Sigma-Aldrich MMP Substrate. ≥95% (HPLC), lyophilized. 1 mg

MCA-Lys-Pro-Leu-Gly-Leu-DNP-Dpa-Ala-Arg-NH2

Matrix Metalloproteases (MMPs) belongs to the zinc metalloprotease family M10.[1] They are zinc-dependent, calcium-containing hydrolases.[2]

Matrix Metalloproteases (MMPs) are involved in extracellular matrix (ECM) degradation.[1] MMPs regulate cellular and disease processes. They are implicated in processes such as cell proliferation, migration, differentiation, angiogenesis, anti-inflammatory response, vasoconstriction, apoptosis and host defense. Dysregulation of MMP is associated with arthritis, ulcers, encephalomyelitis and cancer.[2]

The peptide MCA-Lys-Pro-Leu-Gly-Leu-DNP-Dpa-Ala-Arg-NH2, or FS-6, is a fluorogenic substrate for several matrix metalloproteinases (MMPs). FS-6 is a water-soluble, modified form of the well-established MMP substrate FS-1, where a lysine residue has been added to the N-terminus of FS-1. The resulting FS-6 has been reported to give a peptide with improved kinetic properties for several MMPs, including MMP-1, MMP-8, MMP-13, and MMP-14, compared to FS-1. This MMP substrate has also been described as a particularly useful substrate for the zinc metalloproteinase tumor necrosis factor-α converting enzyme (TACE or ADAM-17). FS-6 can be used to measure metalloproteinase activity in tissue culture conditions, for example, on the surface of viable cells in situ.[3][4]