Anti-HSP27

The heat-shock proteins (HSPs) belong to a larger group of polypeptides, the stress proteins, that are induced in various combinations in response to environmental challenges and developmental transitions. Synthesis of the small (27-kD) HSP has been shown to be correlated with the acquisition of thermotolerance. The deduced 199-amino acid HSP27 protein shows sequence similarity to mammalian alpha-crystallins. Approximately 20% of its residues are susceptible to phosphorylation. The HSP27 gene, which is mapped to 7q11.23 and has 3 exons, produced a 2.2-kb transcript in an in vitro transcription assay. Decreasing ROS in cells expressing mutant huntingtin, HSP27 protects cells against oxidative stress. In other words, HSP27 is a suppressor of polyglutamine (polyQ)-mediated cell death. Furthermore, MAPKAPK5 is a major stress-activated kinase that can phosphorylate HSP27 in vitro.

Liquid

2-8C. For long term -20C after reconstitution.

• 1. Hickey, E., Brandon, S. E., Sadis, S., Smale, G., Weber, L. A. : Molecular cloning of sequences encoding the human heat-shock proteins and their expression during hyperthermia. Gene 43: 147-154, 1986.
• 2. Wyttenbach, A., Sauvageot, O., Carmichael, J., Diaz-Latoud, C., Arrigo, A.-P., Rubinsztein, D. C. : Heat shock protein 27 prevents cellular polyglutamine toxicity and suppresses the increase of reactive oxygen species caused by huntingtin. Hum. Molec. Genet. 11: 1137-1151, 2002.
• 3. New, L., Jiang, Y., Zhao, M., Liu, K., Zhu, W., Flood, L. J., Kato, Y., Parry, G. C. N., Han, J. :
• PRAK, a novel protein kinase regulated by the p38 MAP kinase. EMBO J. 17: 3372-3384, 1998.

Each vial contains 50% glycerol, 0.9mg NaCl, 0.2mg Na2HPO4.