TLR3 Antibody

Western Blot: TLR3 Antibody [NB100-56571]

Western Blot: TLR3 Antibody [NB100-56571] - Analysis of TLR3 in mouse spleen tissue lysate using NB100-56571 at 2 ug/ml.

Immunohistochemistry: TLR3 Antibody [NB100-56571]

Immunohistochemistry: TLR3 Antibody [NB100-56571] - Pig lung poisoned through aspiration with gastric juice and organophosphate (dimethoate EC40) after 48 hours of IC ventilation. Image from verified customer review.

Flow Cytometry: TLR3 Antibody [NB100-56571]

Flow Cytometry: TLR3 Antibody [NB100-56571] - Intracellular flow analysis of TLR3 in Balb/c mouse splenocytes and mouse RAW cells using TLR3 antibody (red) and isotype control antibody (green) at 1 ug/10^6 cells.

Knockdown Validated: TLR3 Antibody [NB100-56571]

Knockdown Validated: TLR3 Antibody [NB100-56571] - siRNA was transfected at 50 nM for 48 hrs, and poly(I:C) was added at 100 ug/ml for 4 hrs before cell harvest. Negative control (NC) siRNA served as control. RNAiMAX transfection reagent was used in all the siRNA experiments. Panel shows the knockdown effects of siRNAs. Image collected and cropped by CiteAb from the following publication (https://doi.wiley.com/10.1111/jcmm.13328) licensed under a CC-BY license.

Western Blot: TLR3 Antibody [NB100-56571] -

Western Blot: TLR3 Antibody [NB100-56571] - Myocardial infarction (MI) increased TLR3 expression & its physical association with Trif in mouse myocardium. Heart samples were taken from infarct area at 4 weeks after MI. (A) & (B) show mRNA & protein levels of TLR3 in sham & MI hearts. n = 4 mice/group. Data are means ± S.D. AP < 0.01 versus sham. (C) Representative immunohistochemistry images of heart sections stained for TLR3 (brown colour). An isotype IgG control was performed to verify the specificity of TLR3 reactivity. (D) Lysates of heart tissue were immunoprecipitated with anti‐TLR3 antibodies (IP: TLR3), followed by SDS–PAGE & immunoblotting (IB) with indicated antibodies. IP with isotype IgG (IP: IgG) was performed as a control to exclude the non‐specific binding of antibodies to cellular proteins. Green arrows indicate non‐specific bands. The association between TLR3 & Trif, but not MyD88, was detectable in sham myocardium & was increased in infarct myocardium. Image collected & cropped by CiteAb from the following publication (https://pubmed.ncbi.nlm.nih.gov/28945004), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: TLR3 Antibody [NB100-56571] -

Western Blot: TLR3 Antibody [NB100-56571] - Myocardial infarction (MI) increased TLR3 expression & its physical association with Trif in mouse myocardium. Heart samples were taken from infarct area at 4 weeks after MI. (A) & (B) show mRNA & protein levels of TLR3 in sham & MI hearts. n = 4 mice/group. Data are means ± S.D. AP < 0.01 versus sham. (C) Representative immunohistochemistry images of heart sections stained for TLR3 (brown colour). An isotype IgG control was performed to verify the specificity of TLR3 reactivity. (D) Lysates of heart tissue were immunoprecipitated with anti‐TLR3 antibodies (IP: TLR3), followed by SDS–PAGE & immunoblotting (IB) with indicated antibodies. IP with isotype IgG (IP: IgG) was performed as a control to exclude the non‐specific binding of antibodies to cellular proteins. Green arrows indicate non‐specific bands. The association between TLR3 & Trif, but not MyD88, was detectable in sham myocardium & was increased in infarct myocardium. Image collected & cropped by CiteAb from the following publication (https://pubmed.ncbi.nlm.nih.gov/28945004), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Immunohistochemistry: TLR3 Antibody [NB100-56571] -

