE1a protein levels in cultured VSMCs and in neointima in situ. (D) Xbp1WT and Xbp1 delta WT and (E) Tgm2 WT and Tgm2 delta carotid artery sections were analyzed by IHC for total IRE1a. Image collected and cropped by CiteAb from the following publication (//doi.org/10.1371/journal.pone.0212235) licensed under a CC-BY license.](http://images.novusbio.com/fullsize/IRE1-alpha-Antibody-Immunohistochemistry-NB100-2324-img0010.jpg "Immunohistochemistry: IRE1 alpha Antibody [NB100-2324] - XBP1 and TG2 deficiency promote increased IRE1a protein levels in cultured VSMCs and in neointima in situ. (D) Xbp1WT and Xbp1 delta WT and (E) Tgm2 WT and Tgm2 delta carotid artery sections were analyzed by IHC for total IRE1a. Image collected and cropped by CiteAb from the following publication (//doi.org/10.1371/journal.pone.0212235) licensed under a CC-BY license.")
![<b>Genetic Strategies Validation. </b>Western Blot: IRE1 alpha Antibody [NB100-2324] - Total IRE1 Alpha protein in lysates from Min6 cells which were transfected with GFP-siRNA or Ire1-siRNA. Theoretical molecular weight: 110 kDa.](http://images.novusbio.com/fullsize/IRE1-alpha-Antibody-Western-Blot-NB100-2324-img0006.jpg)
![Western Blot: IRE1 alpha Antibody [NB100-2324] - ALOX15 knockout blocks alcohol-induced up-regulation of IRE1a in mouse liver. Image from verified customer review.](http://images.novusbio.com/fullsize/IRE1-alpha-Antibody-Western-Blot-NB100-2324-img0009.jpg)
![Immunocytochemistry/Immunofluorescence: IRE1 alpha Antibody [NB100-2324] - IRE-1 alpha antibody was tested in HeLa cells at 1:200 against Dylight 488 (Green). Alpha tubulin and nuclei were counterstained against Dylight 568 (Red) and DAPI (Blue).](http://images.novusbio.com/fullsize/IRE1-alpha-Antibody-Immunocytochemistry-Immunofluorescence-NB100-2324-img0005.jpg)
![Immunohistochemistry-Paraffin: IRE1 alpha Antibody [NB100-2324] - Analysis of a formalin fixed mouse colon tissue section using total IRE1 alpha antibody (NB100-2324) at 1:300. Note a strong cytoplasmic signal in various cells of colonic villi (columnar epithelial and goblet cells) and the muscular layer. A few cells, potentially with active UPR, showed nuclear positivity also while the signal was negligible in cells at base of crypts and lamina propria.](http://images.novusbio.com/fullsize/IRE1-alpha-Antibody-Immunohistochemistry-Paraffin-NB100-2324-img0007.jpg)
![Immunohistochemistry-Paraffin: IRE1 alpha Antibody [NB100-2324] - Analysis of a formalin fixed mouse colon tissue section using total IRE1 alpha antibody (NB100-2324) at 1:300. Note a strong cytoplasmic signal in various cells of colonic villi (columnar epithelial and goblet cells) and the muscular layer. Some cells, most likely with active UPR, depicted nuclear positivity also while the signal was negligible in crypts cells and lamina propria.](http://images.novusbio.com/fullsize/IRE1-alpha-Antibody-Immunohistochemistry-Paraffin-NB100-2324-img0008.jpg)
![Western Blot: IRE1 alpha Antibody [NB100-2324] - Zn (II)-curc induces endoplasmic reticulum (ER) stress in mutant p53H273-carrying cells. (a) Representative photomicrographs of ER-Red Fluorescence staining in U373 cells untreated (Mock) or treated with Zn (II)-curc (100 µg/mL) for 16 h (Original magnification: 40×). (b) Quantization of ER content in U373 cells from ER-Red Fluorescence-stained cells. Mean fluorescence intensity (MFI) of each individual cell was normalized to cell size & expressed as fold-change compared with untreated cells at the same time point. Histograms represent the mean ± SD of three independent experiments. * p ≤ 0.05. (c) Western blot analysis of p53, BiP, total (tot) IRE1 alpha , phosphorylated (p) IRE1 alpha , & XBP1 spliced (s) protein levels evaluated in U373 & HT29 cells untreated or treated with Zn (II)-curc (100 µg/mL) for 24 h. (d) Densitometric analysis was performed using Image J software to calculate the ratio of the protein levels, as detected in (c), vs. beta -actin. Histograms represent the mean ± SD of three independent experiments. * p ≤ 0.05. (e) Total mRNA was extracted from U373 & HT29 cells untreated or treated with Zn (II)-curc (100 µg/mL) for 24 h. Spliced (s) Xbp1 gene expression was assayed by the polymerase chain reaction (PCR) of reverse-transcribed cDNA. Densitometric analysis was performed using Image J software to calculate the Xbp1s/28S ratio. Histograms represent the mean ± SD of three independent experiments. * p ≤ 0.05. (f) p53 gene expression was assayed by PCR as in (e). The p53/28S ratio is indicated. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/32138264), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-2324_rabbit-polyclonal-ire1-alpha-antibody-31020241554542.jpg)
![Western Blot: Bestrophin 1 Antibody (E6-6) - BSA Free [NB300-164] - Western blot analysis of the normal and mutant human Best1 protein in transiently transfected MDCK cells. Best1 proteins are detectable as a 68 kDa band in all transfected cells, but not in non-transfected controls (MDCK lane). Actin bands are shown to indicate equal loading of cell lysates. Image collected and cropped by CiteAb from the following publication (//www.mdpi.com/1422-0067/14/7/15121), licensed under a CC-BY license.](http://images.novusbio.com/fullsize/Bestrophin-1-Antibody-E6-6-BSA-Free-Western-Blot-NB300-164-img0007.jpg "Western Blot: Bestrophin 1 Antibody (E6-6) - BSA Free [NB300-164] - Western blot analysis of the normal and mutant human Best1 protein in transiently transfected MDCK cells. Best1 proteins are detectable as a 68 kDa band in all transfected cells, but not in non-transfected controls (MDCK lane). Actin bands are shown to indicate equal loading of cell lysates. Image collected and cropped by CiteAb from the following publication (//www.mdpi.com/1422-0067/14/7/15121), licensed under a CC-BY license.")
