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HSP90 alpha/beta Antibody: Dylight 350, Polyclonal

HSP90 alpha/beta Antibody: Dylight 350, Polyclonal
394,55 €
Artikelnummer: STRSPC-745D-DY350

Verfügbarkeit: Regellieferzeit: Innerhalb 1 - 2 Wochen

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HSP90 alpha/beta Antibody: Dylight 350, Polyclonal, Host: Llama, Isotype: IgG1, IgG2, IgG3


Llama Anti-Human HSP90 alpha/beta Polyclonal
Target: HSP90 alpha/beta
Purification: Peptide Affinity Purified
Specificity: Detects 90 kDa. Detects HSP90 alpha and beta.
Conjugate: Dylight 350
Immunogen Species: Human
Cellular Location: Cytoplasm, Melanosome, Nucleus, Secreted, Cell Membrane
Immunogen: Synthetic human HSP90 alpha full length protein
Scientific Background: 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 its 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).
Reference: 1. Nemoto, T. et al. (1997) J.Biol Chem. 272: 26179-26187.2. Minami Y, et al. (1991), J.Biol Chem. 266: 10099-10103.3. Arlander SJH, et al. (2003) J Biol Chem 278: 52572-52577.4. Pearl H, et al. (2001) Adv Protein Chem 59: 157-186.5. Neckers L, et al. (2002) Trends Mol Med 8: S55-S61.6. Pratt W, Toft D. (2003) Exp Biol Med 228: 111-133.7. Pratt W, Toft D. (1997) Endocr Rev 18: 306–360. 8. Pratt WB. (1998) Proc Soc Exptl Biol Med 217: 420–434.9. Whitesell L, et al. (1994) Proc Natl Acad Sci USA 91: 8324–8328.10. Kishimoto J, et al. (2005). Cell Stress and Chaperones. 10 (4): 296-311.


Artikelnummer STRSPC-745D-DY350
Hersteller Stressmarq Biosciences
Herstellernummer SPC-745D-DY350
Verpackungseinheit 100 µg
Mengeneinheit FL
Reaktivität Human, Mouse (Murine), Rat (Rattus)
Klonalität Polyclonal
Wirt / Host Llama
Methode ELISA, Western Blotting
Isotype IgG1
Gene ID NCBI (externer Link)
Datenblatt Download
MSDS Download