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Recombinant Human Matrix metalloproteinase-14
Synonyms MMP-X1, MT-MMP 1, MT1-MMP
Accession P50281
GeneID 4323
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.
Biological Activity Test in Process.
Physical Appearance Sterile colorless liquid.
Formulation Supplied as a 0.2 μm filtered solution in 20 mM Tris-HCl, pH 7.4, 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.
Usage This material is offered by Shanghai PrimeGene Bio-Tech for research, laboratory or further evaluation purposes. NOT FOR HUMAN USE.
Background As the first member of membrane type (MT) MMPs, MMP-14, also known as MT1-MMP, plays an important role in extracellular matrix (ECM) remodeling by being able to degrade type I collagen, activate pro-MMP-2 and process cell adhesion molecules such as CD44 and integrin alpha V. MMP-14 is therefore a key enzyme in many physiological and pathological processes such as angiogenesis and tumor invasion. Structurally, MMP-14 consists of the following domains: a pro domain containing the furin cleavage site, a catalytic domain containing the zinc-binding site, a hinge region, a hemopexin-like domain, a transmembrane domain, and a cytoplamasic tail. Recombinant Human MMP-14 consists of the pro and catalytic domains, which can be activated by treatment with furin as described in Activity Assay Protocol.
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