Immunohistochemistry: TLR3 Antibody [NB100-56571] - Myocardial infarction (MI) increased TLR3 expression & its physical association with Trif in mouse myocardium. Heart samples were taken from infarct area at 4 weeks after MI. (A) & (B) show mRNA & protein levels of TLR3 in sham & MI hearts. n = 4 mice/group. Data are means ± S.D. AP < 0.01 versus sham. (C) Representative immunohistochemistry images of heart sections stained for TLR3 (brown colour). An isotype IgG control was performed to verify the specificity of TLR3 reactivity. (D) Lysates of heart tissue were immunoprecipitated with anti‐TLR3 antibodies (IP: TLR3), followed by SDS–PAGE & immunoblotting (IB) with indicated antibodies. IP with isotype IgG (IP: IgG) was performed as a control to exclude the non‐specific binding of antibodies to cellular proteins. Green arrows indicate non‐specific bands. The association between TLR3 & Trif, but not MyD88, was detectable in sham myocardium & was increased in infarct myocardium. Image collected & cropped by CiteAb from the following publication (https://pubmed.ncbi.nlm.nih.gov/28945004), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: TLR3 Antibody [NB100-56571] -

Western Blot: TLR3 Antibody [NB100-56571] - TLR3‐knockout (TLR3‐KO) attenuated cardiac autophagy induced by MI. The infarct & remote tissues were separately sampled from the left ventricle after 4 weeks of MI. Accordingly, anterior & posterior tissues of the left ventricle were sampled from sham hearts as controls. (A) Representative Western blot images & quantitative analyses of autophagy markers. n = 4–8/group. Quantitative data are fold changes of WT‐sham. aP < 0.05, AP < 0.01 versus respective WT‐sham; bP < 0.05, BP < 0.01 versus respective WT‐MI. (B) Representative electron microphotographs of ultrathin sections of resin‐embedded heart biopsies. Arrows indicate autophagic vacuoles. (C) Lysates of infarct tissue were immunoprecipitated (IP), followed by SDS–PAGE & immunoblotting (IB) with indicated antibodies. IP with isotype IgG served as a control. Green arrows indicate non‐specific bands. Representative images were taken from four independent experiments. Image collected & cropped by CiteAb from the following publication (https://pubmed.ncbi.nlm.nih.gov/28945004), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Western Blot: TLR3 Antibody [NB100-56571] -

Western Blot: TLR3 Antibody [NB100-56571] - A TLR3 agonist polyinosinic‐polycytidylic acid (poly(I:C)) induced autophagy in cultured cardiomyocytes through a TRIF‐dependent pathway. (A) Poly(I:C) increased autophagy markers in cultured H9c2 rat ventricular cells. (B) Poly(I:C) stimulated autophagosome formation but did not affect autophagic flux. Primary cultured neonatal rat ventricular myocytes (NRVMs) were transfected with a tandem mRFP‐GFP‐LC3 adenovirus for 24 hrs, followed by treatment with poly(I:C) (100 μg/ml, 4 hrs). Autophagosomes & autolysosomes were, respectively, visualized as yellow‐ & red‐only punctas under a confocal microscope. (C) An autophagic flux inhibitor chloroquine (CQ) induced accumulations of LC3‐II & p62/SQSTM1 proteins in H9c2 myocytes receiving poly(I:C) (100 μg/ml, 4 hrs). CQ was applied at 10 μM, immediately prior to poly(I:C). (D) Effects of indicated siRNA on poly(I:C)‐induced changes in autophagy markers in NRVMs. All the siRNAs were transfected at 50 nM for 48 hrs, & poly(I:C) was added at 100 μg/ml for 4 hrs before cell harvest. Negative control (NC) siRNA served as control. RNAiMAX transfection reagent was used in all the siRNA experiments. The upper panel shows the knockdown effects of siRNAs, & the lower panel shows representative Western blot images (presented from four independent experiments) & densitometry quantitative data (normalized into ‘fold of vehicle group’). All quantitative data are expressed as means ± S.D. aP < 0.05, AP < 0.01 versus vehicle; bP < 0.05, BP < 0.01 versus poly(I:C). Image collected & cropped by CiteAb from the following publication (https://pubmed.ncbi.nlm.nih.gov/28945004), licensed under a CC-BY license. Not internally tested by Novus Biologicals.