Bacterial expression and purification of Interleukin-2 Tyrosine kinase: Single step separation of the chaperonin impurity
Open Access
- 31 August 2008
- journal article
- Published by Elsevier BV in Protein Expression and Purification
- Vol. 60 (2), 194-197
- https://doi.org/10.1016/j.pep.2008.04.001
Abstract
No abstract availableKeywords
This publication has 28 references indexed in Scilit:
- Focal adhesion kinase as a regulator of cell tension in the progression of cancerSeminars in Cancer Biology, 2008
- Signalling through TEC kinases regulates conventional versus innate CD8+ T-cell developmentNature Reviews Immunology, 2007
- Development of an Enzyme Immunoassay for Detection of Sapovirus-Specific Antibodies and Its Application in a Study of Seroprevalence in ChildrenJournal of Clinical Microbiology, 2006
- Sustained correction of B-cell development and function in a murine model of X-linked agammaglobulinemia (XLA) using retroviral-mediated gene transferBlood, 2004
- Functional consequences of single:double ring transitions in chaperonins: life in the coldMolecular Microbiology, 2004
- Rapid screening for improved solubility of small human proteins produced as fusion proteins in Escherichia coliProtein Science, 2002
- Disassembly of the Cytosolic Chaperonin in Mammalian Cell Extracts at Intracellular Levels of K+ and ATPPublished by Elsevier BV ,1999
- Escherichia coli maltose‐binding protein is uncommonly effective at promoting the solubility of polypeptides to which it is fusedProtein Science, 1999
- A method for the separation of GST fusion proteins from co-purifying GroELTrends in Genetics, 1996
- Hydrolysis of adenosine 5'-triphosphate by Escherichia coli GroEL: Effects of GroES and potassium ionBiochemistry, 1993