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

Chaperonin 10 (cpn10) is the ~10kD mammalian equivalent to GroES of E. coli. Chaperonins (1) play fundamental roles in the folding, assembly and translocation of other proteins (2,3). Chaperonin function in vivo requires two distinct family members., cpn60 and cpn10, both of which are also present in chloroplasts and mitochondria. The best studied cpn60 and cpn10, are the GroEL and GroES proteins of E. coli, respectively. Cpn10 and cpn60 both exhibit sevenfold axis of symmetry and function as a team in the protein folding and assembly processes (2,3). Chaperonin 10 has been located in human platelets but more importantly it may also be present in human maternal serum (4,5). It has been reported (5) that human cpn10 is identical with early pregnancy factor (EPF), which is involved in control over cell growth and development. This identification suggests that cpn10 may act like a hormone in stressful situations such as pregnancy. Recombinant Chaperonin 10 protein (human) is also known as Heat Shock Protein 10 (Hsp10) or Mitochondrial Hsp10. It is reported to be identical to Early Pregnancy Factor (EPF).\n\nApplications:\nSuitable for use in Western Blot. Other applications not tested.\n\nRecommended Dilution:\nWestern Blot: 100ng On a 15-well minigel system recommended in a colorimetric.\nOptimal dilutions to be determined by the researcher.\n\nStorage and Stability:\nAliquot to avoid repeated freezing and thawing and store at -70 degrees C. Aliquots are stable for at least 6 months. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap.

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SPECIFICATIONS

Catalog Number

C3450

Size

25ug

Applications

WB

Form

Supplied as a liquid in 20mM Tris, pH 8.0, 150mM sodium chloride.

Purity

(same/more than)90% pure as determined by SDS-PAGE and Western Blot analysis.

References

1. Hemmingsen, S.M., et al., Nature 333: 330-334 (1988). 2. Gething, M.-J. and Sambrook, J., Nature 355: 33-45 (1992). 3. Gatenby, A.A. and Viitanen, P.V., Annu. Rev. Plant Physiol. Plant Mol. Biol. 45: 469-491 (1994). 4. Morton, H., et al., Nature (London) 249: 459-460 (1974). 5. Cavanagh, A.C. and Morton, H., Eur. J. Biochem. 222: 551-560 (1994).