![Immunocytochemistry/Immunofluorescence: Bestrophin 1 Antibody (E6-6) - BSA Free [NB300-164] - X-Z confocal single image scan of transiently transfected cells with different BEST1 cDNA constructs showing mislocalization of mutants Y85H, Q96R, L100R and Y227N. Cells were stained for Best1 (green), beta-catenin (red) and nuclei (blue). Scale bar = 10 um. Image collected and cropped by CiteAb from the following publication (//www.mdpi.com/1422-0067/14/7/15121), licensed under a CC-BY license.](http://images.novusbio.com/fullsize/Bestrophin-1-Antibody-E6-6-BSA-Free-Immunocytochemistry-Immunofluorescence-NB300-164-img0008.jpg)
![Immunohistochemistry-Paraffin: Bestrophin 1 Antibody (E6-6) - BSA Free [NB300-164] - Bestrophin 1 was detected in immersion fixed paraffin sections of human small intestine using t Mouse Anti-Human Bestrophin 1 Monoclonal Antibody (Catalog # NB300-164) at 5 ug/mL for 1 hour at room temperature followed by incubation with the Anti-Mouse IgG VisUCyte™ HRP Polymer Antibody (Catalog # VC001). Tissue was stained using DAB (brown) and counterstained with hematoxylin (blue). Specific staining was localized to the cell surface and extracellular.](http://images.novusbio.com/fullsize/Bestrophin-1-Antibody-E6-6-BSA-Free-Immunohistochemistry-Paraffin-NB300-164-img0005.jpg)
![Western Blot: Bestrophin 1 Antibody (E6-6) - BSA Free [NB300-164] - Detection of Bestrophin (68 kDa) from human RPE cell lysate.](http://images.novusbio.com/fullsize/Bestrophin-1-Antibody-E6-6-BSA-Free-Western-Blot-NB300-164-img0003.jpg)
![Immunohistochemistry-Paraffin: Bestrophin 1 Antibody (E6-6) - BSA Free [NB300-164] - Bestrophin 1 was detected in immersion fixed paraffin-embedded sections of human brain using Mouse Anti-Human Bestrophin 1 (E6-6) Monoclonal Antibody (Catalog # NB300-164) at 1:300 for 1 hour at room temperature followed by incubation with the Anti-Mouse IgG VisUCyte™ HRP Polymer Antibody (Catalog # VC001). Tissue was stained using DAB (brown) and counterstained with hematoxylin (blue). Specific staining was localized to the cytoplasm in neurons.](http://images.novusbio.com/fullsize/Bestrophin-1-Antibody-E6-6-BSA-Free-Immunohistochemistry-Paraffin-NB300-164-img0004.jpg)
![<b>Genetic Strategies Validation. </b>Western Blot: Bestrophin 1 Antibody (E6-6) - BSA Free [NB300-164] - 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.](http://images.novusbio.com/fullsize/Bestrophin-1-Antibody-E6-6-BSA-Free-Knockout-Validated-NB300-164-img0009.jpg)
![Dual RNAscope ISH-IHC: Bestrophin 1 Antibody (E6-6) - BSA Free [NB300-164] - Formalin-fixed paraffin-embedded tissue sections of human duodenum were probed for Bestrophin 1 mRNA (ACD RNAScope Probe, catalog # 433181; Fast Red chromogen, ACD catalog # 322360). Adjacent tissue section was processed for immunohistochemistry using mouse anti-human (Novus Biologicals catalog # NB300-164) at 0.3ug/mL with overnight incubation at 4 degrees Celsius followed by incubation with anti-mouse IgG VisUCyte HRP Polymer Antibody (Catalog # VC001) and DAB chromogen (yellow-brown). Tissue was counterstained with hematoxylin (blue). IHC signal is confined to cytoplasm.](http://images.novusbio.com/fullsize/Bestrophin-1-Antibody-E6-6-BSA-Free-Dual-RNAscope-ISH-IHC-NB300-164-img0006.jpg)
![Western Blot: Bestrophin 1 Antibody (E6-6) - BSA Free [NB300-164] - (a) Schematic drawing showing localization of the different mutations (black diamonds) tested in our study (modified from [12]); (b) Western blot analysis of the normal & mutant human Best1 protein in transiently transfected MDCK cells. Best1 proteins are detectable as a 68 kDa band in all transfected cells, but not in non-transfected controls (MDCK lane). Actin bands are shown to indicate equal loading of cell lysates. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/23880862), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb300-164_mouse-monoclonal-bestrophin-1-antibody-e6-6-31020241534336.jpg)
![Immunocytochemistry/ Immunofluorescence: Bestrophin 1 Antibody (E6-6) - BSA Free [NB300-164] - Subcellular localization of WT & mutant BEST1 in iPSC-RPEs. Confocal images showing the co-staining of BEST1, Collagen IV & Hoechst in iPSC-RPEs derived from a WT donor or patients. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31836750), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb300-164_mouse-monoclonal-bestrophin-1-antibody-e6-6-310202415363746.jpg)
![Western Blot: Bestrophin 1 Antibody (E6-6) - BSA Free [NB300-164] - (a) HPRT & BEST1 mRNAs are expressed in MDCK & RPE-J cells. M–100 bp ladder, N–negative control; (b) Quantification of BEST1 expression levels between MDCK & RPE-J cells using quantitative Real-Time PCR. Fold change variation in BEST1 expression levels is reported as 2^-delta delta Ct value, the reference mRNA being HPRT (mean ± SEM., n = 2); (c) Western blot analysis—Best1 protein is not synthesized by RPE-J or MDCK cells. After transfection, MDCK produce human Best1 at 68 kDa. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/23880862), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb300-164_mouse-monoclonal-bestrophin-1-antibody-e6-6-310202415284544.jpg)
![Immunocytochemistry/ Immunofluorescence: Bestrophin 1 Antibody (E6-6) - BSA Free [NB300-164] - Characterization of WT iPSC & iPSC-RPE.(A) Phase picture of established WT iPSC line before differentiation. Scale bar, 400 μm. (B) Immunocytofluorescence images of pluripotency markers in established iPSC. Scale bar, 200 μm. (C) Confocal images showing plasma membrane localization of BEST1. Scale bar, 10 μm. (D) Comparison of current amplitudes in iPSC-RPEs from two BEST1 WT donors. Bar chart showing the steady-state current amplitudes at 0 [Ca2+]i, 1.2 μM [Ca2+]i, & 1.2 μM [Ca2+]i + 100 μM NFA in RPEs from two distinct BEST1 WT human donors; n = 5–6. ∗$p<0.05 compared to current amplitudes at 1.2 μM [Ca2+]i from donor #1 & #2, respectively, using two-tailed unpaired Student t test. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/29063836), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb300-164_mouse-monoclonal-bestrophin-1-antibody-e6-6-31020241535684.jpg)
![Western Blot: Bestrophin 1 Antibody (E6-6) - BSA Free [NB300-164] - CRISPR/Cas9-mediated gene silencing in combination with augmentation.(a) Augmented BEST1-GFP & endogenous BEST1 were detected by immunoblotting in hPSC-RPE cells. (b) Schematic of the baculovirus-based silencing (BVSi) vector. (c) Immunoblotting showing the knockdown of endogenous BEST1 expression with BVSi vectors & augmentation of wobble BEST1-mCherry in WT hPSC-RPE cells. (d) Immunoblotting showing the knockdown of endogenous BEST1 expression with BVSi 3–8 & augmentation of wobble BEST1-mCherry in hPSC-RPE cells carrying BEST1 gain-of-function mutations. 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.](http://images.novusbio.com/fullsize/nb300-164_mouse-monoclonal-bestrophin-1-antibody-e6-6-31020241537190.jpg)
![Western Blot: Bestrophin 1 Antibody (E6-6) - BSA Free [NB300-164] - CRISPR/Cas9-mediated gene silencing in combination with augmentation.(a) Augmented BEST1-GFP & endogenous BEST1 were detected by immunoblotting in hPSC-RPE cells. (b) Schematic of the baculovirus-based silencing (BVSi) vector. (c) Immunoblotting showing the knockdown of endogenous BEST1 expression with BVSi vectors & augmentation of wobble BEST1-mCherry in WT hPSC-RPE cells. (d) Immunoblotting showing the knockdown of endogenous BEST1 expression with BVSi 3–8 & augmentation of wobble BEST1-mCherry in hPSC-RPE cells carrying BEST1 gain-of-function mutations. 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.](http://images.novusbio.com/fullsize/nb300-164_mouse-monoclonal-bestrophin-1-antibody-e6-6-31020241539730.jpg)
![Western Blot: Bestrophin 1 Antibody (E6-6) - BSA Free [NB300-164] - 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.](http://images.novusbio.com/fullsize/nb300-164_mouse-monoclonal-bestrophin-1-antibody-e6-6-31020241535628.jpg)
![Immunocytochemistry/ Immunofluorescence: Bestrophin 1 Antibody (E6-6) - BSA Free [NB300-164] - Impact of BEST1 pathogenic variants in bestrophin-1 RPE localization. Cryosections obtained from the BD donors & an 88-year-old control were labeled with antibodies specific to bestrophin-1 (green), while cell nuclei have been labeled with TO-PRO-3 (blue). Bruch’s membrane is indicated by the hashed white line. Arrow = mislocalized apical RPE distribution of bestrophin-1; arrowheads = basolateral RPE distribution of bestrophin-1; double arrowheads = intracellular bestrophin-1. Scale bar = 40 μm (all images). Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/33154968), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb300-164_mouse-monoclonal-bestrophin-1-antibody-e6-6-310202415395959.jpg)
