| Protein Description: | Matrix metalloproteinases are a family of zinc and calcium dependent endopeptidases with the combined ability to degrade all the components of the extracellular matrix. MMP-2 (gelatinase A), a type IV collagenase, can degrade a broad range of substrates including type IV, V, VII and X collagens as well as elastin and fibronectin. It is believed to act synergistically with interstitial collagenase (MMP-1) in the degradation of fibrillar collagens as it degrades their denatured gelatin forms. MMP-2 has been shown to be associated with many connective tissue cells as well as neutrophils, macrophages and monocytes. Structurally, MMP-2 may be divided into several distinct domains: a pro-domain which is cleaved upon activation; a catalytic domain containing the zinc binding site; a fibronectin-like domain thought to play a role in substrate targeting; and a carboxyl terminal (hemopexin-like) domain containing 2 N-linked glycosylation sites. |
| Endotoxin: | < 0.1 EU/μg of the protein by LAL method. |
| Purity: | ≥ 90 % as determined by SDS-PAGE. |
| Formulation: | Lyophilized from a 0.2 μm filtered solution of 150 mM NaCl, 5 mM CaCl2, 50 mM Tris, pH 7.5..Contact us for customized product form or formulation. |
| Gene ID: | 4313 |
