CHAPERONIN 10 FROM¡ESCHERICHIA COLI =95.0% (SDS-PAGE) RECOMBINANT EXPRESSED IN E. COLI OVERPRODUCING STRAIN LYOPHILIZED POWDER

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.

UPC:

41106202

Condition:

New

Weight:

1.00 Ounces

HazmatClass:

No

MPN:

C7438-250UG