![Immunocytochemistry/ Immunofluorescence: Bestrophin 1 Antibody (E6-6) - BSA Free [NB300-164] - Subcellular localization of WT & mutant BEST1 in iPSC-RPEs. Confocal images showing the co-staining of BEST1, Collagen IV & Hoechst in iPSC-RPEs derived from a WT donor or patients. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31836750), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb300-164_mouse-monoclonal-bestrophin-1-antibody-e6-6-310202415175245.jpg)
![Immunocytochemistry/ Immunofluorescence: Bestrophin 1 Antibody (E6-6) - BSA Free [NB300-164] - (a) X-Z confocal single image scan of transiently transfected cells with different BEST1 cDNA constructs showing mislocalization of mutants Y85H, Q96R, L100R & Y227N. Cells were stained for Best1 (green), beta -catenin (red) & nuclei (blue). Scale bar = 10 μm; (b) Z-series confocal stack signals corresponding to each labeling were quantified. Curves indicate the pixel intensity of each section along the Z-axis for each cell (Best1, green; beta -catenin, red; nuclei, blue). The black vertical line indicates the Z-focal plane chosen as threshold for apical & basolateral domains separation. Basolateral & apical sides are as indicated. Horizontal axis represents μm distance & vertical axis shows pixel intensities; (c) Bar graph illustrating quantification of Best1 mutants distribution in the basolateral & apical domains of the cells compared with normal protein (mean ± SEM., n = 10, *p < 0.01, ***p < 0.0001). Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/23880862), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb300-164_mouse-monoclonal-bestrophin-1-antibody-e6-6-31020241621835.jpg)
![Immunohistochemistry: SMN Antibody (2B1) [NB100-1936] - CBs lose their colocalization with SMN nuclear foci in diabetic mice. Normal and pathological distribution of SMN proteins in sensory neurons. SMN proteins were found throughout the cytoplasm and as nuclear foci in control sensory neurons. SMN nuclear foci localized within CBs (coilin) in controls (upper panels, white arrows), whereas in the diabetic nucleus the numerous CBs were present but lost their colocalization with SMN nuclear foci (lower panels, yellow arrows). Arrowheads indicate sensory neurons magnified in the insets. Scale bars: 20 um, 10 um in insets. Image collected and cropped by CiteAb from the following publication (//dmm.biologists.org/lookup/doi/10.1242/dmm.028225), licensed under a CC-BY license.](http://images.novusbio.com/fullsize/SMN-Antibody-2B1-Immunohistochemistry-NB100-1936-img0007.jpg "Immunohistochemistry: SMN Antibody (2B1) [NB100-1936] - CBs lose their colocalization with SMN nuclear foci in diabetic mice. Normal and pathological distribution of SMN proteins in sensory neurons. SMN proteins were found throughout the cytoplasm and as nuclear foci in control sensory neurons. SMN nuclear foci localized within CBs (coilin) in controls (upper panels, white arrows), whereas in the diabetic nucleus the numerous CBs were present but lost their colocalization with SMN nuclear foci (lower panels, yellow arrows). Arrowheads indicate sensory neurons magnified in the insets. Scale bars: 20 um, 10 um in insets. Image collected and cropped by CiteAb from the following publication (//dmm.biologists.org/lookup/doi/10.1242/dmm.028225), licensed under a CC-BY license.")
![Western Blot: SMN Antibody (2B1) [NB100-1936] - Analysis of SMN expression in 1) HeLa, 2) NTera2, 3) HepG2, 4) MCF7, 5) NIH 3T3, 6) PC12, and 7) COS7 whole cell lysates.](http://images.novusbio.com/fullsize/SMN-Antibody-2B1-Western-Blot-NB100-1936-img0003.jpg)
![Immunocytochemistry/Immunofluorescence: SMN Antibody (2B1) [NB100-1936] - HeLa cells were fixed in 4% paraformaldehyde for 10 minutes and permeabilized in 0.5% Triton X-100 in PBS for 5 minutes. The cells were incubated with anti- NB100-1936 at 2 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 100X objective and digitally deconvolved.](http://images.novusbio.com/fullsize/SMN-Antibody-2B1-Immunocytochemistry-Immunofluorescence-NB100-1936-img0011.jpg)
![Immunocytochemistry/Immunofluorescence: SMN Antibody (2B1) [NB100-1936] - scIF of control (f) and etv5b MO (g) cells from pmnx1:eGFP embryos. H2B, GFP and Smn signals are shown in Z-projected confocal sections. GFP+ cells marked by white rectangles are magnified on the right. Scale bars: 10 um for low and 5 um for high magnification. Image collected and cropped by Citeab from the following publication (Transcriptional enhancement of Smn levels in motoneurons is crucial for proper axon morphology in zebrafish. Sci Rep (2016) licensed under a CC-BY license.](http://images.novusbio.com/fullsize/SMN-Antibody-2B1-Immunocytochemistry-Immunofluorescence-NB100-1936-img0010.jpg)
![Immunocytochemistry/Immunofluorescence: SMN Antibody (2B1) [NB100-1936] - HeLa 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 SMN Antibody [2B1] conjugated to Alexa Fluor 488 (NB100-1936AF488) at 5 ug/ml for 1 hour at room temperature. Nuclei were counterstained with DAPI (Blue). Cells were imaged using a 100X objective and digitally deconvolved.](http://images.novusbio.com/fullsize/SMN-Antibody-2B1-Immunocytochemistry-Immunofluorescence-NB100-1936-img0012.jpg)
![Flow Cytometry: SMN Antibody (2B1) [NB100-1936] - An intracellular stain was performed on Neuro2a cells with SMN Antibody (2B1) NB100-1936 (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).](http://images.novusbio.com/fullsize/SMN-Antibody-2B1-Flow-Cytometry-NB100-1936-img0009.jpg)
![Immunocytochemistry/Immunofluorescence: SMN Antibody (2B1) [NB100-1936] - The SMN antibody was tested at a 1:250 dilution in HeLa cells against DyLight 488 (Green). Actin nuclei were counterstained against Phalloidin 568 (Red) and DAPI (Blue), respectively.](http://images.novusbio.com/fullsize/SMN-Antibody-2B1-Immunocytochemistry-Immunofluorescence-NB100-1936-img0004.jpg)
![Immunohistochemistry: SMN Antibody (2B1) [NB100-1936] - Analysis of SMN on mouse brain using NB100-1936.](http://images.novusbio.com/fullsize/SMN-Antibody-2B1-Immunohistochemistry-NB100-1936-img0001.jpg)
![Flow Cytometry: SMN Antibody (2B1) [NB100-1936] - An intracellular stain was performed on Ntera2 cells with SMN Antibody (2B1) NB100-1936 (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).](http://images.novusbio.com/fullsize/SMN-Antibody-2B1-Flow-Cytometry-NB100-1936-img0008.jpg)
![Immunocytochemistry/ Immunofluorescence: SMN Antibody (2B1) [NB100-1936] - CWC22 is colocalized with nuclear speckles & upregulated in diabetic DRG sensory neurons. (A) Subcellular distribution of TDP-43 & CWC22 in control DRG sensory neurons. TDP-43 was stained diffusely in the nucleus, excluding SMN foci in sensory neurons. CWC22 consistently colocalized with a marker protein SC35 of nuclear speckles in sensory neurons. No obvious differences in the subcellular localization of CWC22 were identified in diabetic neurons (not shown) compared with controls. Scale bar: 10 μm. (B) qRT-PCR analysis of Cwc22 mRNA expression in diabetic & control mice. Cwc22 expression was upregulated ∼2.5-fold in diabetic DRGs. *P<0.05, unpaired two-tailed Student's t-test. Data represented as mean±s.e.m. See Cheng et al. (2015) for microarray data indicating rises in Cwc22 expression as reported separately. Image collected & cropped by CiteAb from the following publication (//journals.biologists.com/dmm/article/10/3/215/2257/Diabetic-polyneuropathy-sensory-neurons-nuclear), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-1936_mouse-monoclonal-smn-antibody-2b1-3102024168396.jpg)
![Western Blot: TDP-43/TARDBP Antibody [NB110-55376] - Total protein from HeLa, MCF7 and mouse brain was separated on a 12% gel by SDS-PAGE, transferred to PVDF membrane and blocked in 5% non-fat milk in TBST. The membrane was probed with 1.0 ug/ml anti-TARDBP in 1% block buffer and detected with an anti-rabbit HRP secondary antibody using chemiluminescence.](http://images.novusbio.com/fullsize/TDP-43-TARDBP-Antibody-Western-Blot-NB110-55376-img0012.jpg "Western Blot: TDP-43/TARDBP Antibody [NB110-55376] - Total protein from HeLa, MCF7 and mouse brain was separated on a 12% gel by SDS-PAGE, transferred to PVDF membrane and blocked in 5% non-fat milk in TBST. The membrane was probed with 1.0 ug/ml anti-TARDBP in 1% block buffer and detected with an anti-rabbit HRP secondary antibody using chemiluminescence.")
