Human MMP-9 (20-707) Protein, His Tag (active enzyme, MALS verified)

Matrix metallopeptidase 9 (MMP-9) is also known as 92 kDa type IV collagenase, 92 kDa gelatinase or gelatinase B (GELB), CLG4B, is secreted from neutrophils, macrophages, and a number of transformed cells, and is the most complex family member in terms of domain structure and regulation of its activity. . Structurally, MMP9 maybe be divided into five distinct domains: a prodomain which is cleaved upon activation, a gelatinbinding domain consisting of three contiguous fibronectin type II units, a catalytic domain containing the zinc binding site, a prolinerich linker region, and a carboxyl terminal hemopexinlike domain. This enzyme degrades various substrates including gelatin, collagen types IV and V, and elastin. MMP9 is involved in a variety of autoimmune diseases such as systemic lupus erythematosus, rheumatoid arthritis, and multiple sclerosis, and be regarded as a potential therapeutic target.

This protein carries a polyhistidine tag at the C-terminus. The protein has a calculated MW of 78.2 kDa. The protein migrates as 85-95 kDa under reducing (R) condition (SDS-PAGE) due to glycosylation.

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