Matrix Metalloproteinase 14, Pro Domain-Catalytic Domain-Hemopexin Domain Recombinant Protein

Matrix metalloproteinases (MMPs) are Zn2+-and Ca2+-dependent endopeptidases which function in the turnover of extracellular matrix components (1). Presently, eighteen secreted MMPs and five membrane-type MMPs (2-5) are known to be expressed in vertebrates. Human MT1-MMP consists of 559 amino acid residues with a calculated Mr of 63516 (2,3). The following domains and sequence regions are distinguished in MT1-MMP: Prodomain (Ser1-Arg88), catalytic domain (Tyr89-Gly261), junction between catalytic domain and hemopexin domain (Gly262-Gly292), hemopexin-like domain (Pro293-Cys485) and C-terminal sequence (Pro486-Val559) with transmembrane segment. When expressed in cells, the catalytic domain and the hemopexin domain of MT1-MMP become exposed on cell surfaces (2,6). A soluble form of MT1-MMP without transmembrane segment has been found in culture medium of a breast carcinoma cell line (7). MT1-MMP is expressed in adult lung, placenta, kidney, ovaries, intesting, prostate and spleen (3). Increased amounts of the enzyme are found in tumor tissues such as lung carcinoma (2), gastric carcinoma (8), breast, head and neck carcinoma (9). MT1-MMP is activated by removal of its prodomain. The reaction is catalyzed by furin, a subtilysin-type serine protease, which recognizes a motif of four basic amino acid residues located between the prodomain and catalytic domain (6). MT1-MMP activates progelatinase A (2,10,11) and procollagenase-3 (12) by proteolytic cleavage of their domains. The ability of MT1-MMP to activate other matrix metalloproteinases provides potential for enhanced pericellular proteolysis in physiological and pathological processes. In particular, activation of progelatinase A by MT1-MMP is considered to contribute to local degradation of extracellular matrix during cell migration and proliferation. MT1-MMP also hydrolyzes fibrillar collagens I, II and III into characteristic 3/4 and 1/4 fragments (13) and it cleaves a number of other ECM proteins, including fibronectin, vitronectin, laminin-1 and dermatan sulfate proteoglycan (6,13). The activity of MT1-MMP is poorly inhibited by TIMP-1 but efficiently inhibited by TIMP-2 and TIMP-3 (11). The recombinant prodomain and catalytic domain of MT1-MMP is useful for the study of Progelatinase A (MMP-2) activation and the degradation of proteins of the extracellular matrix. The enzyme allows screening of matrix metalloproteinase inhibitors and characterization of inhibitor action.

Recombinant polypeptide sequence produced as a periplasmic protein in E. coli. The pro-MT1-MMP deletion mutant consists of MT1-MMP residues corresponding to Ser1-Gly265 followed by the His-tag sequence Leu-Val-Thr-(His)6. The calculated Mr of the recombinant proenzyme is 30860 Da. Upon activation with trypsin the prodomain sequence Ser1-Arg88 is removed from recombinant pro-MT1MMP and enzymatically active catalytic domain beginning with Tyr89 is liberated.

Small volumes of Matrix Metalloproteinase 14, Pro Domain-catalytic Domain-hemopexin Domain recombinant protein vial(s) may occasionally become entrapped in the seal of the product vial during shipment and storage. If necessary, briefly centrifuge the vial on a tabletop centrifuge to dislodge any liquid in the container`s cap. Certain products may require to ship with dry ice and additional dry ice fee may apply.

MBS635999 is a recombinant protein targeting Matrix Metalloproteinase 14, Pro Domain-catalytic Domain-hemopexin Domain. Also known as Matrix Metalloproteinase 14, Pro Domain-catalytic Domain-hemopexin Domain (MT1-MMP, MMP-14, Collagenase-3) Recombinant. Host: Human recombinant from E Coli.