Technical Data
GroES, Recombinant (Chaperonin 10, cpn10, Heat Shock Protein 10, HSP10)
Molecular Biology Storage: -20CShipping: Blue Ice
GroES protein is the co-chaperonin of GroES in E. coli and assists protein folding. GroEL mediated folding requires the co-chaperonin GroES which is essential for viability. GroES is composed of a single heptameric ring of 10kD subunits that binds to the ends of the GroEL cylinder. GroES 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 GroES produced in E. coli is a single, non-glycosylated polypeptide chain containing 97 amino acids and having a molecular mass of 10.4kD.


Storage and Stability:
May be stored at 4C for short-term only. For long-term storage and to avoid repeated freezing and thawing, add 0.1% HSA or BSA, aliquot and store at -20C. Aliquots are stable for at least 6 months at -20C. 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..

Molecular Weight:
Source: E. coli
Purity: 95% 95% as determined by RP-HPLC, anion-exchange FPLC and/or reducing and non-reducing SDS-PAGE Coomassie.
Concentration: ~1mg/ml
Form: Supplied as a liquid in 25mM Tris-HCl, pH 7.5, 100mM sodium chloride, 5mM DTT and 10% glycerol.

Important Note: This product as supplied is intended for research use only, not for use in human, therapeutic or diagnostic applications without the expressed written authorization of United States Biological.
1. Mol. Syst. Biol. 2: 36 (2006). 2. Org. Biomol. Chem. 4(13): 2568-2574 (2006). 3. Cell 125(5): 903-914 (2006). 4. Chem. Rev. 106(5): 1917-1930 (2006). 5. Mol. Biol. (Mosk) 40(2): 277-283 (2006).

Intended for research use only. Not for use in human, therapeutic, or diagnostic applications.