![Immunocytochemistry/Immunofluorescence: TDP-43/TARDBP Antibody [NB110-55376] - HeLa cells were fixed in 4% paraformaldehyde for 10 minutes and permeabilized in 0.5% Triton X-100 in PBS for 5 minutes. The cells were incubated with TDP-43/TARDBP Antibody conjugated to Alexa Fluor 488 (NB110-55376AF488) at 10 ug/ml for 1 hour at room temperature. Nuclei were counterstained with DAPI (Blue). Cells were imaged using a 100X objective and digitally deconvolved.](http://images.novusbio.com/fullsize/TDP-43-TARDBP-Antibody-Immunocytochemistry-Immunofluorescence-NB110-55376-img0014.jpg)
![Immunocytochemistry/Immunofluorescence: TDP-43/TARDBP Antibody [NB110-55376] - HeLa cells were fixed for 10 minutes using 10% formalin and then permeabilized for 5 minutes using 1X PBS + 0.5% Triton X-100. The cells were incubated with anti-TARDBP at 2 ug/ml overnight at 4C and detected with an anti-rabbit DyLight 488 (Green) at a 1:500 dilution. Nuclei were counterstained with DAPI (Blue). Cells were imaged using a 40X objective.](http://images.novusbio.com/fullsize/TDP-43-TARDBP-Antibody-Immunocytochemistry-Immunofluorescence-NB110-55376-img0011.jpg)
![Immunohistochemistry-Paraffin: TDP-43/TARDBP Antibody [NB110-55376] - Analysis of FFPE human placenta using TDP-43 antibody at 1:250 on a Bond Rx autostainer (Leica Biosystems). The assay involved 20 minutes of heat induced antigen retrieval (HIER) using 10mM sodium citrate buffer (pH 6.0) and endogenous peroxidase quenching with peroxide block. The sections were incubated with primary antibody for 30 minutes and Bond Polymer Refine Detection (Leica Biosystems) with DAB was used for signal development followed by counterstaining with hematoxylin. Whole slide scanning and capturing of representative images was performed using Aperio AT2 (Leica Biosystems). Nuclear staining was observed. Staining was performed by Histowiz.](http://images.novusbio.com/fullsize/TDP-43-TARDBP-Antibody-Immunohistochemistry-Paraffin-NB110-55376-img0010.jpg)
![Western Blot: TDP-43/TARDBP Antibody [NB110-55376] - TARDBP antibody was tested in HeLa WCE.](http://images.novusbio.com/fullsize/TDP-43-TARDBP-Antibody-Western-Blot-NB110-55376-img0004.jpg)
![Western Blot: TDP-43/TARDBP Antibody [NB110-55376] - Cells were transfected with the pCMV6-ENTRY control or pCMV6-ENTRY TARDBP cDNA for 48 hrs and lysed. Equivalent amounts of cell lysates (5 ug per lane) were separated by SDS-PAGE and immunoblotted with anti-TARDBP.](http://images.novusbio.com/fullsize/TDP-43-TARDBP-Antibody-Western-Blot-NB110-55376-img0006.jpg)
![Immunocytochemistry/Immunofluorescence: TDP-43/TARDBP Antibody [NB110-55376] - TARDBP antibody was tested in MCF-7 cells with DyLight 488 (Green). Nuclei and alpha-tubulin were counterstained with DAPI (Blue) and DyLight 550 (Red).](http://images.novusbio.com/fullsize/TDP-43-TARDBP-Antibody-Immunocytochemistry-Immunofluorescence-NB110-55376-img0001.jpg)
![Immunocytochemistry/Immunofluorescence: TDP-43/TARDBP Antibody [NB110-55376] - Analysis using the DyLight 550 conjugate of NB110-55376. Staining of Human iPS derived neurons, fixed in 4% formaldehyde solution. NB110-55376R was diluted 1:200. All antibodies were diluted in PBS/BSA 3% (w/v) ) Triton X-100 0,3 % (v/v). Images taken by an Arrayscan (Cellomics). Blue dots in TDP staining is Hoechst.](http://images.novusbio.com/fullsize/TDP-43-TARDBP-Antibody-Immunocytochemistry-Immunofluorescence-NB110-55376-img0008.jpg)
![Immunocytochemistry/Immunofluorescence: TDP-43/TARDBP Antibody [NB110-55376] - Subcellular distribution of TDP-43 and CWC22 in control DRG sensory neurons. TDP-43 was stained diffusely in the nucleus, excluding SMN foci in sensory neurons. Scale bar: 10 um. Image collected and cropped by CiteAb from the following publication (//dmm.biologists.org/lookup/doi/10.1242/dmm.028225) licensed under a CC-BY license.](http://images.novusbio.com/fullsize/TDP-43-TARDBP-Antibody-Immunocytochemistry-Immunofluorescence-NB110-55376-img0013.jpg)
![Western Blot: GABA-A R gamma 2 Antibody [NB300-190] - Mouse whole brain lysate showing specific immunolabeling of the ~46 kDa gamma-2-subunit of GABAa -R.](http://images.novusbio.com/fullsize/GABA-A-R-gamma-2-Antibody-Western-Blot-NB300-190-img0002.jpg "Western Blot: GABA-A R gamma 2 Antibody [NB300-190] - Mouse whole brain lysate showing specific immunolabeling of the ~46 kDa gamma-2-subunit of GABAa -R.")
