Matrix metallopeptidase 9 (MMP-9), also known as 92 kDa type IV collagenase, 92 kDa gelatinase or gelatinase B, is the mostly studied MMP, due to its fundamental role in cancer biology, autoimmune disease, and other conditions. This enzyme degrades various substrates including gelatin, collagen types IV and V, and elastin. MMP-9 is structurally a multi-domain metalloenzyme, composed of a prodomain, a catalytic domain, a gelatin binding domain, a metal-binding domain, and a carboxyl terminal hemopexin like domain. This active human MMP-9 is composed of the catalytic domain, a gelatin binding domain, and a metal binding domain (AA 107-457). The protein was expressed in E.coli and purified and refolded using proprietary techniques. MW: 39 kDa
Size
500 Units
Concentration
n/a
Applications
RUO
Other Names
Matrix Metalloproteinase-9, Gelatinase B, 92 kDa Type IV Collagenase, MMP9, CLG4B, GELB, MANDP2