HSP90 is an abundantly and ubiquitously expressed heat shock protein.
It is understood to exist in two principal forms α and β, which share 85% sequence amino acid homology.
The two isoforms of Hsp90, are expressed in the cytosolic compartment (1).
Despite the similarities, HSP90α exists predominantly as a homodimer while HSP90β exists mainly as a monomer.(2) From a functional perspective, hsp90 participates in the folding, assembly, maturation, and stabilization of specific proteins as an integral component of a chaperone complex.
(3-6) 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 it’s label of being a heat-shock protein, hsp90 is one of the most highly expressed proteins in unstressed cells (1–2% of 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.
(7-8).
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.5 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.
In most cases, hsp90-interacting proteins have been shown to co-precipitate with hsp90 when carrying out immunoadsorption studies, and to exist in cytosolic heterocomplexes with it.
In a number of cases, variations in hsp90 expression or hsp90 mutation has been shown to degrade signaling function via the protein or to impair a specific function of the protein (such as steroid binding, kinase activity) in vivo.
Ansamycin antibiotics, such as geldanamycin and radicicol, inhibit hsp90 function (9).
Applications:Suitable for use in Western Blot.
Other applications not tested.
Recommended Dilution:Western Blot:1:5000Optimal dilutions to be determined by the researcher.
Storage and Stability:May be stored at 4°C for short-term only.
Aliquot to avoid repeated freezing and thawing.
Store at -20°C.
Aliquots are stable for at least 12 months.
For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap.
仕様
Size：100ul
Host：rabbit
Source Antibody：human
Grade：Serum
Purity：Serum
Form：Supplied as a lyophilized powder. Reconstitute with 100ul sterile water.
Specificity：Recognizes Hsp90. Species Crossreactivity: In salmonid fish a cross-reactive band at 40kDa is observed. Antibody will also detect a human recombinant Hsp90 protein.
Isotype：IgG
Calc Applications Abbrev：WB
Calc Crossreactivity：Hu
Immunogen：The peptide was chosen from a highly conserved region of Hsp90 found in both the alpha and beta form of the protein. The target peptide is perfectly conserved in animals.