![Immunohistochemistry: GABA-A R gamma 2 Antibody [NB300-190] - Immunostaining of mouse retina showing specific labeling of the GABAa gamma-2 subunit in green, calbindin in red and DNA in blue. Photo courtesy of Dr. Arlene Hirano, UCLA.](http://images.novusbio.com/fullsize/GABA-A-R-gamma-2-Antibody-Immunocytochemistry-Immunofluorescence-NB300-190-img0001.jpg)
![Western Blot: GABA-A R gamma 2 Antibody [NB300-190] - Pattern of YFP gamma 2 expression in retinas of Thy1-YFP gamma 2 transgenic mice.(A) Maximum intensity projections (MIP) of confocal image stacks (2 µm total thickness) of vertical slices of Thy1-YFP gamma 2 retinas at postnatal day (P)12 & P21. Diffuse fluorescence expression in cell bodies within the ganglion cell layer (GCL) at both ages, & punctate expression throughout both OFF & ON layers of the inner plexiform layer (IPL) are apparent. There was no expression in the outer plexiform layer (OPL) or the outer nuclear layer (ONL) at either age. (B) Images of MIPs (∼20 µm thick) at various depths of a P21 flat mount Thy1-YFP gamma 2 retina. Inserts are 3× magnification of the images. (C) Western blot of whole brain lysates from Thy1-YFP gamma 2 (Tg) & wildtype (WT) mice. YFP gamma 2 (arrowhead) was detected with anti-GABAAR gamma 2 (upper) & anti-GFP (lower). Image collected & cropped by CiteAb from the following publication (//dx.plos.org/10.1371/journal.pone.0069612), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb300-190_rabbit-polyclonal-gaba-a-r-gamma-2-antibody-31020241620510.jpg)
![Immunocytochemistry/ Immunofluorescence: GABA-A R gamma 2 Antibody [NB300-190] - YFP gamma 2 fluorescence correlates with immunostaining for GABAAR alpha subunits.Cross-correlation analysis of vertical sections from P12 & P21 Thy1-YFP gamma 2 retinas stained with anti-GABAAR alpha 1 (A–D), GABAAR alpha 2 (E–H), or GABAAR alpha 3 (I–L). (M) Image stack of a single ON RGC labeled by transfection of CMV:tdTomato in a Thy1-YFP gamma 2 retina, immunostained for GABAAR alpha 3. (N) The dendritic label was used to mask out the YFP gamma 2 & GABAAR alpha 3 fluorescence. (O) (Upper) YFP gamma 2 & GABAAR alpha 3 puncta within sections of dendritic arbors identified by custom-written software. (Lower) Fraction of the population of YFP gamma 2 puncta that colocalized with GABAAR alpha 3, & vice-versa (average & SEM of 4 cells). White arrowheads are examples of colocalized puncta, green & red arrowheads, non-colocalized puncta. Scale bars 5 µm. Image collected & cropped by CiteAb from the following publication (//dx.plos.org/10.1371/journal.pone.0069612), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb300-190_rabbit-polyclonal-gaba-a-r-gamma-2-antibody-310202416212325.jpg)
![Immunocytochemistry/ Immunofluorescence: GABA-A R gamma 2 Antibody [NB300-190] - YFP gamma 2 fluorescence correlates with immunostaining for GABAAR alpha subunits.Cross-correlation analysis of vertical sections from P12 & P21 Thy1-YFP gamma 2 retinas stained with anti-GABAAR alpha 1 (A–D), GABAAR alpha 2 (E–H), or GABAAR alpha 3 (I–L). (M) Image stack of a single ON RGC labeled by transfection of CMV:tdTomato in a Thy1-YFP gamma 2 retina, immunostained for GABAAR alpha 3. (N) The dendritic label was used to mask out the YFP gamma 2 & GABAAR alpha 3 fluorescence. (O) (Upper) YFP gamma 2 & GABAAR alpha 3 puncta within sections of dendritic arbors identified by custom-written software. (Lower) Fraction of the population of YFP gamma 2 puncta that colocalized with GABAAR alpha 3, & vice-versa (average & SEM of 4 cells). White arrowheads are examples of colocalized puncta, green & red arrowheads, non-colocalized puncta. Scale bars 5 µm. Image collected & cropped by CiteAb from the following publication (//dx.plos.org/10.1371/journal.pone.0069612), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb300-190_rabbit-polyclonal-gaba-a-r-gamma-2-antibody-310202416212373.jpg)
![Immunocytochemistry/ Immunofluorescence: GABA-A R gamma 2 Antibody [NB300-190] - YFP gamma 2 fluorescence correlates with immunostaining for GABAAR alpha subunits.Cross-correlation analysis of vertical sections from P12 & P21 Thy1-YFP gamma 2 retinas stained with anti-GABAAR alpha 1 (A–D), GABAAR alpha 2 (E–H), or GABAAR alpha 3 (I–L). (M) Image stack of a single ON RGC labeled by transfection of CMV:tdTomato in a Thy1-YFP gamma 2 retina, immunostained for GABAAR alpha 3. (N) The dendritic label was used to mask out the YFP gamma 2 & GABAAR alpha 3 fluorescence. (O) (Upper) YFP gamma 2 & GABAAR alpha 3 puncta within sections of dendritic arbors identified by custom-written software. (Lower) Fraction of the population of YFP gamma 2 puncta that colocalized with GABAAR alpha 3, & vice-versa (average & SEM of 4 cells). White arrowheads are examples of colocalized puncta, green & red arrowheads, non-colocalized puncta. Scale bars 5 µm. Image collected & cropped by CiteAb from the following publication (//dx.plos.org/10.1371/journal.pone.0069612), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb300-190_rabbit-polyclonal-gaba-a-r-gamma-2-antibody-31020241621817.jpg)
![Immunocytochemistry/ Immunofluorescence: GABA-A R gamma 2 Antibody [NB300-190] - YFP gamma 2 fluorescence correlates with immunostaining for GABAAR alpha subunits.Cross-correlation analysis of vertical sections from P12 & P21 Thy1-YFP gamma 2 retinas stained with anti-GABAAR alpha 1 (A–D), GABAAR alpha 2 (E–H), or GABAAR alpha 3 (I–L). (M) Image stack of a single ON RGC labeled by transfection of CMV:tdTomato in a Thy1-YFP gamma 2 retina, immunostained for GABAAR alpha 3. (N) The dendritic label was used to mask out the YFP gamma 2 & GABAAR alpha 3 fluorescence. (O) (Upper) YFP gamma 2 & GABAAR alpha 3 puncta within sections of dendritic arbors identified by custom-written software. (Lower) Fraction of the population of YFP gamma 2 puncta that colocalized with GABAAR alpha 3, & vice-versa (average & SEM of 4 cells). White arrowheads are examples of colocalized puncta, green & red arrowheads, non-colocalized puncta. Scale bars 5 µm. Image collected & cropped by CiteAb from the following publication (//dx.plos.org/10.1371/journal.pone.0069612), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb300-190_rabbit-polyclonal-gaba-a-r-gamma-2-antibody-310202416212319.jpg)
![Immunocytochemistry/ Immunofluorescence: GABA-A R gamma 2 Antibody [NB300-190] - YFP gamma 2 fluorescence correlates with immunostaining for GABAAR alpha subunits.Cross-correlation analysis of vertical sections from P12 & P21 Thy1-YFP gamma 2 retinas stained with anti-GABAAR alpha 1 (A–D), GABAAR alpha 2 (E–H), or GABAAR alpha 3 (I–L). (M) Image stack of a single ON RGC labeled by transfection of CMV:tdTomato in a Thy1-YFP gamma 2 retina, immunostained for GABAAR alpha 3. (N) The dendritic label was used to mask out the YFP gamma 2 & GABAAR alpha 3 fluorescence. (O) (Upper) YFP gamma 2 & GABAAR alpha 3 puncta within sections of dendritic arbors identified by custom-written software. (Lower) Fraction of the population of YFP gamma 2 puncta that colocalized with GABAAR alpha 3, & vice-versa (average & SEM of 4 cells). White arrowheads are examples of colocalized puncta, green & red arrowheads, non-colocalized puncta. Scale bars 5 µm. Image collected & cropped by CiteAb from the following publication (//dx.plos.org/10.1371/journal.pone.0069612), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb300-190_rabbit-polyclonal-gaba-a-r-gamma-2-antibody-310202416205172.jpg)
![Immunocytochemistry/ Immunofluorescence: GABA-A R gamma 2 Antibody [NB300-190] - YFP gamma 2 fluorescence correlates with immunostaining for GABAAR alpha subunits.Cross-correlation analysis of vertical sections from P12 & P21 Thy1-YFP gamma 2 retinas stained with anti-GABAAR alpha 1 (A–D), GABAAR alpha 2 (E–H), or GABAAR alpha 3 (I–L). (M) Image stack of a single ON RGC labeled by transfection of CMV:tdTomato in a Thy1-YFP gamma 2 retina, immunostained for GABAAR alpha 3. (N) The dendritic label was used to mask out the YFP gamma 2 & GABAAR alpha 3 fluorescence. (O) (Upper) YFP gamma 2 & GABAAR alpha 3 puncta within sections of dendritic arbors identified by custom-written software. (Lower) Fraction of the population of YFP gamma 2 puncta that colocalized with GABAAR alpha 3, & vice-versa (average & SEM of 4 cells). White arrowheads are examples of colocalized puncta, green & red arrowheads, non-colocalized puncta. Scale bars 5 µm. Image collected & cropped by CiteAb from the following publication (//dx.plos.org/10.1371/journal.pone.0069612), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb300-190_rabbit-polyclonal-gaba-a-r-gamma-2-antibody-310202416205153.jpg)
