| Literature DB >> 23329490 |
Ayesha Murshid1, Jianlin Gong2, Stuart K Calderwood3.
Abstract
The molecular chaperone heat-shock protein 70 (Hsp70) possesses immune stimulatory properties that have been employed in the preparation of anticancer vaccines. Hsp70 binds antigenic peptides in the cytoplasm of cancer cells. Hsp70 thus serves as a convenient, non-discriminating transporter of antigens and can protect the peptides during internalization by APC and cross presentation to T lymphocytes. We describe a method for purifying Hsp70-peptide complexes that can be used to prepare molecular chaperone-based vaccines, involving sequential gel filtration, ion exchange, and affinity chromatography.Entities:
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Year: 2013 PMID： 23329490 PMCID： PMC4100612 DOI： 10.1007/978-1-62703-218-6_17
Source DB: PubMed Journal: Methods Mol Biol ISSN： 1064-3745