Biochem/physiol Actions
Chaperonin60 (GroEL) and chaperonin10 (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, e.g., the photosynthetic enzyme rubisco and the mitochondrial enzyme rhodanese.
The folding activity of a 1:1 molar mixture of GroEL and GroES was tested using urea-denatured rhodanese. At least 2-fold reactivation of rhodanese over the spontaneous reactivation was obtained.
Packaging
Package size based on protein content.
Physical form
Lyophilized powder containing Tris buffer salts, potassium chloride, dithiothreitol and trehalose as stabilizer.
| biological source | Escherichia coli |
| Quality Segment | 200 |
| recombinant | expressed in E. coli overproducing strain |
| assay | ≥95.0% (SDS-PAGE) |
| form | lyophilized powder |
| technique(s) | activity assay: suitable |
| UniProt accession no. | P61604 |
| storage temp. | 2-8°C |
| Gene Information | human ... HSPE1(3336) |