![Immunocytochemistry/ Immunofluorescence: GABA-A R gamma 2 Antibody [NB300-190] - YFP gamma 2 fluorescence correlates with immunostaining for GABAAR alpha subunits.Cross-correlation analysis of vertical sections from P12 & P21 Thy1-YFP gamma 2 retinas stained with anti-GABAAR alpha 1 (A–D), GABAAR alpha 2 (E–H), or GABAAR alpha 3 (I–L). (M) Image stack of a single ON RGC labeled by transfection of CMV:tdTomato in a Thy1-YFP gamma 2 retina, immunostained for GABAAR alpha 3. (N) The dendritic label was used to mask out the YFP gamma 2 & GABAAR alpha 3 fluorescence. (O) (Upper) YFP gamma 2 & GABAAR alpha 3 puncta within sections of dendritic arbors identified by custom-written software. (Lower) Fraction of the population of YFP gamma 2 puncta that colocalized with GABAAR alpha 3, & vice-versa (average & SEM of 4 cells). White arrowheads are examples of colocalized puncta, green & red arrowheads, non-colocalized puncta. Scale bars 5 µm. Image collected & cropped by CiteAb from the following publication (//dx.plos.org/10.1371/journal.pone.0069612), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb300-190_rabbit-polyclonal-gaba-a-r-gamma-2-antibody-310202416212384.jpg)
![Immunocytochemistry/ Immunofluorescence: GABA-A R gamma 2 Antibody [NB300-190] - YFP gamma 2 fluorescence correlates with immunostaining for GABAAR alpha subunits.Cross-correlation analysis of vertical sections from P12 & P21 Thy1-YFP gamma 2 retinas stained with anti-GABAAR alpha 1 (A–D), GABAAR alpha 2 (E–H), or GABAAR alpha 3 (I–L). (M) Image stack of a single ON RGC labeled by transfection of CMV:tdTomato in a Thy1-YFP gamma 2 retina, immunostained for GABAAR alpha 3. (N) The dendritic label was used to mask out the YFP gamma 2 & GABAAR alpha 3 fluorescence. (O) (Upper) YFP gamma 2 & GABAAR alpha 3 puncta within sections of dendritic arbors identified by custom-written software. (Lower) Fraction of the population of YFP gamma 2 puncta that colocalized with GABAAR alpha 3, & vice-versa (average & SEM of 4 cells). White arrowheads are examples of colocalized puncta, green & red arrowheads, non-colocalized puncta. Scale bars 5 µm. Image collected & cropped by CiteAb from the following publication (//dx.plos.org/10.1371/journal.pone.0069612), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb300-190_rabbit-polyclonal-gaba-a-r-gamma-2-antibody-310202416212327.jpg)
![Western Blot: Apolipoprotein E R2/ApoE R2 Antibody [NB100-2216] - Analysis of ApoER2 on mouse brain membrane.](http://images.novusbio.com/fullsize/Apolipoprotein-E-R2-ApoE-R2-Antibody-Western-Blot-NB100-2216-img0005.jpg "Western Blot: Apolipoprotein E R2/ApoE R2 Antibody [NB100-2216] - Analysis of ApoER2 on mouse brain membrane.")
![Immunocytochemistry/Immunofluorescence: Apolipoprotein E R2/ApoE R2 Antibody [NB100-2216] - Antibody was tested in Neuro-2a cells with Dylight 488 (green). Nuclei and alpha-tubulin were counterstained with DAPI (blue) and Dylight 550 (red).](http://images.novusbio.com/fullsize/Apolipoprotein-E-R2-ApoE-R2-Antibody-Immunocytochemistry-Immunofluorescence-NB100-2216-img0006.jpg)
![Western Blot: TDP-43/TARDBP Antibody (3H8) [NBP1-92695] - Analysis of whole brain lysates and nuclear inreached extract from whole brain using mouse mAb to TDP43, NBP1-92695, dilution 1:2,000 in green: [1] protein standard (red), [2] rat brain, [3] rat brain nuclear extract, [4] mouse brain, [5] mouse brain nuclear extract. Strong band at 43 kDa mark corresponds to TDP43 protein.](http://images.novusbio.com/fullsize/TDP-43-TARDBP-Antibody-3H8-Western-Blot-NBP1-92695-img0005.jpg "Western Blot: TDP-43/TARDBP Antibody (3H8) [NBP1-92695] - Analysis of whole brain lysates and nuclear inreached extract from whole brain using mouse mAb to TDP43, NBP1-92695, dilution 1:2,000 in green: [1] protein standard (red), [2] rat brain, [3] rat brain nuclear extract, [4] mouse brain, [5] mouse brain nuclear extract. Strong band at 43 kDa mark corresponds to TDP43 protein.")
![Immunocytochemistry/Immunofluorescence: TARDBP Antibody (3H8) [NBP1-92695] - NBP1-92695 was used to stain a section of formalin fixed adult rat brain, specifically the hippocampus. Hippocampal neuron nuclei are stained strongly. Chicken antibody to GFAP (NBP1-05198, green) shows the processes of astrocytic glial cells. Nuclei of all cells are revealed with DAPI DNA stain (blue). The TARDBP (3H8) antibody stains neuronal nuclei strongly and the nuclei of some non-neuronal cells much more weakly. Neuronal nuclei therefore look crimson, since they are both red due to the content of TARDBP and blue due to their content of DNA, stained blue with DAPI.](http://images.novusbio.com/fullsize/TARDBP-Antibody-3H8-Immunocytochemistry-Immunofluorescence-NBP1-92695-img0003.jpg)
![Immunohistochemistry Free-Floating: TDP-43/TARDBP Antibody (3H8) [NBP1-92695] - Analysis of rat hippocampus section stained with mouse mAb to TDP43, NBP1-92695, dilution 1:2,000 in red, and costained with chicken pAb to GFAP,, dilution 1:5,000 in green. The blue is DAPI staining of nuclear DNA. Following transcardial perfusion of rat with 4% paraformaldehyde, brain was post fixed for 24 hours, cut to 45uM, and free-floating sections were stained with above antibodies. The TDP43 protein is concentrated in the nuclei of hippocampal neurons, while the GFAP antibody stains the intermediate filament network of astroglial cells.](http://images.novusbio.com/fullsize/TDP-43-TARDBP-Antibody-3H8-Immunocytochemistry-Immunofluorescence-NBP1-92695-img0004.jpg)
![<b>Genetic Strategies Validation. </b>Western Blot: TDP-43/TARDBP Antibody (3H8) [NBP1-92695] - Lysates of HAP1 (WT) and TDP-43/TARDBP (KO) were prepared, and 50 ug of protein was processed for western blot with the TDP-43/TARDBP antibody. The Ponceau stained transfers of the blot is shown (right). Antibody dilution used: NBP1-92695 at 1/1000. Image, protocol, and testing courtesy of YCharOS Inc. (ycharos.com).](http://images.novusbio.com/fullsize/TDP-43-TARDBP-Antibody-3H8-Knockout-Validated-NBP1-92695-img0006.jpg)
![Immunoprecipitation: TDP-43/TARDBP Antibody (3H8) [NBP1-92695] - HAP1 lysates were prepared, and immunoprecipitation was performed using 2.0 ug of the TDP-43/TARDBP antibody pre-coupled to Dynabeads protein G. Sample was washed and processed for immunoblot with the TDP-43/TARDBP antibody. The Ponceau stained transfer of the blot is shown. Image, protocol, and testing courtesy of YCharOS Inc. (ycharos.com).](http://images.novusbio.com/fullsize/TDP-43-TARDBP-Antibody-3H8-Immunoprecipitation-NBP1-92695-img0007.jpg)
![<b>Genetic Strategies Validation. </b>Immunocytochemistry/ Immunofluorescence: TDP-43/TARDBP Antibody (3H8) [NBP1-92695] - HAP1 (WT) and TDP-43/TARDBP (KO) cells were labelled with a green or a far-red fluorescent dye, respectively. WT and KO cells were mixed and plated to a 1:1 ratio in a 96-well plate with glass bottom. Cells were stained with the TDP-43/TARDBP antibody and with the corresponding Alexa-fluor 555 coupled secondary antibody including DAPI. Acquisition of the blue (nucleus-DAPI), green (identification of WT cells), red (antibody staining) and far-red (identification of KO cells) channels was performed. Representative images of the blue and red (grayscale) channels are shown. WT and KO cells are outlined on both channels with green and magenta dashed line, respectively. Antibody dilution used: NBP1-92695 at 1/1000. Image, protocol, and testing courtesy of YCharOS Inc. (ycharos.com).](http://images.novusbio.com/fullsize/TDP-43-TARDBP-Antibody-3H8-Knockout-Validated-NBP1-92695-img0008.jpg)
![Immunohistochemistry: SHANK1 Antibody [NB300-167] - Synaptic distribution of Shank1/2 and somato-synaptic distribution of Shank3 in the mouse hippocampus, codistribution with VGLUT1, no codistribution with VGLUT2. 5x magnification of hippocampus. Immunofluorescence stainings of coronal sections from wild-type mice probed with Shank1-3 (white; green in merge) and VGLUT1 (white; red in merge) antibodies; green arrow points toward the intragranular mossy fibers where there is a prominent synaptic stain of Shank3; scale bar =300 um. Image collected and cropped by CiteAb from the following publication (//journal.frontiersin.org/Article/10.3389/fncel.2016.00106/abstract) licensed under a CC-BY license.](http://images.novusbio.com/fullsize/SHANK1-Antibody-Immunohistochemistry-NB300-167-img0012.jpg "Immunohistochemistry: SHANK1 Antibody [NB300-167] - Synaptic distribution of Shank1/2 and somato-synaptic distribution of Shank3 in the mouse hippocampus, codistribution with VGLUT1, no codistribution with VGLUT2. 5x magnification of hippocampus. Immunofluorescence stainings of coronal sections from wild-type mice probed with Shank1-3 (white; green in merge) and VGLUT1 (white; red in merge) antibodies; green arrow points toward the intragranular mossy fibers where there is a prominent synaptic stain of Shank3; scale bar =300 um. Image collected and cropped by CiteAb from the following publication (//journal.frontiersin.org/Article/10.3389/fncel.2016.00106/abstract) licensed under a CC-BY license.")
