Chaperonin 10, Recombinant, Human (cpn10, Heat Shock Protein 10, Hsp10)

Chaperonin 10, otherwise known as Cpn10, (groES in E.coli) make up a family of small heart shock proteins with an approximate molecular mass of 10kDa (Hsp10s). Cpn10 acts as a co-chaperone and interacts with the Hsp60 family to promote proper folding of polypeptides. \nCpn10 and Cpn60 both exhibit sevenfold axis of symmetry and function as a team in the protein folding and assembly process (1). Cpn10 has been located in human platelets, but is also present in human maternal serum (2, 3). It has been reported that human Cpn10 is \nidentical with early pregnancy factor, which is involved in control over cell growth and development. This identification suggest that Cpn10 may act like a hormone in stressful situations such as pregnancy (4). \n \nSource:\nHuman DNA, (NM_002157.2) made in E.coli \n\nApplications:\nSuitable for use in Western Blot. Other applications not tested.\n\nRecommended Dilution:\nOptimal dilutions to be determined by the researcher.\n\nStorage and Stability:\nMay be stored at 4 degrees C for short-term only. Aliquot to avoid repeated freezing and thawing.. 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

C3451

Size

50ug

Applications

WB

Form

Supplied as a liquid in 20mM Tris, pH 7.5, 0.3M Sodium Chloride 10% glycerol, 1 mM DTT.

Purity

~90% (SDS-PAGE).

References

1. Velez-Granell C.S., et al. (1994) J of Cell Science. 107(3):539-549. 2. Morton H., Hegh V., and Clunie G.J.A. (1974) Nature (London) 249:459-460. 3. Cavanagh A.C., and Morton H. (1994) Eur. J. Biochem. 222:551-560. 4. Minto M., et al. (1998) Molecular Cell Research. 1403(2):151-157.