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Expression Optimization and Characterization of the Catalytic Domain of Human MT3-MMP11 Supported by the National Natural Science Foundation of China (No. 30371656).

Authors
Journal
Chemical Research in Chinese Universities
1005-9040
Publisher
Springer-Verlag
Publication Date
Volume
22
Issue
2
Identifiers
DOI: 10.1016/s1005-9040(06)60061-5
Keywords
  • Articles
Disciplines
  • Biology
  • Medicine

Abstract

Matrix metalloproteinases (MMPs) are a family of proteases that are required for many biological processes and are also elevated in many pathological conditions. MMP inhibitors (MMPIs) may therefore be useful as therapeutic agents in treating a number of diseases including cancer, cardiovascular diseases and arthritis. Attempts have been made to develop MMPIs. Recombinant MMPs have been used to screening MMPs in vitro assays. In this work, we report the expression of MMP-16 in E. coli and the characterization of the recombinant MMP-16 with a commonly used MMP substrate DQ-gelatin.

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