Recombinant Human Chaperonin 60 (CRP0843)
|Recombinant Human Chaperonin 60
- Product Overview
- 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.
- 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 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)
All listed customized services & products are for research use only, not intended for pharmaceutical, diagnostic, therapeutic or any in vivo human use.