CHAPERONIN 60 FROM ESCHERICHIA COLI >95% (SDS-PAGE) RECOMBINANT EXPRESSED IN E. COLI OVERPRODUCING STRAIN LYOPHILIZED POWDER

Application

Chaperonin 60 from Escherichia coli has been used:

• in mass spectroscopy
• in cryo-electron microscopy imaging as control for testing particle distribution
• as standard in infrared spectrum measurements

Biochem/physiol Actions

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, 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, magnesium chloride, dithiothreitol, and trehalose as stabilizer.

UPC:

51281672

Condition:

New

Weight:

1.00 Ounces

HazmatClass:

No

Quantity:

1

Unit of Measurement:

MG

MPN:

C7688-1MG