• Product NameRecombinant Human Matrix metalloproteinase-14
• Host SpeciesEscherichia coli.
• Purification> 95 % by SDS-PAGE and HPLC analyses.
• Biological ActivityTest in Process.
• EndotoxinLess than 1 EU/ug of rHuMMP-14 as determined by LAL method.
• Alternative Names    MMP-X1, MT-MMP 1, MT1-MMP
• UniprotP50281
• Gene ID4323
• Calculated MW Approximately 29.6 kDa, a single non-glycosylated polypeptide chain containing 264 amino acids.
• Target 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
• 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.
• 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.

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.

• Flow Cytometry (FCM) General Protocol
• Immunofluorescence(IC)
• Immunohistochemistry(Polymer)
• Western Blotting