Boc-Ile-Glu-Gly-Arg-AMC (IEGR-AMC) is a specific, highly fluorogenic substrate for clotting enzyme factor Xa (coagulation factor Xa) and is also hydrolyzed by acrosin from the ascidian Halocynthia roretzi.
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
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).
Ac-RGK(Ac)-AMC, fluorogenic substrate for assaying histone deacetylase (HDAC) activity in a two-step enzymatic reaction. The assay consists of the initial lysine deacetylation by HDAC followed by the release of the fluorescent group by trypsin.
Ac-Ile-Glu-Thr-Asp-pNA is a caspase-8 substrate that undergoes enzymatic binding and cleavage specifically at the Ile-Glu-Thr-Asp (IETD) peptide sequence. This cleavage results in the release of p-nitroalinide, which can be quantitatively measured using colorimetric detection at 405 nm. This measure serves as an indicator of caspase-8 enzyme activity.
Z-Gly-Gly-Arg-AMC is a specific fluorogenic substrate utilized for assessing thrombin generation in Platelet-Rich Plasma (PRP) and Platelet-Poor Plasma (PPP), with a particular focus on thrombin activity.
Boc-Gly-Gly-Phe-Gly-OH TFA is a self-assembly of N-protected and C-protected tetrapeptides and is a protease cleaved connector for antibody-drug binding (ADC).
Z-Gly-Gly-Arg-AMC acetate is a thrombase-specific fluorescent matrix used to detect thrombin production in platelet-rich plasma (PRP) and poor platelet plasma (PPP).
Tos-Gly-Pro-Arg-ANBA-IPA, a chromogenic peptide substrate, is utilized for the rapid and specific photometric assay of recombinant hirudin (r-hirudin).
Arg-Gly-Asp-Cys TFA serves as the binding motif through which fibronectin interacts with cell adhesion molecules. This compound has the ability to hinder platelet aggregation and fibrinogen binding.