Versatile E. coli thioredoxin specific monoclonal antibodies afford convenient analysis and purification of prokaryote expressed soluble fusion protein
- 1 January 1995
- journal article
- Published by Elsevier in Journal of Immunological Methods
- Vol. 185 (2) , 237-244
- https://doi.org/10.1016/0022-1759(95)00119-u
Abstract
No abstract availableKeywords
This publication has 9 references indexed in Scilit:
- Cloning and Expression of a Murine Fascin Homolog from Mouse BrainPublished by Elsevier ,1995
- Enhanced detection of human IL-5 in biological fluids utilizing murine monoclonal antibodies which delineate distinct neutralizing epitopesCytokine, 1994
- A Thioredoxin Gene Fusion Expression System That Circumvents Inclusion Body Formation in the E. coli CytoplasmNature Biotechnology, 1993
- Protein Folding Intermediates and Inclusion Body Formation.Nature Biotechnology, 1989
- An Escherichia coli vector to express and purify foreign proteins by fusion to and separation from maltose-binding proteinGene, 1988
- Single-step purification of polypeptides expressed in Escherichia coli as fusions with glutathione S-transferaseGene, 1988
- THIOREDOXINAnnual Review of Biochemistry, 1985
- A solid-phase immunoenzymatic technique for the enumeration of specific antibody-secreting cellsJournal of Immunological Methods, 1983
- Utilization of the biotin/avidin system to amplify the sensitivity of the enzyme-linked immunosorbent assay (ELISA)Journal of Immunological Methods, 1983