IMBECU   20882
INSTITUTO DE MEDICINA Y BIOLOGIA EXPERIMENTAL DE CUYO
Unidad Ejecutora - UE
artículos
Título:
Isolation of Heat Shock Protein complexes
Autor/es:
CUELLO CARRIÓN F. D.; FANELLI M. A.; CAYADO-GUTIÉRREZ N.; CASTRO G. N.; CIOCCA D. R.
Revista:
METHODS IN MOLECULAR BIOLOGY (CLIFTON, N.J.)
Editorial:
SPRINGER
Referencias:
Año: 2010
ISSN:
1064-3745
Resumen:
Heat shock proteins (Hsp), are molecular chaperones having the capability to interact with several proteins, thus the isolation of a “pure” Hsp might be difficult because they frequently appear coupled with other heat shock and non-heat shock proteins. This can be an advantage to study the specific interaction between a chaperone and other proteins and to generate an anti-tumoral immune response. In this chapter we present two protocols to isolate Hsp, one is by column chromatography with hydroxyapatite and the other is using immunoprecipitation with antibodies coupled to magnetic beads. In both cases we specifically want to bring Hsp coupled with other proteins to use the Hsp together with other compounds as intermediaries to present the coupled peptides/proteins to the immune system, or to explore the associations of a particular Hsp with other proteins.