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Cpn10 Antibody
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Application 
| WB, IHC, IP, ICC |
|---|---|
| Primary Accession | P61604 |
| Other Accession | NP_002148.1 |
| Host | Rabbit |
| Reactivity | Human, Mouse, Rat, Rabbit, Pig, Bovine, Xenopus, Dog, Sheep, Guinea Pig |
| Clonality | Polyclonal |
| Description | Rabbit Anti-Human Cpn10 Polyclonal |
| Target/Specificity | Detects ~10kDa |
| Other Names | 10kDa Chaperonin Antibody, Chaperonin 10 Antibody, Cpn 10 Antibody, EPF Antibody, GROES Antibody, Heat Shock 10kD protein1 Antibody, HSP10 Antibody, HSPE1 Antibody |
| Immunogen | Human Cpn10 peptide AA 91-101 |
| Purification | Protein A Purified |
| Storage | -20ºC |
| Storage Buffer | PBS pH7.3, 0.02% sodium azide |
| Shipping Temperature | Blue Ice or 4ºC |
| Certificate of Analysis | 1 µg/ml of SPC-193 was sufficient for detection of Cpn10 in 10 µg of Hela lysates by colorimetric immunoblot analysis using Goat anti-rabbit IgG:HRP as the secondary antibody. |
| Cellular Localization | Mitochondrion | Mitochondrion Matrix |
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Provided below are standard protocols that you may find useful for product applications.
Background
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. Cpn10 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 identical 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).
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.
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