Recombinant Human Chaperonin 10 (CRP0842)
|Recombinant Human Chaperonin 10
- Product Overview
- Recombinant Human Chaperonin 10 produced in E. coli has a molecular mass of approximately 11 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.
- Antigen Description
- 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 denaturedproteins. Chaperonin 10 (GroES) is expressed in E. coli.
- ATP binding, chaperone binding, unfold protein binding
- CPN10; GROES; HSP10; EPF; HSP10; Hsp10; 10 kDa chaperonin; 10 kDa heat shock protein; mitochondrial; Early-pregnancy factor; chaperonin 10; heat shock 10kD protein 1
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