Cathepsin B Substrate

Z-Arg-Arg-AMC hydrochloride is a highly selective fluorescent Cathepsin B substrate. Z-Arg-Arg-AMC hydrochloride can be hydrolyzed by Cathepsin B to produce a fluorescent product for enzyme activity detection.

Z-Val-Val-Arg-AMC is a fluorescent peptide substrate that can be used to test the activity of cathepsins. Z-Val-Val-Arg-AMC exhibits preference for Cathepsin S. Z-Val-Val-Arg-AMC undergoes hydrolysis catalyzed by cathepsin to release the AMC fluorophore, thereby enabling fluorescence-based quantitative assessment of the target enzyme activity.

Z-Nle-Lys-Arg-AMC acetate is a selective Fluorescent peptide substrate for Cathepsin B. Z-Nle-Lys-Arg-AMC acetate releases AMC upon cleavage, thereby enabling monitoring of proteolytic activity over an acidic to neutral pH range.

diABZI-V/C-Mal is a STING agonist (with a STING EC₅₀ of 314 nM in TH1 dual reporter cells) and a Cathepsin B substrate. diABZI-V/C-Mal activates STING, thereby triggering the IRF3 signaling pathway. diABZI-V/C-Mal is cleaved by Cathepsin B to regenerate diABZI-NH₂.

Ac-RR-AFC TFA is a Cathepsin B fluorogenic substrate (Ex=400 nm, Em=505 nm). Cathepsin B activity in cells lysates is determined by measuring cleavage of Ac-RR-AFC TFA and its cleavage occurs at the RR-AFC amide bond. Ac-RR-AFC TFA can be used for activity assays and mechanistic studies on cathepsin B.

Z-Nle-Lys-Arg-AMC is a selective Fluorescent peptide substrate for Cathepsin B. Z-Nle-Lys-Arg-AMC releases AMC upon cleavage, thereby enabling monitoring of proteolytic activity over an acidic to neutral pH range.