Expression and Purification of Active Monomeric MMP7.

Yamamoto, Kazuhiro ORCID: 0000-0002-8481-775X, Isohata, Moe and Higashi, Shouichi (2024) Expression and Purification of Active Monomeric MMP7. Methods in molecular biology (Clifton, N.J.), 2747. pp. 67-73.

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Abstract

MMP7 is the smallest member of the MMP family and plays multiple physiological and pathological roles through interaction with a variety of molecules. Purified MMP7 would be beneficial for studying its function and for the development of inhibitors, which could be potential therapeutics. Due to low levels of endogenously produced MMP7, its recombinant expression and purification using E. coli have been established. Here, we describe an effective method to express and purify an active form of MMP7. Our recent discovery is that adding high concentration of CaCl₂ during refolding process prevents nonspecific binding of MMP7 to plastic and its aggregation, significantly improving the yield of active monomeric forms of MMP7.

Item Type:	Article
Uncontrolled Keywords:	Escherichia coli, Matrix Metalloproteinase 7
Divisions:	Faculty of Health and Life Sciences Faculty of Health and Life Sciences > Institute of Life Courses and Medical Sciences
Depositing User:	Symplectic Admin
Date Deposited:	20 Dec 2023 09:28
Last Modified:	02 Jan 2024 22:33
DOI:	10.1007/978-1-0716-3589-6_6
Related URLs:	Author Publisher
URI:	https://livrepository.liverpool.ac.uk/id/eprint/3177454