Anti-MMP-9 from rabbit, purified by affinity chromatography

Matrix metalloproteinase-9 (UniProt: P50282; also known as EC: 3.4.24.35, MMP-9, 92 kDa gelatinase, 92 kDa type IV collagenase, Gelatinase B, GELB) is encoded by the Mmp9 gene (Gene ID: 81687) in rat. Matrix Metalloproteinases (MMPs) are a family of zinc metallo-endopeptidases secreted by cells and are responsible for much of the turnover of matrix components. MMP-9 is a secreted extracellular matrix metalloproteinase that exhibits a broad range of substrate specificity for native collagens including types IV, V, VII, and X as well as gelatin, proteoglycans, and elastin. It can exist as monomer or disulfide-linked homodimer. MMP-9 is synthesized with a signal peptide (aa 1-19) and a propeptide (aa 20-107) that are subsequently cleaved to produce active enzyme. Its activity can be inhibited by TIMP-1, which binds exclusively to pro-MMP-9 (Kd ~35 nM). MMP-9 contain a fibronectin-like domain inserted into the catalytic domain, presumably to enhance substrate binding. MMP-9 also contains a collagen type-V-like domain, which may enhance substrate binding and specificity. MMP-9 contains a cysteine switch (aa 98-105) where the conserved cysteine binds the catalytic zinc ion and inhibits its enzyme activity. The dissociation of the cysteine from the zinc ion upon the activation-peptide release activates the enzyme.