Anti-Cpn10/HSPE1 Antibody Picoband® Fluoro647 Conjugated

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 ion is approximately twice that in the HSP10 ion under normal growth conditions; upon heat shock, promoter activity in either ion 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.

A synthetic peptide corresponding to a sequence at the C-terminus of human Cpn10, different from the related rat and mouse sequences by one amino acid.

Cancer, Chaperones, Heat Shock Proteins, Metabolism, Mitochondrial, Mitochondrial Markers, Mitochondrial Metabolism, Pathways and Processes, Protein Trafficking, Signal Transduction

Eukaryotic CPN10 homolog which is essential for mitochondrial protein biogenesis, together with CPN60. Binds to CPN60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter.

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 biional 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.