||Recombinant Human Chaperonin 60 produced inE. colihas a molecular mass of approximately 60 KDa.
||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 inE. coli.
||>95% as determined by SDS-PAGE.
||Liquid. In Tris-HCl Buffer (pH 7.4).
||caspase activation, protein folding, response to unfolded protein