Cloning strategy, production and purification of proteins with exopeptidase-cleavable His-tags
Author:
Publisher
Springer Science and Business Media LLC
Subject
General Biochemistry, Genetics and Molecular Biology
Link
http://www.nature.com/articles/nprot.2006.388.pdf
Reference9 articles.
1. Arnau, J., Lauritzen, C., Petersen, G.E. & Pedersen, J. Current strategies for the use of affinity tags and tag removal for the purification of recombinant proteins. Protein Expr. Purif. 48, 1–13 (2006).
2. Pedersen, J., Lauritzen, C., Madsen, M.T. & Weis Dahl, S. Removal of N-terminal polyhistidine tags from recombinant proteins using engineered aminopeptidases. Protein Expr. Purif. 15, 389–400 (1999).
3. Cebe, R. & Geiser, M. Rapid and easy thermodynamic optimization of the 5′-end of mRNA dramatically increases the level of wild type protein expression in Escherichia coli. Protein Expr. Purif. 45, 374–380 (2006).
4. Svensson, J., Andersson, C., Reseland, J.E., Lyngstadaas, P. & Bulow, L. Histidine tag fusion increases expression levels of active recombinant amelogenin in Escherichia coli. Protein Expr. Purif. 48, 134–141 (2006).
5. Dahl, S.W. et al. Carica papaya glutamine cyclotransferase belongs to a novel plant enzyme subfamily: cloning and characterization of the recombinant enzyme. Protein Expr. Purif. 20, 27–36 (2000).
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