Heat Shock Protein 90, beta (HSP90) (Biotin)

The 90kD heat shock protein (HSP90) is a molecular chaperone that keeps a target protein in a folding-competent state. Hsp90 is ubiquitously expressed and abundant, and it participates in the folding, assembly, maturation, and stabilization of specific proteins as an integral component of a chaperone complex. 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. In its ATP-bound state, Hsp90 interacts with the co-chaperones Cdc37, p23, and an assortment of immunophilin-like proteins, forming a complex that stabilizes and protects target proteins from proteasomal degradation. Hsp90 is highly conserved between species; mammalian proteins demonstrate 60% amino acid identity with the corresponding yeast and 78% identity with the corresponding Drosophila proteins. Two isoforms of HSP90, alpha and beta, are expressed in the cytosolic compartment.6 The amino acid sequence of human HSP90 alpha is 85% homologous to HSP90 beta, but HSP90 alpha exists predominantly as a homodimer while HSP90 beta exists mainly as a monomer.

Applications:
Suitable for use in ELISA, Immunohistochemistry, Immunoprecipitation, Western Blot, Immunocytochemistry and Immunofluorescence. Other applications have not been tested.

Recommended Dilutions:
Optimal dilutions to be determined by the researcher.

Storage and Stability:
Store product at 4°C if to be used immediately within two weeks. For long-term storage, aliquot to avoid repeated freezing and thawing and store at -20°C. Aliquots are stable at -20°C for 12 months after receipt. Dilute required amount only prior to immediate use. Further dilutions can be made in assay buffer. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap.