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Products Hsp90(alpha)/(beta) Monoclonal Antibody (Clone K41220A)
| Catalogue number: | 10011439 |
| Hosts: | Mouse |
| Applications: | Western Blot |
| Weight: | 90 |
| Form: | 100 microg |
| Antigen: | human recombinant Hsp90.alpha./.beta. |
| P type: | Antibodies|Heat Shock Protein |
| Shipping temp: | -20 |
| Storage temp: | -20 |
| Additional info: | Hsp90 is an abundantly and ubiquitously expressed Hsp. It is understood to exist in two principal forms, .alpha. and .beta., which share 85% amino acid sequence homology. The two isoforms of Hsp90 are expressed in the cytosolic compartment. Despite the similarities, Hsp90.alpha. exists predominantly as a homodimer while Hsp90.beta. exists mainly as a monomer. From a functional perspective, Hsp90 participates in the folding, assembly, maturation, and stabilization of specific proteins as an integral component of a chaperone complex. Furthermore, Hsp90 is highly conserved between species, having 60% and 78% amino acid similarity between mammalian and the corresponding yeast and Drosophila proteins, respectively. Hsp90 is a highly conserved and essential stress protein that is expressed in all eukaryotic cells. Despite its label of being a Hsp, Hsp90 is one of the most highly expressed proteins in unstressed cells (1-2% cytosolic protein). It carries out a number of housekeeping functions - including controlling the activity, turnover, and trafficking of a variety of proteins. Most of the Hsp90-regulated proteins that have been discovered to date are involved in cell signaling. The number of proteins now know to interact with Hsp90 is about 100. Target proteins include the kinases v-Src, Wee1, and c-Raf, transcriptional regulators such as p53 and steroid receptors, and the polymerases of the hepatitis B virus and telomerase. When bound to ATP, Hsp90 interacts with co-chaperones Cdc37, p23, and an assortment of immunophilin-like proteins, forming a complex that stabilizes and protects target proteins from proteasomal degradation. |
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