ArticleDaru : journal of Faculty of Pharmacy, Tehran University of Medical Sciences2010
An efficient procedure for purification of recombinant human β heat shock protein 90.
Article in Daru : journal of Faculty of Pharmacy, Tehran University of Medical Sciences, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
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Who cites it
2 citing papers in PubMed.
- Using recombinant Chlamydia trachomatis OMP2 as antigen in diagnostic ELISA test.Iranian journal of microbiology · 2014Article
- Affinity Purification of Tumor Necrosis Factor-α Expressed in Raji Cells by Produced scFv Antibody Coupled CNBr-Activated Sepharose.Advanced pharmaceutical bulletin · 2013Article
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Authors and funding
6 authors.
Funding
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Abstract
background and the purpose of the studyHeat Shock Protein 90 (Hsp90) is typically the most abundant chaperone in the eukaryotic cell cytoplasm, and its expression is essential for loading immunogenic peptides onto major histocompatibility complex molecules for presentation to T-cells. Therefore, it may act as a good candidate as an adjuvant molecule in vaccine technology.
methodsInitially the human Hsp90β gene was cloned into the heat inducible expression vector pGP1-2 and then the recombinant protein was isolated by ion exchange chromatography. After intradermal injection of confirmed purified band of protein to rabbits and isolation of the serum IgG antibody, for its affinity purification, the rabbit's purified Hsp90 specific IgG was coupled to the cyanogen bromide-activated Sepharose 4B.
resultsThe recovery of the purified protein of interest by affinity chromatography was 50%.
conclusionThis research enabled purification of human heat shock protein by a laboratory prepared column chromatography.
Indexed as
Identifiers
22615596PMC3232084What OpenQuestion holds
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