| Source: |
Escherichia coli |
| Molecular Weight: |
Approximately 29.6 kDa, a single non-glycosylated polypeptide chain containing 264 amino acids. |
| AA Sequence: |
ALASLGSAQS SSFSPEAWLQ QYGYLPPGDL RTHTQRSPQS LSAAIAAMQK FYGLQVTGKA DADTMKAMRR PRCGVPDKFG AEIKANVRRK RYAIQGLKWQ HNEITFCIQN YTPKVGEYAT YEAIRKAFRV WESATPLRFR EVPYAYIREG HEKQADIMIF FAEGFHGDST PFDGEGGFLA HAYFPGPNIG GDTHFDSAEP WTVRNEDLNG NDIFLVAVHE LGHALGLEHS SDPSAIMAPF YQWMDTENFV LPDDDRRGIQ QLYG |
| Purity: |
> 95% by SDS-PAGE and HPLC analyses. |
| Physical Appearance: |
Sterile colorless liquid. |
| Formulation: |
Supplied as a 0.2 μm filtered solution in 20 mM Tris-HCl, pH7.4, 300 mM NaCl, 3 mM CaCl2,10 μM ZnCl2, with 30% glycerol. |
| Endotoxin: |
Less than 1 EU/µg of rHuMMP-14 as determined by LAL method. |
| Stability & Storage: |
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.- 6 months from date of receipt, -20 to -70°C as supplied.- 3 months, -20 to -70°C under sterile conditions after opening. |
| Synonyms: |
MMP-X1, MT-MMP 1, MT1-MMP |
| Background: |
MMP-14, also known as MT1-MMP, is the inaugural member of the membrane-type (MT) matrix metalloproteinases (MMPs), crucial for extracellular matrix (ECM) remodeling. It effectively degrades type I collagen, activates pro-MMP-2, and processes cell adhesion molecules like CD44 and integrin alpha V. MMP-14 plays pivotal roles in various physiological and pathological processes, including angiogenesis and tumor invasion. Structurally, MMP-14 comprises distinct domains: a prodomain housing the furin cleavage site, a catalytic domain with a zinc-binding site, a hinge region, a hemopexin-like domain, a transmembrane domain, and a cytoplasmic tail. Recombinant Human MMP-14 consists of the pro and catalytic domains, activatable via furin treatment as outlined in the activity assay protocol. |
