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RP-77535 is purified recombinant MMP-17 (catalytic domain) protein, expressed in E.coli. The polypeptide contains 186 amino acids of MT4-MMP linked to a C-terminal polyhistidine tag.
RP-77535 may be used as a control with corresponding anti-MMP-17 antibodies.
The specific activity of MT4-MMP catalytic domain is greater than 4 mU/mg. 1 U is the activity that hydrolyzes 1 µmol peptide (7-methoxycoumarin-4-yl) acetyl-Pro-Leu-Gly-Leu-(3- [2,4-dinitrophenyl]-L-2,3-diamino-propionyl)-Ala-Arg-NH2(Mca-Pro-Leu-Gly-Leu-Dpa-Ala-Arg) within 1 min. MT4-MMP is inhibited by tissue inhibitor of matrix metalloproteinase-1 (TIMP-1) and by chelators of divalent cations like EDTA.
Proteins of the matrix metalloproteinase (MMP) family are involved in the breakdown of extracellular matrix in normal physiological processes, such as embryonic development, reproduction, and tissue remodeling, as well as in disease processes, such as arthritis and metastasis. Most MMP's are secreted as inactive proproteins which are activated when cleaved by extracellular proteinases. The protein encoded by this gene is considered a member of the membrane-type MMP (MT-MMP) subfamily. However, this protein is unique among the MT-MMP's in that it is a GPI-anchored protein rather than a transmembrane protein. The protein activates MMP-2 by cleavage.
For Research Use Only. Not for use in diagnostic procedures. Not for resale without express authorization.
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