Journal: Journal of experimental & clinical cancer research : CR
Article Title: Blockade of αvβ6 and αvβ8 integrins with a chromogranin A-derived peptide inhibits TGFβ activation in tumors and suppresses tumor growth.
doi: 10.1186/s13046-025-03352-4
Figure Lengend Snippet: Fig. 2 Binding of 5a-HSA and peptide 5a to recombinant human αvβ6 and αvβ8 (competitive and direct binding assays). Schematic representation of the assays (left panels) and dose-response curves (middle-right panels). A) Direct binding of 5a-HSA to αvβ6- or αvβ8-coated microtiter plates as detected with an anti-HSA rabbit polyclonal antibody and HRP-labeled goat anti-rabbit antibody. B) Competitive binding of 5a-HSA and isoDGR-HRP conjugate to αvβ6- or αvβ8-coated microtiter plates. C) Competitive binding of peptide 5a (upper panels) or 5a-HSA (lower panels) and biotinylated-αvβ6 or -αvβ8 integrins to latent TGFβ1-coated microtiter plates, as detected with HRP-labeled streptavidin (STV-HRP). Dots, mean ± SE of technical duplicates. Inhibition constant (Ki) or dissociation constant (Kd) are also indicated in each panel
Article Snippet: The competitive integrin binding assay 3 was performed as follows: ninety-six-well microtiter plates (Greiner Bio-One, cat. #675061) were coated with or without human recombinant latent TGFβ1 (Acro Biosystems, cat. TG1-H524x) in 50 mM sodium carbonate buffer, pH 9.5, containing 1 mM calcium chloride, 1 mM manganese chloride (2 μg/ml, 50 μl/well overnight at 4 °C).
Techniques: Binding Assay, Recombinant, Labeling, Inhibition