Robust production of active Ulp1 (SUMO protease) from inclusion bodies.
E. coli BL21(DE3)
SUMO (small ubiquitin like modifier protein)
Ulp1
Journal
Protein expression and purification
ISSN: 1096-0279
Titre abrégé: Protein Expr Purif
Pays: United States
ID NLM: 9101496
Informations de publication
Date de publication:
11 2023
11 2023
Historique:
received:
02
05
2023
revised:
26
06
2023
accepted:
26
06
2023
medline:
18
8
2023
pubmed:
2
7
2023
entrez:
1
7
2023
Statut:
ppublish
Résumé
High yield purification of Ulp1 is required during the isolation and purification of SUMO-tagged recombinant proteins. However, when expressed as a soluble protein, Ulp1 is toxic to E. coli host cells and most of the protein forms inclusion bodies. The extraction of insoluble Ulp1 followed by its purification and refolding into its active form is a lengthy and costly procedure. In our present study, we developed a simple, cost effective procedure for the large scale production of active Ulp1 that can be used for industrial scale requirements.
Identifiants
pubmed: 37392905
pii: S1046-5928(23)00099-2
doi: 10.1016/j.pep.2023.106328
pii:
doi:
Substances chimiques
Recombinant Fusion Proteins
0
Peptide Hydrolases
EC 3.4.-
Cysteine Endopeptidases
EC 3.4.22.-
Small Ubiquitin-Related Modifier Proteins
0
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
106328Informations de copyright
Copyright © 2023 The Authors. Published by Elsevier Inc. All rights reserved.
Déclaration de conflit d'intérêts
Declaration of competing interest BKRP, VRV and CRR are stock holders of Loka Biosciences Pvt. Ltd. BKRP is the director of operations; VRV and CRR are the managing directors. All the authors declare that they have no conflict of interest.