Literature DB >> 22078528

Production of recombinant serpins in Escherichia coli.

Mary C Pearce1, Lisa D Cabrita.   

Abstract

Serpins represent a diverse family of proteins that are found in a wide range of organisms and cellular locations. In order to study them, most need to be produced recombinantly, as isolation from their source is not always possible. Due to their relatively uncomplicated structure (single domain, few posttranslational modifications), the serpins are usually amenable to expression in Escherichia coli, which offers a fast and cost-effective solution for the generation of large amounts of protein. This chapter outlines the general procedures used in the expression and subsequent purification of serpins in E. coli, with a particular focus on the methods used for antitrypsin, the archetypal member of the family.
Copyright © 2011 Elsevier Inc. All rights reserved.

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Year:  2011        PMID: 22078528     DOI: 10.1016/B978-0-12-385950-1.00002-X

Source DB:  PubMed          Journal:  Methods Enzymol        ISSN: 0076-6879            Impact factor:   1.600


  3 in total

1.  Expression and Purification of Active Recombinant Human Alpha-1 Antitrypsin (AAT) from Escherichia coli.

Authors:  Beena Krishnan; Lizbeth Hedstrom; Daniel N Hebert; Lila M Gierasch; Anne Gershenson
Journal:  Methods Mol Biol       Date:  2017

Review 2.  Engineering the serpin α1 -antitrypsin: A diversity of goals and techniques.

Authors:  Benjamin M Scott; William P Sheffield
Journal:  Protein Sci       Date:  2019-12-09       Impact factor: 6.725

3.  Efficient strategies to enhance plasmid stability for fermentation of recombinant Escherichia coli harboring tyrosine phenol lyase.

Authors:  Xiao-Ling Tang; Wen-Ye Hu; Zhi-Chao Wang; Ren-Chao Zheng; Yu-Guo Zheng
Journal:  Biotechnol Lett       Date:  2021-04-08       Impact factor: 2.461

  3 in total

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