Literature DB >> 25859961

Glutathione-S-transferase (GST)-fusion based assays for studying protein-protein interactions.

Haris G Vikis1, Kun-Liang Guan.   

Abstract

Glutathione-S-transferase (GST)-fusion proteins have become an effective reagent to use in the study of protein-protein interactions. GST-fusion proteins can be produced in bacterial and mammalian cells in large quantities and purified rapidly. GST can be coupled to a glutathione matrix, which permits its use as an effective affinity column to study interactions in vitro or to purify protein complexes in cells expressing the GST-fusion protein. Here, we provide a technical description of the utilization of GST-fusion proteins as both a tool to study protein-protein interactions and also as a means to purify interacting proteins.

Entities:  

Mesh:

Substances:

Year:  2015        PMID: 25859961     DOI: 10.1007/978-1-4939-2425-7_22

Source DB:  PubMed          Journal:  Methods Mol Biol        ISSN: 1064-3745


  1 in total

1.  Calmodulin binds and modulates K+-dependent Na+/Ca2+-exchanger isoform 4, NCKX4.

Authors:  Stephanie Thibodeau; Weidong Yang; Sunita Sharma; Jonathan Lytton
Journal:  J Biol Chem       Date:  2020-11-23       Impact factor: 5.157

  1 in total

北京卡尤迪生物科技股份有限公司 © 2022-2023.