| Species : |
Human |
| Source : |
E.coli |
| Tag : |
Non |
| Protein Length : |
100-272 aa |
| 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. This gene encodes an enzyme which degrades fibronectin, laminin, collagens III, IV, IX, and X, and cartilage proteoglycans. The enzyme is thought to be involved in wound repair, progression of atherosclerosis, and tumor initiation. The gene is part of a cluster of MMP genes which localize to chromosome 11q22.3. |
| Bio-activity : |
> 30 U/μg. Activity described as U=100 pmol/min at 37 centigrade using a colorimetric assay with thiopeptolide Ac-Pro-Leu-Gly-[2- mercapto-4-methyl-pentanoyl]-Leu-Gly-OC2H5 (Biomol) as substrate. |
| Molecular Mass : |
19.5 kDa |
| AASequence : |
M-FRTFPGIPKWRKTHLTYRIVN130140150160170180YTPDLPKDAVDSAVEKALKVWEEVTPLTFSRLYEGEADIMISFAVREHGDDYPFDGPGNV190200210220230240LAHAYAPGPGINGDAHFDDDEQWTKDTTGTNLFLVAAHEIGHSLGLFHSANTEALMYPLY250260265HSLTDLTRFRLSQDDINGIQSLYGP |
| Purity : |
> 95% by SDS-PAGE. The protein is observed, in denaturing conditions, as a single band migrating at a molecular weight between 18.4 and 25.0 kDa. |
| Applications : |
Enzyme kinetic studies, cleavage of target substrates and screening of inhibitors. |
| Storage : |
At -80 centigrade. After initial defrost, aliquot the product into individual tubes and refreeze at -80 centigrade.
Avoid repeated freeze/thaw cycles. |
| Concentration : |
0.2 mg/mL. The concentration is calculated by the analysis of the absorbance at 280 nm (ε280 = 28420 M-1cm-1 calculated). |
| Shipping : |
Dry Ice |
| Storage Buffer : |
Tris 20 mM, pH 7.2, CaCl2 10 mM, ZnCl2 0.1 mM, NaCl 0.3 M, acetohydroxamic acid (AHA) 0.2 M. |