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Products Polyclonal Anti-HSPE1
| Catalogue number: | PA1790 |
| Price: | $200.00 |
| Reactivities: | Human, Mouse, Rat |
| Applications: | Immunocytochemistry, Immunohistochemistry, Western Blot |
| Size: | 100ug/vial |
| Gene: | HSPE1 |
| Swiss prot: | P61604 |
| Form: | Lyophilized |
| Format: | Each vial contains 5mg BSA, 0.9mg NaCl, 0.2mg Na2HPO4, 0.05mg Thimerosal, 0.05mg NaN3. |
| Storage temp: | At -20 degree C for one year. After reconstitution, at 4 degree C for one month. It can also be aliquotted and stored frozen at -20 degree C for a longer time.Avoid repeated freezing and thawing. |
| Scientific background: | HSPE1(heat shock 10kDa protein 1 (chaperonin 10)), also called CPN10, GROES, CHAPERONIN 10 HOMOLOG, cpn10 HOMOLOG or HSP10, is a protein that in humans is encoded by the HSPE1 gene. GroES is a heptameric ring of identical 10.4-kD subunits that binds to each end of GroEL to form a symmetric, functional heterodimer. The HSP10 gene consists of 4 exons. The HSPE1 gene is mapped to 2q33.1. The transcriptional activity of the promoter fragment in the HSP60 direction is approximately twice that in the HSP10 direction under normal growth conditions; upon heat shock, promoter activity in either direction increased by a factor of approximately 12. Mutational drifts performed in vitro with 4 different enzymes indicated the GroES overexpression doubled the number of accumulating mutations, and promoted the folding of enzyme variants carrying mutations in the protein core and/or mutations with higher destabilizing effects. |
| References: | 1. Georgopoulos, C., Welch, W. J. Role of the major heat shock proteins as molecular chaperones. Annu. Rev. Cell Biol. 9: 601-634, 1993. 2. Hansen, J. J., Bross, P., Westergaard, M., Nielsen, M. N., Eiberg, H., Borglum, A. D., Mogensen, J., Kristiansen, K., Bolund, L., Gregersen, N. Genomic structure of the human mitochondrial chaperonin genes: HSP60 and HSP10 are localised head to head on chromosome 2 separated by a bidirectional promoter. Hum. Genet. 112: 71-77, 2003. Note: Erratum: Hum. Genet. 112: 436 only, 2003. 3. Todd, M. J., Viitanen, P. V., Lorimer, G. H. Dynamics of the chaperonin ATPase cycle: implications for facilitated protein folding. Science 265: 659-666, 1994. |
| Additional info: | A synthetic peptide corresponding to a sequence at the C-terminal of human HSPE1, different from the related rat and mouse sequences by one amino acid. |
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