Literature DB >> 28092034

Expression and Purification of SH2 Domains Using Baculovirus Expression System.

Mari Ogiue-Ikeda1, Kazuya Machida2.   

Abstract

Recombinant proteins expressed in bacteria are sometimes insoluble, aggregated, and incorrectly folded. For those Src homology 2 (SH2) domains that are insoluble in bacteria, baculovirus-insect cell expression systems can be an alternative to produce soluble and functionally active proteins. We describe a protocol for cloning and purification of GST-tagged SH2 domains using the Bac-to-Bac baculovirus expression system.

Keywords:  Bac-to-Bac; Baculovirus expression system; GST fusion protein; Insect cells; SH2 domain

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Year:  2017        PMID: 28092034     DOI: 10.1007/978-1-4939-6762-9_11

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


  2 in total

1.  Expression of a New Recombinant Collagenase Protein of Lucilia Sericata in SF9 Insect Cell as a Potential Method for Wound Healing.

Authors:  Hamzeh Alipour; Abbasali Raz; Navid Dinparast Djadid; Sedigheh Zakeri
Journal:  Iran J Biotechnol       Date:  2019-12-01       Impact factor: 1.671

2.  A Comparative Analysis of Bombyx mori (Lepidoptera: Bombycidae) β-fructofuranosidase Homologs Reveals Different Post-Translational Regulations in Glyphodes pyloalis Walker (Lepidoptera: Pyralidae).

Authors:  Yue Zhao; Liangli Yang; Yu Chen; Xinwei Zhang; Jing Li; Dan Liang; Song Jiang; Junshan Gao; Yan Meng
Journal:  Insects       Date:  2022-04-26       Impact factor: 3.139

  2 in total

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