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-9 (gelatinase B) can degrade a broad range of substrates including gelatin, collagen types IV and V, elastin and proteoglycan core protein. 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-9 is produced by keratinocytes, monocytes, macrophages and PMN leukocytes. MMP-9 is present in most cases of inflammatory responses. Structurally, MMP-9 maybe be divided into five distinct domains: a pro-domain which is cleaved upon activation, a gelatin-binding domain consisting of three contiguous fibronectin type II units, a catalytic domain containing the zinc binding site, a proline-rich linker region, and a carboxyl terminal hemopexin-like domain.
Recombinant protein corresponding to Ala20-Asp707 (Gln279Arg) from human MMP-9, expressed in CHO cells.
Biological Activity:Measured by its ability to cleave the fluorogenic peptide substrate, Mca-PLGL-Dpa-AR-NH2.
Specific Activity: >1,300 pmol/min/ug, as measured under the described conditions.
Storage and Stability:Aliquot to avoid repeated freezing and thawing and store at -70°C. Aliquots are stable for 6 months after receipt. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap.
仕様
Size：10ug
Source Antigen：Recombinant, CHO cells
Grade：Purified
Purity：≥90%, by SDS-PAGE under reducing conditions and visualized by silver stain. Endotoxin: ≤1.1EU/ug.
Form：Supplied as a liquid in 50mM Tris-HCl, 150mM sodium chloride, 10mM calcium chloride, 0.05% Brij 35.
