GroEL, Recombinant (Chaperonin 60, cpn60, Heat Shock Protein 60, HSP60)

GroEL protein is the major heat shock protein of E.coli and belongs to the chaperonin(HSP60) family. GroEL protein prevents misfolding of proteins and promotes the refolding and proper assembly of unfolded polypeptiedes generated under stress condition. GroEL gene was amplified by PCR from E.coli and cloned into an expression vector. This protein was overexpressed in E.coli and was purified by using conventional chromatography techniques. Recombinant GroEL produced in E. coli is a single,non-glycosylated polypeptide chain conjtaining 548 amino acids and having a molecular mass of 57.3kD.\n\nStorage and Stability:\nMay be stored at 4 degrees C for short-term only. For long-term storage, add 0.1% HSA or BSA, aliquot and store at -20 degrees C. Aliquots are stable for at least 6 months at -20 degrees C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Further dilutions can be made in assay buffer.

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SPECIFICATIONS

Catalog Number

G8976-01A

Size

20ug

Form

Supplied as a liquid in Tris buffer salts, potassium chloride, magnesium chloride, DTT, and trehalose as stabilizer.

Purity

(same/more than) 95% (SDS-PAGE).

References

1. Markov propagation of allosteric effects in biomolecular systems: application to GroEL-GroES.Mol Syst Biol 2006;2:36 2. Heat shock proteins form part of a danger signal cascade in response to lipopolysaccharide and GroELClin Exp Immunol 2006 Jul;145(1):183- 3. Hydrogel polymer appears to mimic the performance of the GroEL/GroES molecular chaperone machine. Org Biomol Chem 2006 Jul 7;4(13):2568-74 4. Survival and stress induced expression of groEL and rpoD of Campylobacter jejuni from different growth phases. Int J Food Microbiol 2006 Jun 15; 5. Automated cryoEM data acquisition and analysis of 284742 particles of GroEL.J Struct Biol 2006 May 22; 6. Co-translational binding of GroEL to nascent polypeptides is followed by post-translational encapsulation by GroES to mediate protein folding. J Biol Chem 2006 Jun 5;