Matrix Metalloproteinase 17 MT4, Recombinant Catalytic Domain (MT4-MMP-17)

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-\ntype MMPs (2-5) are known to be expressed in vertebrates. Human MT4-MMP consists of 478aa with a calculated Mr of 53,428D. The following domains and sequence regions are distinguished in MT4-MMP: Prodomain, catalytic domain junction between catalytic domain and hemopexin domain, hemopexin-like domain and C-terminal sequence with transmembrane segment. MT4-MMP transcripts are found mainly in brain, leukocytes, colon, ovary and testis (5). In addition, MT4-MMP mRNA is transcribed in invasive and noninvasive breast carcinoma cell lines (5,6). The recombinant catalytic domain of MT4-MMP is useful for the study of tumorigenesis, arthritis, and inflammatory processes. The enzyme allows screening of matrix metallo- proteinase inhibitors and charac- terization of inhibitor action.\n\nRecombinant 186aa polypeptide, produced by tryptic activation of a recombinant soluble proform purified from E. coli periplasm. The polypeptide contains the native sequence of 185aa, plus a C-terminal linked polyhistidine tag. The calculated Mr of recombinant catalytic domain is 21,693D.\n\nSpecific Activity: The specific activity of MT4-MMP catalytic domain is 3-6mU/mg, where 1U is the activity that hydrolyzes 1umol peptide (7-methoxycoumarin- 4-yl)acetyl-Pro- Leu-Gly-Leu-Dpa-Ala-\nArg) within 1 minute under the assay conditions described by Knight ,et al.\n\nInhibitors: No inhibition of MT4-MMP by TIMPs or chelators of divalent cations like EDTA or o-phenanthroline is yet known. \n\nStorage and Stability: May be stored at 4 degrees C for 1 week or at

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SPECIFICATIONS

Catalog Number

M2432-05

Size

5ug

Form

Supplied as a liquid in 50mM Tris-HCl, pH 7.5, 150mM sodium chloride, 5mM calcium chloride, 0.1% Triton X-100. No preservatives added.

Purity

MT4-MMP catalytic domain appears as a homogeneous band at 24kD in SDS-PAGE

References

1. Matrisian, L.M., (1992) Bioassays 14: 455-463. 2. Sato, H., et al., (1994) Nature 370: 61-65. 3.Will, H. and Hinzmann, B. (1995) Eur. J. Biochem. 231: 602-608. 4. Takino, T., et al., (1995) J. Biol. Chem. 270: 23,013-23,020. 5. Puente, X.S., et al., (1996) Cancer Res. 56: 944-949. 6. Gilles, C., et al., (1997) Lab Invest. 76: 651-660. 7. Knight, C.G., et al., (1992) FEBS Lett. 296: 263-266.