Matrix Metalloproteinase 9, Recombinant, Human (MMP-9, Collagenase 4, Gelatinase B)
Biozol Catalog Number:
USB-M2425-22B
Supplier Catalog Number:
M2425-22B
Alternative Catalog Number:
USB-M2425-22B-10
Manufacturer:
US Biological
Category:
Molekularbiologie
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. Molecular Weight: ~77kD, 93kD (reducing conditions) N-Terminal Sequence Analysis: Ala20 Structure/Form: Pro form 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 -70C. 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.
