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Chaperonin 10 (GroEL) and chaperonin 10 (GroES) belong to the ubiquitous family of heat-shock molecular chaperones found in prokaryotes and in eukaryotic organelles. The chaperonins assist the folding of nascent, organelle-imported or stress-destabilized polypeptides. In vitro, purified GroEL together with purified GroES in the presence of Mg-ATP facilitate refolding and reactivation of denatured proteins. Chaperonin 10 (GroES) is expressed in E. coli.
Purity: ≥ 95% by SDS-PAGE.
M.W.: ~11,000
Ref.: Goloubinoff, P., et al., 1989. Nature 342, 884
Mendoza, J. A., et al., 1991. J. Biol. Chem. 266, 13044
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Chaperonin 60(GroEL) and chaperonin 10(GroES) belong to the ubiquitous family of heat-shock molecular chaperones found in prokaryotes and in eukaryotic organelles. The chaperonins assist the folding of nascent, organelle-imported or stress-destabilized polypeptides. In vitro, purified GroEL together with purified GroES in the presence of Mg- ATP facilitate refolding and reactivation of denatured proteins. Chaperonin 60(GroEL) is expressed in E. coli.
Purity: ≥95% by SDS-PAGE.
M.W.: ~ 60,000
Ref.: Goloubinoff, P., et al., 1989. Nature 342, 884
Mendoza, J. A., et al., 1991. J.Biol.Chem. 266, 13044
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