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Recombinant Human Chaperonin 60 produced in E. coli has a molecular mass of approximately 60 KDa.
>95% as determined by SDS-PAGE.
Liquid. In Tris-HCl Buffer (pH 7.4).
A chaperonin called GroEL-GroES complex (from Escherichia coli) (PDB code=1aon). Two rings of 7x2GroEL proteins (shown in blue and green) with a cap (just on one side) of GroES proteins (red and yellow). Unfolded proteins enter that cavity (which is protein sized) to be protected during folding.
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.
ATP binding, chaperone binding, unfold protein binding
CPN60; GROEL; HSP-60; HSP60; HSP65; Hsp60; HuCHA60; SPG13; chaperonin; 60 kDa chaperonin; 60 kDa heat shock protein; mitochondrial precursor; Heat shock protein 60; Mitochondrial matrix protein P1; P60 lymphocyte protein; heat shock 60kD protein 1 (chaperonin); heat shock protein 65; short heat shock protein 60 Hsp60s1; spastic paraplegia 13 (autosomal dominant)