![Immunohistochemistry: SHANK1 Antibody [NB300-167] - Mouse retina using NB300-167.](http://images.novusbio.com/fullsize/SHANK1-Antibody-Immunohistochemistry-NB300-167-img0005.jpg)
![Western Blot: SHANK1 Antibody [NB300-167] - Shank1a in rat brain lysate using NB300-167 at 1:500 dilution.](http://images.novusbio.com/fullsize/SHANK1-Antibody-Western-Blot-NB300-167-img0007.jpg)
![Immunohistochemistry: SHANK1 Antibody [NB300-167] - Synaptic distribution of Shank1/2 and somato-synaptic distribution of Shank3 in the mouse hippocampus, codistribution with VGLUT1, no codistribution with VGLUT2. Immunofluorescence stainings of coronal sections from wild-type mice probed with Shank1-3 (white; green in merge) and VGLUT2 (white; red in merge) antibodies; green arrow points toward the intragranular mossy fibers where there is a prominent synaptic stain of Shank3. Red arrow points toward the VGLUT2-band of the DG; scale bar = 300 um. Image collected and cropped by CiteAb from the following publication (//journal.frontiersin.org/Article/10.3389/fncel.2016.00106/abstract) licensed under a CC-BY license.](http://images.novusbio.com/fullsize/SHANK1-Antibody-Immunohistochemistry-NB300-167-img0013.jpg)
![Immunocytochemistry/Immunofluorescence: SHANK1 Antibody [NB300-167] - An ASD biometal profile affects cell health and synapse numbers in vitro. Immunocytochemistry of hippocampal neurons DIV 14 grown under control, ASD1, and ASD2 conditions. The fluorescence intensity of Shank positive puncta was measured using antibodies specific for Shank1, Shank2, and Shank3. Exemplary images (upper panel) and quantification of average puncta signal intensity of 10 cells per condition (lower panel). Merged images show additional DAPI staining of the nucleus. Neurons grown under ASD1 conditions show a significant decrease of synaptic Shank proteins, while neurons under ASD2 conditions did not show a reduction. Image collected and cropped by CiteAb from the following publication (//www.hindawi.com/journals/np/2015/985083/), licensed under a CC-BY license.](http://images.novusbio.com/fullsize/SHANK1-Antibody-Immunocytochemistry-Immunofluorescence-NB300-167-img0010.jpg)
![Immunohistochemistry: SHANK1 Antibody [NB300-167] - Colocalization of Shank puncta with VGLUT1 puncta in the intragranular mossy fibers and the stratum moleculare of the dentate gyrus. Confocal immunofluorescence stainings of coronal sections from wild-type mice probed with the Shank1 (white; green in merge) and VGLUT1 (white; red in merge) antibodies. The upper rows (large squares) show the enlarged region (3 = SM; 2 = SG; 1 = PL; scale bar = 100 um), the bottom rows (small rectangles) show further enlargements (indicated in upper row by white rectangles) in the PL (1, top row) and SM (3, bottom row) (scale bar = 5 um). Image collected and cropped by CiteAb from the following publication (//journal.frontiersin.org/Article/10.3389/fncel.2016.00106/abstract) licensed under a CC-BY license.](http://images.novusbio.com/fullsize/SHANK1-Antibody-Immunohistochemistry-NB300-167-img0014.jpg)
![Immunocytochemistry/Immunofluorescence: SHANK1 Antibody [NB300-167] - Colocalization of Shank immunoreactivity with VGLUT1 in the stratum radiatum/stratum lucidum of the CA3 region. confocal immunofluorescence stainings of coronal sections from wild-type mice probed with the Shank1 (white; green in merge) and VGLUT1 (white;red in merge) antibodies. The upper row (large squares) shows the enlarged region (3 = SO; 2 = SP; 1 = SR; scale bar = 100 um), the bottom row (small rectangles) shows a further enlargement (indicated in upper row by white rectangle) in the SR (scale bar = 5 um). Image collected and cropped by CiteAb from the following publication (//journal.frontiersin.org/Article/10.3389/fncel.2016.00106/abstract) licensed under a CC-BY license.](http://images.novusbio.com/fullsize/SHANK1-Antibody-Immunocytochemistry-Immunofluorescence-NB300-167-img0011.jpg)
![Immunohistochemistry: SHANK1 Antibody [NB300-167] - Colocalization of Shank puncta with VGLUT1 puncta in the stratum radiatum of the CA1. confocal immunofluorescence stainings of coronal sections from wild-type mice probed with the Shank1 (white; green in merge) and VGLUT1 (white; red in merge) antibodies. The upper row (large squares) shows the enlarged region (3 = SO; 2 = SP; 1 = SR; scale bar = 100 um), the bottom row (small rectangles) shows a further enlargement (indicated in upper row by white rectangle) in the SR (scale bar = 5 um). Image collected and cropped by CiteAb from the following publication (//journal.frontiersin.org/Article/10.3389/fncel.2016.00106/abstract) licensed under a CC-BY license.](http://images.novusbio.com/fullsize/SHANK1-Antibody-Immunohistochemistry-NB300-167-img0017.jpg)
![Immunohistochemistry: SHANK1 Antibody [NB300-167] - Retinal tissue using NB300-167 at 1:800 dilution. Images are 2048 X 2048, 12 bit, collected with a 40X water objective, 10 stacks 0.55 um per stack.](http://images.novusbio.com/fullsize/SHANK1-Antibody-Immunohistochemistry-NB300-167-img0006.jpg)
![Immunocytochemistry/ Immunofluorescence: SHANK1 Antibody - BSA Free [NB300-167] - Synaptic distribution of Shank1/2 & somato-synaptic distribution of Shank3 in the mouse hippocampus, codistribution with VGLUT1, no codistribution with VGLUT2. Top box: 5x magnification of hippocampus. Immunofluorescence stainings of coronal sections from wild-type mice probed with Shank1-3 (white; green in merge) & VGLUT1 (white; red in merge) antibodies; green arrow points toward the intragranular mossy fibers where there is a prominent synaptic stain of Shank3; scale bar = 300 μm. Bottom box: same stainings as top box but with the VGLUT2 antibody (white; red in merge). Red arrow points toward the VGLUT2-band of the DG; scale bar = 300 μm. Image collected & cropped by CiteAb from the following publication (//journal.frontiersin.org/Article/10.3389/fncel.2016.00106/abstract), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb300-167_rabbit-polyclonal-shank1-antibody-310202415291988.jpg)
![Immunocytochemistry/ Immunofluorescence: SHANK1 Antibody - BSA Free [NB300-167] - Synaptic distribution of Shank1/2 & somato-synaptic distribution of Shank3 in the mouse hippocampus, codistribution with VGLUT1, no codistribution with VGLUT2. Top box: 5x magnification of hippocampus. Immunofluorescence stainings of coronal sections from wild-type mice probed with Shank1-3 (white; green in merge) & VGLUT1 (white; red in merge) antibodies; green arrow points toward the intragranular mossy fibers where there is a prominent synaptic stain of Shank3; scale bar = 300 μm. Bottom box: same stainings as top box but with the VGLUT2 antibody (white; red in merge). Red arrow points toward the VGLUT2-band of the DG; scale bar = 300 μm. Image collected & cropped by CiteAb from the following publication (//journal.frontiersin.org/Article/10.3389/fncel.2016.00106/abstract), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb300-167_rabbit-polyclonal-shank1-antibody-310202415304214.jpg)
