Arg-Gly-Asp-Ser is an integrin-binding sequence that inhibits integrin receptor function. It decreases systemic inflammation via inhibition of collagen-triggered activation of leukocytes and attenuates expression of inflammatory cytokines, MMP-9, and iNOS
H-D-Phe-Pip-Arg-pNA hydrochloride, a chromogenic substrate, mimics the N-terminal segment of the A alpha chain of fibrinogen, the native substrate of thrombin. It displays specificity towards thrombin and is employed for quantifying antithrombin-heparin cofactor (AT-III). The utilization of H-D-Phe-Pip-Arg-pNA hydrochloride in the AT-III assay enables a sensitive, accurate, and straightforward measurement process.
N-CBZ-Phe-Arg-AMC (Z-FR-AMC) is a substrate for serine proteases, including cathepsins, kallikrein, and plasmin. The substrate exhibits absorption emission at 330 390 nm (weak fluorescence), while the end product (AMC) shows absorption emission at 342 441 nm (strong fluorescence).
pGlu-Pro-Arg-MNA [N-(3-[2-Furyl]-acryloyl) - L - leucyl - glycyl - p - nitroanilide] is a chromogenic peptide substrate, specifically utilized for its role in biochemical assays.
H-D-Phe-Pip-Arg-pNA (S-2238) acetate is a chromogenic substrate designed based on the N-terminal fragment of the A alpha chain of fibrinogen, which is the physiological target of thrombin. As a specific indicator of thrombin activity, H-D-Phe-Pip-Arg-pNA acetate is utilized to quantify. This assay, utilizing H-D-Phe-Pip-Arg-pNA acetate, ensures high sensitivity, accuracy, and ease of execution.