Species : |
Human |
Source : |
E.coli |
Tag : |
Non |
Protein Length : |
278-470 a.a. |
Description : |
Proteins of the matrix metalloproteinase (MMP) family are involved in the breakdown of extracellular matrix in normal physiological processes, such as embryonic development, reproduction, and tissue remodeling, as well as in disease processes, such as arthritis and metastasis. Most MMP''s are secreted as inactive proproteins which are activated when cleaved by extracellular proteinases. It is thought that the protein encoded by this gene is cleaved at both ends to yield the active enzyme, but this processing has not been fully described. The enzyme degrades soluble and insoluble elastin. It may play a role in aneurysm formation and studies in mice suggest a role in the development of emphysema. The gene is part of a cluster of MMP genes which localize to chromosome 11q22.3. |
Form : |
Solution in Tris 50mM pH 7.2, CaCl2 10mM, ZnCl2 0.1mM, NaCl 300mM. The concentration is calculated from the absorbance at 280nm (ε280 = 46995 M-1 cm-1). |
Molecular Mass : |
23.2 kDa |
AA Sequence : |
M-EPA LCDPNLSFDA VTTVGNKIFF FKDRFFWLKV SERPKTSVNL ISSLWPTLPS GIEAAYEIEA RNQVFLFKDD KYWLISNLRP EPNYPKSIHS FGFPNFVKKI DAAVFNPRFY RTYFFVDNQY WRYDERRQMM DPGYPKLITK NFQGIGPKID AVFYSKNKYY YFFQGSNQFE YDFLLQRITK TLKSNSWFGC |
Purity : |
>95% by SDS-PAGE. The protein was observed as a single band migrating at a molecular weight between 20 and 30kDa. |
Storage : |
-20°C. After initial defrost, aliquot product into individual tubes and refreeze at -20°C. Avoid repeated freeze/defrost cycles. |
Concentration : |
200μM |