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| Catalog Code: | NB110-61642 |
| Product Name: | Hsp60 Antibody |
| Product Description: | Mouse Monoclonal anti-Hsp60 (LK-1) |
| Clone: | LK-1 |
| Clonality: | Monoclonal |
| ListPrice: | 325 |
| Concentration: | 1 mg/ml |
| Immunogen: | Human Hsp60 produced through recombinant DNA methods in E.coli. |
| Specificity: | Recognizes a ~60kDa protein, corresponding to the molecular mass of hsp60 on SDS-PAGE immunoblots. |
| Cross Reactivity: | Human, Mouse, Rat, Bovine, Canine, Chicken, Drosophila, Guinea Pig, Hamster, Monkey, Pig, Rabbit, Sheep, Xenopus. Not tested in other species. |
| Packaging: | 0.2 mg IgG purified Mouse ascites. |
| Background: | Hsp60 is a member of a highly conserved family which includes molecular chaperones from several species such as plant Hsp60 (known as Rubisco binding protein), GroEL, the E.coli Hsp60 and 65 kDa major antigen of mycobacteria. In eukaryotes, Hsp60 is localized in the mitochondrial matrix and in plants Hsp60 is localized in the chloroplast. Mitochondria, chloroplasts and bacteria have a common ancestry (>1 billion years) and this fact together with the high degree of homology between the divegent Hsp60s would indicate that these proteins carry out a primitive but important function which is similar to all of these different species. The common characteristics of the Hsp60s from the divergent species are i) high abundance, ii) induction with environmental stress such as heat shock, iii) homo oligomeric structures of either 7 or 14 subunits which reversibly dissociate in the presence of magnesium ions and ATP, iv) ATPase activity and v) a role in folding and assembly of oligomeric protein structures. These similarities are supported by recent studies where the single ring human mitochondrial homolog, Hsp60 with its co chaperonin, Hsp10 were expressed in a E. coli strain, engineered so that the groE operon is under strict regulatory control. This study has demonstrated that expression of Hsp60-Hsp10 was able to carry out all essential in vivo functions of GroEL and its co chaperonin, GroES. Consistent with their functions as chaperones, Hsp60 and Hsp10 have been suggested to act as docking molecules with a passive role in the maturation of caspase processing. Data demonstrates that recombinant Hsp60 and Hsp10 have been shown to accelerate the activation of procaspase 3 by cytochrome c and dATP in an ATP dependent manner. Hsps are intracellular proteins which are thought to serve protective functions against infection and cellular stress, however several recent studies indicate that members of the Hsp60 family are linked to a number of autoimmune diseases, artherosclerosis and chlamydial disease. |
| Storage: | Aliquot and store at -20C. |
| Purity: | IgG purified |
| Isotype: | IgG1 |
| Host Name: | Mouse |
| Buffer: | PBS, 50% glycerol |
| Application Summary: | flow cytometry / FACS analysis, ELISA, immunoprecipitation, Western Blot |
| Species Summary: | Bv, Ca, Ch, Dr, Ha, Hu, Mu, Po, Mk, Rt, Rb, Gp, Sh, Xp, |
| Alternate Names: | anti-60 kDa chaperonin antibody, anti-60 kDa heat shock protein mitochondrial antibody, anti-Chaperonin antibody, anti-CPN 60 antibody, anti-CPN60 antibody, anti-GROEL antibody, anti-GroEL Homolog antibody, anti-Heat shock 60kD protein 1 chaperonin antibody, anti-Heat shock 60kDa protein 1 antibody, anti-Heat Shock Protein 60 antibody, anti-Heat shock protein 65 antibody, anti-Hsp 60 antibody, anti-HSP 65 antibody, anti-HSP65 antibody, anti-HSPD 1 antibody, anti-HSPD1 antibody, anti-HuCHA60 antibodyanti-Mitochondrial matrix protein P1 antibody, anti-P60 lymphocyte protein antibody, anti-Short heat shock protein 60 Hsp60s1 antibody, anti-Spastic paraplegia 13 antibody, anti-SPG 13 antibody, anti-SPG13 antibody |
| Package Size: | 0.2 mg |
| Preservative: | 0.09% Sodium Azide |
| General References: | 1. Hartl, F.U. (1996) Nature 381: 571-579. 2. Bukau, B. and Horwich, A.L. (1998) Cell 92: 351-366. 3.Hartl, F.U. and Hayer-Hartl, M. (2002) Science 295: 1852-1858. 4. Jindal, S., et al. (1989) Molecular and Cellular Biology 9: 2279-2283. 5. La Verda, D., et al (1999) Infect Dis. Obstet. Gynecol. 7: 64-71. 6. Itoh, H. et al. (2002) Eur. J. Biochem. 269: 5931-5938. 7. Gupta, S. and Knowlton, A.A. J. Cell Mol Med. 9: 51-58. 8. Deocaris, C.C. et al. (2006) Cell Stress Chaperones 11: 116- 128. 9. Lai, H.C. et al. (2007) Am. J. Physiol. Endocrinol. Metab. 292: E292-E297. 10. Gao, Y.L., et al (1995) J. of Immunology 154: 3548-3556. 11. Neuer, A., et al (1997) European Society for Human Reproduction and Embryology 12(5):925-929. 12. Bason, C., et al (2003) Lancet 362(9400): 1971-1977. |
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