![Immunocytochemistry/ Immunofluorescence: SHANK1 Antibody - BSA Free [NB300-167] - No colocalization of Shank puncta with VGLUT2 puncta in the VGLUT2-band nor in the intragranular mossy fibers of the dentate gyrus. Top box: Schematic overview of hippocampus with enlarged region (yellow square; here: dentate Gyrus = DG, containing stratum granulare = SG, stratum moleculare = SM, & polymorphic layer = PL; I. indicates uppermost row/figure in bottom box). Bottom box: confocal immunofluorescence stainings of coronal sections from wild-type mice probed with the Shank1-3 (white; green in merge), & VGLUT2 (white; red in merge) antibodies. The upper rows (large squares) show the enlarged region (3 = SM; 2 = SG; 1 = PL; scale bar = 100 μm), the bottom rows (small rectangles) show further enlargements (indicated in upper row by white rectangles) in the outer part of the SG (2, top row) & in the PL (1, bottom row) (scale bar = 5 μm). Red arrows indicate VGLUT2-band. Image collected & cropped by CiteAb from the following publication (//journal.frontiersin.org/Article/10.3389/fncel.2016.00106/abstract), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb300-167_rabbit-polyclonal-shank1-antibody-310202416205165.jpg)
![Immunocytochemistry/ Immunofluorescence: SHANK1 Antibody - BSA Free [NB300-167] - Colocalization of Shank puncta with VGLUT1 puncta in the stratum radiatum of the CA1. Top box: Schematic overview of hippocampus with enlarged region (yellow square; here: CA1 containing stratum pyramidale = SP, stratum oriens = SO & stratum radiatum = SR; I./II./III. indicates uppermost/middle/bottom figure in bottom box). Bottom box: confocal immunofluorescence stainings of coronal sections from wild-type mice probed with the Shank1-3 (white; green in merge) & VGLUT1 (white; red in merge) antibodies. The upper row (large squares) shows the enlarged region (3 = SO; 2 = SP; 1 = SR; scale bar = 100 μm), the bottom row (small rectangles) shows a further enlargement (indicated in upper row by white rectangle) in the SR (scale bar = 5 μm). Image collected & cropped by CiteAb from the following publication (//journal.frontiersin.org/Article/10.3389/fncel.2016.00106/abstract), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb300-167_rabbit-polyclonal-shank1-antibody-310202416212374.jpg)
![Immunocytochemistry/ Immunofluorescence: SHANK1 Antibody - BSA Free [NB300-167] - Colocalization of Shank puncta with VGLUT1 puncta in the intragranular mossy fibers & the stratum moleculare of the dentate gyrus. Top box: Schematic overview of hippocampus with enlarged region (yellow square; here: dentate Gyrus = DG, containing stratum granulare = SG, stratum moleculare = SM, & polymorphic layer = PL; I. indicates uppermost row/figure in bottom box). Bottom box: confocal immunofluorescence stainings of coronal sections from wild-type mice probed with the Shank1-3 (white; green in merge) & VGLUT1 (white; red in merge) antibodies. The upper rows (large squares) show the enlarged region (3 = SM; 2 = SG; 1 = PL; scale bar = 100 μm), the bottom rows (small rectangles) show further enlargements (indicated in upper row by white rectangles) in the PL (1, top row) & SM (3, bottom row) (scale bar = 5 μm). Image collected & cropped by CiteAb from the following publication (//journal.frontiersin.org/Article/10.3389/fncel.2016.00106/abstract), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb300-167_rabbit-polyclonal-shank1-antibody-310202416203722.jpg)
![Immunocytochemistry/ Immunofluorescence: SHANK1 Antibody - BSA Free [NB300-167] - No colocalization of Shank immunoreactivity with VGLUT2 puncta in the VGLUT2-band of the stratum pyramidale nor in the mossy fibers of the CA3. Top box: Schematic overview of hippocampus with enlarged region (yellow square; here: CA3 containing stratum pyramidale = SP, stratum oriens = SO & stratum radiatum = SR). Bottom box: confocal immunofluorescence stainings of coronal sections from wild-type mice probed with the Shank1-3 (white; green in merge) & VGLUT2 (white; red in merge) antibodies. The upper row (large squares) shows the enlarged region (3 = SO; 2 = SP; 1 = SR; scale bar = 100 μm), the bottom row (small rectangles) shows further enlargements (indicated in upper row by white rectangles) in the lateral part of the SP (2, top row) & the SR (1, bottom row) (scale bar = 5 μm). Red arrows indicate VGLUT2-band. Image collected & cropped by CiteAb from the following publication (//journal.frontiersin.org/Article/10.3389/fncel.2016.00106/abstract), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb300-167_rabbit-polyclonal-shank1-antibody-310202416205156.jpg)
![Immunocytochemistry/ Immunofluorescence: SHANK1 Antibody - BSA Free [NB300-167] - Colocalization of Shank immunoreactivity with VGLUT1 in the stratum radiatum/stratum lucidum of the CA3 region. Top box: Schematic overview of hippocampus with enlarged region (yellow square; here: CA3 containing stratum pyramidale = SP, stratum oriens = SO & stratum radiatum = SR). Bottom box: confocal immunofluorescence stainings of coronal sections from wild-type mice probed with the Shank1-3 (white; green in merge) & VGLUT1 (white; red in merge) antibodies. The upper row (large squares) shows the enlarged region (3 = SO; 2 = SP; 1 = SR; scale bar = 100 μm), the bottom row (small rectangles) shows a further enlargement (indicated in upper row by white rectangle) in the SR (scale bar = 5 μm). Image collected & cropped by CiteAb from the following publication (//journal.frontiersin.org/Article/10.3389/fncel.2016.00106/abstract), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb300-167_rabbit-polyclonal-shank1-antibody-310202416203718.jpg)
![Western Blot: GABA-A R gamma 2 Antibody [NB300-151] - 10 ug of rat brain lysate showing immunolabeling of the ~45-47 kDa GABA - A R, g2-subunit.](http://images.novusbio.com/fullsize/GABA-A-R-gamma-2-Antibody-Western-Blot-NB300-151-img0007.jpg "Western Blot: GABA-A R gamma 2 Antibody [NB300-151] - 10 ug of rat brain lysate showing immunolabeling of the ~45-47 kDa GABA - A R, g2-subunit.")
![Immunohistochemistry-Paraffin: GABA-A R gamma 2 Antibody [NB300-151] - Rat cerebellum.](http://images.novusbio.com/fullsize/GABA-A-R-gamma-2-Antibody-Immunohistochemistry-Paraffin-NB300-151-img0005.jpg)
![Western Blot: GABA-A R gamma 2 Antibody [NB300-151] - 10 ug of rat hippocampal lysate showing immunolabeling of the ~46k gamma2-subunit of the GABA-A R.](http://images.novusbio.com/fullsize/GABA-A-R-gamma-2-Antibody-Western-Blot-NB300-151-img0006.jpg)