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Hsp90(beta) Monoclonal Antibody (Clone K3701)

Hsp90(beta) Monoclonal Antibody (Clone K3701)

Cat no: 10011440


Supplier: Cayman Chemical Company
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Antigen: human recombinant Hsp90.beta. . Host: mouse, clone K3701 . Cross-reactivity: (+) human (.beta.-specific); (-) Hsp90.alpha. and rat Hsp90.beta. . Applications: WB, EIA, and IHC
Catalogue number: 10011440
Hosts: Mouse
Applications: Immunohistochemistry, Western Blot
Weight: 90
Form: 100 microg
Antigen: human recombinant Hsp90.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, Hsp90a exists predominantly as a homodimer while Hsp90b 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 heat shock protein, 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 signalling. The number of proteins now known 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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