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Tytuł pozycji:

Functional expression and purification of the untagged C-terminal domain of MMP-2 from Escherichia coli inclusion bodies.

Tytuł:
Functional expression and purification of the untagged C-terminal domain of MMP-2 from Escherichia coli inclusion bodies.
Autorzy:
Zhou Y; School of Chemistry and Chemical Engineering, South China University of Technology, 510640, Guangzhou, China.
He C; School of Chemistry and Chemical Engineering, South China University of Technology, 510640, Guangzhou, China. Electronic address: .
Źródło:
Protein expression and purification [Protein Expr Purif] 2020 Dec; Vol. 176, pp. 105726. Date of Electronic Publication: 2020 Aug 11.
Typ publikacji:
Journal Article; Research Support, Non-U.S. Gov't
Język:
English
Imprint Name(s):
Publication: Orlando, FL : Academic Press
Original Publication: San Diego : Academic Press, c1990-
MeSH Terms:
Cloning, Molecular*
Escherichia coli*/chemistry
Escherichia coli*/genetics
Escherichia coli*/metabolism
Gene Expression*
Matrix Metalloproteinase 2*/biosynthesis
Matrix Metalloproteinase 2*/chemistry
Matrix Metalloproteinase 2*/genetics
Matrix Metalloproteinase 2*/isolation & purification
Inclusion Bodies/*chemistry
Humans ; Inclusion Bodies/genetics ; Inclusion Bodies/metabolism ; Protein Domains
Contributed Indexing:
Keywords: C-terminal domain; Expression and purification; Inclusion body; Matrix metalloproteinase 2
Substance Nomenclature:
EC 3.4.24.24 (MMP2 protein, human)
EC 3.4.24.24 (Matrix Metalloproteinase 2)
Entry Date(s):
Date Created: 20200814 Date Completed: 20210128 Latest Revision: 20210128
Update Code:
20240105
DOI:
10.1016/j.pep.2020.105726
PMID:
32791091
Czasopismo naukowe
The C-terminal domain (CTD) of MMP-2, which includes a hemopexin-like domain, has been increasingly studied as an alternative target in developing selective intervention strategies towards MMP-2. Moreover, The CTD itself has been implicated in a growing number of biological events, either MMP-dependent or -independent. The production of CTD, however, has been mostly based on the uncontrolled lysis of the latent ProMMP-2 or fusion protein expression that leaves a fusion tag. In this work we present a facile production of the untagged CTD in E. coli. The target protein was expressed as inclusion bodies, and we established an efficient wash and refolding strategy that allows us to obtain the target protein in extremely high purity. The yield was established at ~6 mg/L of the culture medium, which would greatly facilitate the production and hence the biological study of CTD. The method described herein might also prove useful for related (domain) proteins in MMP family and beyond.
(Copyright © 2020 Elsevier Inc. All rights reserved.)

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