anti rage polyclonal goat igg  (Bio-Techne corporation)

Journal: PLoS ONE

Article Title: Oxidation by Neutrophils-Derived HOCl Increases Immunogenicity of Proteins by Converting Them into Ligands of Several Endocytic Receptors Involved in Antigen Uptake by Dendritic Cells and Macrophages

doi: 10.1371/journal.pone.0123293

Figure Lengend Snippet: ( A ) Uptake of fluorescently-labelled proteins by CHO cells transfected with human CD36 as compared to non-transfected cells. ( B ) Binding of anti-CD36 mAb and control mouse IgA to CD36-transfected and non-transfected CHO cells, determined by cellular ELISA. ( C ) Binding of rCD36 to plate-adsorbed proteins. ( D ) Effects of 10 or 100 μg/ml of indicated, soluble ligands on rCD36 binding to plate-adsorbed OVA-Cl. ( E ) Binding of polyclonal anti-mouse CD36 Ab and control goat IgG to BM-DC, splenic DC and PEM. A representative histogram of Ab binding to BM-DC is displayed on the left graph. ( F ) Binding of anti-mouse SR-A mAb and control rat IgG2b to BM-DC, splenic DC and PEM. A representative histogram of Ab binding to BM-DC is shown on the left graph. ( G ) Binding of SR-A present in lysates of PEM to plate-adsorbed proteins. ( H ) Effects of anti-SR-A 2F8 mAb and AcLDL on the uptake of fluorescently-labelled proteins by BM-DC. Shown are results of single experiments, each representative of at least 3 similar experiments performed (A-D, G, H) or averages +SEM from 4–6 independent experiments (E, F). The data were analysed with the unpaired (A-C, G) or one-sample (H) Student’s t-test or with ANOVA, followed by the Tukey-Kramer post-test (D). *, p < 0.05; ND, not done.

Article Snippet: Moreover, RAGE was expressed on the surface of neither BM-DC nor PEM, as indicated by the absence of specific binding of three different anti-RAGE Ab: rat anti-mouse RAGE mAb (clone 175440, R&D Systems) and two different goat anti-mouse RAGE polyclonal Ab (from R&D Systems and Santa Cruz Biotechnology) ( ).

Techniques: Transfection, Binding Assay, Enzyme-linked Immunosorbent Assay

Journal: PLoS ONE

Article Title: Oxidation by Neutrophils-Derived HOCl Increases Immunogenicity of Proteins by Converting Them into Ligands of Several Endocytic Receptors Involved in Antigen Uptake by Dendritic Cells and Macrophages

doi: 10.1371/journal.pone.0123293

Figure Lengend Snippet: ( A ) Binding of rLOX-1 to plate-adsorbed proteins. ( B , C ) Effects of 10 or 100 μg/ml of indicated, soluble ligands on rLOX-1 binding to plate-adsorbed OVA-Cl (B) or GA-BSA (C). ( D ) Binding of PE-conjugated anti-mouse LOX-1 mAb and control rat IgG2a to CBA BM-DC, determined by flow cytometry. ( E ) The effect of blocking goat anti-mouse LOX-1 polyclonal Ab, relative to normal goat IgG, on AF-OVA-Cl uptake by untreated and LPS-pre-treated CBA BM-DC. ( F ) LOX-1 expression on LPS-pre-treated CBA BM-DC. Results of single experiments are shown, repeated at least twice with similar results. The data were analysed by the Student’s t-test (A, E) or by ANOVA, followed by the Tukey-Kramer post-test (B, C). *, p < 0.05; NS, non-significant.

Article Snippet: Moreover, RAGE was expressed on the surface of neither BM-DC nor PEM, as indicated by the absence of specific binding of three different anti-RAGE Ab: rat anti-mouse RAGE mAb (clone 175440, R&D Systems) and two different goat anti-mouse RAGE polyclonal Ab (from R&D Systems and Santa Cruz Biotechnology) ( ).

Techniques: Binding Assay, Flow Cytometry, Blocking Assay, Expressing

Journal: PLoS ONE

Article Title: Oxidation by Neutrophils-Derived HOCl Increases Immunogenicity of Proteins by Converting Them into Ligands of Several Endocytic Receptors Involved in Antigen Uptake by Dendritic Cells and Macrophages

doi: 10.1371/journal.pone.0123293

Figure Lengend Snippet: ( A ) Binding of rSREC-I to proteins coated onto ELISA plates. ( B ) Effects of 10 or 100 μg/ml of indicated, soluble ligands on rSREC-I binding to plate-adsorbed AcLDL. ( C ) Binding of goat anti-mouse SREC-I Ab to untreated and LPS-pre-treated BM-DC. ( D ) Effects of polyclonal goat anti-mouse SREC-I Ab, relative to normal goat IgG, on the uptake of AF-AcLDL, AF-OVA-Cl and pHr-HSA-Cl by LPS-pre-treated, SR-A-deficient BM-DC. ( E ) Binding of rRAGE to plate-adsorbed proteins. ( F ) Effects of 10 or 100 μg/ml of indicated, soluble ligands on rRAGE binding to plate-adsorbed GA-BSA. The data were analysed by the Student’s t-test (A, D, E) or by ANOVA, followed by the Tukey-Kramer post-test (B, F). *, p < 0.05; NS, non-significant.

Article Snippet: Moreover, RAGE was expressed on the surface of neither BM-DC nor PEM, as indicated by the absence of specific binding of three different anti-RAGE Ab: rat anti-mouse RAGE mAb (clone 175440, R&D Systems) and two different goat anti-mouse RAGE polyclonal Ab (from R&D Systems and Santa Cruz Biotechnology) ( ).

Techniques: Binding Assay, Enzyme-linked Immunosorbent Assay