• Purity

  >90%, by SDS-PAGE under reducing conditions and visualized by Colloidal Coomassie® Blue stain

• Activity

  HSP60/HSPD1 is a molecular chaperone that assists in the folding of nascent polypeptides and the refolding of denatured proteins. Reaction conditions will need to be optimized for each specific application.  We recommend an initial HSP60/HSPD1 concentration of 2-3 μM for in vitro use. IMPORTANT: HSP10/HSPE1 (Catalog # AP-150) is required for HSP60/HSPD1 activity and should be used at a concentration that is at least equimolar to HSP60/HSPD1.

• Source

  E. coli-derived Accession # P10809

• Accession #

• Predicted Molecular Mass

  61 kDa

Background: HSP60

HSP60 (also known as Chaperonin 60) is the eukaryotic homologue of prokaryotic GroEL chaperone. This protein is found mainly in mitochondria, but can also be detected in cytosol and extracellular fluids including peripheral blood. HSP60 and HSP10 (also known as Chaperonin 10) form a complex that plays an essential role in the translocation and refolding of proteins from the cytosol into the mitochondrial matrix. Under physiological conditions, HSP60 creates two stacked heptameric rings that form a pair of central hydrophobic cavities. After an unfolded substrate protein enters one of the cavities it is capped by a heptameric HSP10 complex, thereby trapping the unfolded protein. Structural rearrangement of the substrate-containing cavity is effected via HSP60-mediated ATP hydrolysis; this changes the lining of the cavity from hydrophobic to hydrophilic and helps promote refolding of the substrate protein. Binding of ATP to HSP60 subunits on the distal ring of the complex then causes the dissociation of the HSP10 cap complex and concomitant release of the substrate protein from the proximal cavity. If the protein is not completely folded, it can be further processed by the HSP60/HSP10 complex, or can interact with other chaperoning systems.

• References:

1. Cappello F, et al. (2008) Cancer Biol. Therapy 7: 801-809

2. Hartl F.U. & Hayer-Hartl M. (2009) Nat. Struc. Mol. Biol. 16: 574-581

• Long Name:

  Heat Shock Protein 60

• Entrez Gene IDs:

  3329 (Human); 110907 (Mouse); 63868 (Rat)

• Alternate Names:

  60 kDa chaperonin; Chaperonin 60; cpn60; GROEL; heat shock 60kD protein 1 (chaperonin); heat shock 60kDa protein 1 (chaperonin); Heat shock protein 60; heat shock protein 65; HLD4; HSP60; HSP-60; HSP60SPG13; HSP65; HSPD1; HuCHA60; Mitochondrial matrix protein P1,60 kDa heat shock protein, mitochondrial; P60 lymphocyte protein; short heat shock protein 60 Hsp60s1; spastic paraplegia 13 (autosomal dominant); SPG13