HSPE1 (10kD chaperonin, Chaperonin 10)

HSPE1(heat shock 10kDa protein 1 (chaperonin 10)), also called CPN10, GROES, CHAPERONIN 10 \nHOMOLOG, cpn10 HOMOLOG or HSP10, is a protein that in humans is encoded by the HSPE1 gene. \nGroES is a heptameric ring of identical 10.4-kD subunits that binds to each end of GroEL to form a \nsymmetric, functional heterodimer. The HSP10 gene consists of 4 exons. The HSPE1 gene is mapped to \n2q33.1. The transcriptional activity of the promoter fragment in the HSP60 direction is approximately \ntwice that in the HSP10 direction under normal growth conditions; upon heat shock, promoter activity in \neither direction increased by a factor of approximately 12. Mutational drifts performed in vitro with 4 \ndifferent enzymes indicated the GroES overexpression doubled the number of accumulating mutations, \nand promoted the folding of enzyme variants carrying mutations in the protein core and/or mutations with \nhigher destabilizing effects.\n\nUniProt Number:\nP61604\n\nGene ID:\nHSPE1\n\nApplications:\nSuitable for use in Western Blot, Immunohistochemistry (Paraffin) and Immunocytochemistry.\n\nRecommended Dilution:\nOptimal dilutions to be determined by the researcher.\n\nStorage and Handling:\nStore at -20?C for one year. After reconstitution, store at 4?C for one month. Can also be aliquoted and stored frozen at -20?C for long term.\nAvoid repeated freezing and thawing. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap.

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SPECIFICATIONS

Catalog Number

144706

Size

100ug

Applications

ICC, IHC, WB

Hosts

Rabbit

Reactivities

Hum, Mouse, Rat

Form

Supplied as a lyophilized powder. Each vial contains 5mg BSA, 0.9mg NaCl, 0.2mg Na2HPO4, 0.05mg Thimerosal, 0.05mg NaN3. Reconstitution: Add 0.2ml of distilled water will yield a concentration of 500ug/ml.

P Type

Pab

Purity

Purified by immunoaffinity chromatography.

Isotype

IgG

References

1. Georgopoulos, C., Welch, W. J. Role of the major heat shock proteins as molecular \nchaperones. Annu. Rev. Cell Biol. 9: 601-634, 1993.\n2. Hansen, J. J., Bross, P., Westergaard, M., Nielsen, M. N., Eiberg, H., Borglum, A. D., Mogensen, J., \nKristiansen, K., Bolund, L., Gregersen, N. Genomic structure of the human mitochondrial chaperonin \ngenes: HSP60 and HSP10 are localised head to head on chromosome 2 separated by a \nbidirectional promoter. Hum. Genet. 112: 71-77, 2003. Note: Erratum: Hum. Genet. 112: 436 only, \n2003.\n3. Todd, M. J., Viitanen, P. V., Lorimer, G. H. Dynamics of the chaperonin ATPase cycle: implications for \nfacilitated protein folding. Science 265: 659-666, 1994.

Additional Info

Recognizes human, mouse and rat HSPE1. No crossreactivity with other proteins.