Belongs to the peptidase M10A family.Contains 4 hemopexin-like domains.
Secreted > extracellular space > extracellular matrix.
The conserved cysteine present in the cysteine-switch motif binds the catalytic zinc ion, thus inhibiting the enzyme. The dissociation of the cysteine from the zinc ion upon the activation-peptide release activates the enzyme.
pH: 8.50Constituents: 10% DMSO, 0.6% Tris, 0.15% EDTA, 0.1% BSA
Shipped at 4°C. Upon delivery aliquot and store at -80℃. Avoid freeze / thaw cycles. pH: 8.50Constituents: 10% DMSO, 0.6% Tris, 0.15% EDTA, 0.1% BSA
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 MMPs are secreted as inactive proproteins which are activated when cleaved by extracellular proteinases. This gene encodes an enzyme which degrades fibronectin, laminin, collagens III, IV, IX, and X, and cartilage proteoglycans. The enzyme is thought to be involved in wound repair, progression of atherosclerosis, and tumor initiation. The gene is part of a cluster of MMP genes which localize to chromosome 11q22.3. [provided by RefSeq, Jul 2008]
calcium ion binding; metalloendopeptidase activity; zinc ion binding;
MMP3; matrix metallopeptidase 3 (stromelysin 1, progelatinase); SL-1; STMY; STR1; CHDS6; MMP-3; STMY1; stromelysin-1; transin-1; proteoglycanase; matrix metalloproteinase-3; matrix metalloproteinase 3 (stromelysin 1, progelatinase);