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Produktmerkmale
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Synonyms: HSP90AB1, HSP90B, HSPC2, HSPCB, HSP84, HSP-90, HSP-84, Heat shock protein HSP90-beta, HSP90AA1, HSP90A, HSPC1, HSPCA, HSP86, HSP-86, Renal carcinoma antigenNY-REN-38, Heat shock protein HSP 90-alpha
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Weitere Bezeichnung
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Heat Shock Protein 90 (HSP90) alpha/beta
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Gen-ID
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3320
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Swiss-Prot
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P07900
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Immunogen
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Recombinant Human hsp90 alpha
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Kreuzreaktivität
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Human, Ratte (Rattus), Hefe (Saccharomyces Cerevisiae), Schizosaccharomyces pombe (S. pombe)
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Isotyp
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IgG2a (Passende Sekundärantikörper)
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Klon
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Hyb-K41220A
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Beschreibung
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HSP90 is an abundantly and ubiquitously expressed heat shock protein. It is understoodto 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 thesimilarities, HSP90α exists predominantly as a homodimer while HSP90β exists mainly asa monomer. (2) From a functional perspective, hsp90 participates in the folding, assembly,maturation, and stabilization of specific proteins as an integral component of a chaperonecomplex. (3-6) Furthermore, Hsp90 is highly conserved between species, having 60% and78% amino acid similarity between mammalian and the corresponding yeast andDrosophila proteins, respectively. Hsp90 is a highly conserved and essential stress protein that is expressed in all eukaryoticcells. Despite its label of being a heat-shock protein, hsp90 is one of the most highlyexpressed proteins in unstressed cells (1–2% of cytosolic protein). It carries out a numberof housekeeping functions – including controlling the activity, turnover, and trafficking of avariety of proteins. Most of the hsp90-regulated proteins that have been discovered todate are involved in cell signaling (7-8). The number of proteins now know to interact withHsp90 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 thehepatitis B virus and telomerase. 5 When bound to ATP, Hsp90 interacts withco-chaperones Cdc37, p23, and an assortment of immunophilin-like proteins, forming acomplex that stabilizes and protects target proteins from proteasomal degradation. In most cases, hsp90-interacting proteins have been shown to co-precipitate with hsp90when carrying out immunoadsorption studies, and to exist in cytosolic heterocomplexeswith it. In a number of cases, variations in hsp90 expression or hsp90 mutation has beenshown to degrade signaling function via the protein or to impair a specific function of theprotein (such as steroid binding, kinase activity) in vivo. Ansamycin antibiotics, such asgeldanamycin and radicicol, inhibit hsp90 function (9).
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Spezifität
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Detects 90kD proteins corresponding to the molecular mass of HSP90 alpha or beta. Species: Human (beta-specific), Rat (Liver), S. cerevisiae, S. pombe. Limited or no crossreactivityto rice or P. caudatum (Ref. 10). Others not tested.
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