Hsp90alphabeta antibody

Antigen: Hsp90alphabeta

Clonality: Monoclonal (Hyb-K41220A)

Host: Mouse

Reactivity: Human, Rat (Rattus), Yeast (Saccharomyces cerevisiae), Schizosaccharomyces pombe (S. pombe)

Application: Western Blotting (WB), ELISA, Immunohistochemistry (IHC)

Catalog no.: ABIN361715

Additional Information

Gene ID: 3326, 3320

UniProt: P08238, P07900

Immunogen: Recombinant human Hsp90alpha

Isotype: IgG2a

Clone: Hyb-K41220A

Description: HSP90 is an abundantly and ubiquitously expressed heat shock protein. It is understood to exist in two principal forms alpha and beta, which share 85% sequence amino acid homology. The two isoforms of Hsp90 are expressed in the cytosolic compartment. Despite the similarities, HSP90alpha exists predominantly as a homodimer while HSP90beta 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% 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. 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.

Synonyms: Hsp86, Hsp89A, Hsp90AA1, Hsp90Alpha, HspC1, HSPCA, HspCAL3, Hsp84, Hsp90B, HspC2, HspCB, D6S182, FLJ26984

Characteristics: Accession Number: NP_031381.2, NP_001017963.2

Specificity: Detects 90kD proteins corresponding to the molecular mass of hsp90 alpha or beta.

Sensitivity: 1µg/ml was sufficient for detection of Hsp90alphabeta in 20µg of heat shocked HeLa cell lysate by colorimetric immunoblot analysis using Goat Anti-Mouse IgG:HRP as the secondary.

Application Details

Application Notes: 1µg/ml was sufficient for detection of hsp90alphabeta by Western Blot in 20µg of HeLa lysate.

Concentration: 1mg/mL

Purification: Protein G Purified

Buffer: PBS pH7.2, 50% glycerol

Storage: Store at -20° C. Shipping Conditions: Blue Ice or 4° C

Storage Shipping Temp Max: Blue Ice or 4 °C

Research Area: Heat Shock Proteins

Restrictions: For Research Use only

Images

Hsp90 (K41220A), CellLine copy.

Publications

Minami, Kawasaki, Miyata et al.: "Analysis of native forms and isoform compositions of the mouse 90-kDa heat shock protein, HSP90." in: The Journal of biological chemistry, Vol. 266, Issue 16, pp. 10099-103, 1991 (PubMed).

Whitesell, Mimnaugh, De Costa et al.: "Inhibition of heat shock protein HSP90-pp60v-src heteroprotein complex formation by benzoquinone ansamycins: essential role for stress proteins in oncogenic transformation." in: Proceedings of the National Academy of Sciences of the United States of America, Vol. 91, Issue 18, pp. 8324-8, 1994 (PubMed).

Pratt, Toft: "Steroid receptor interactions with heat shock protein and immunophilin chaperones." in: Endocrine reviews, Vol. 18, Issue 3, pp. 306-60, 1997 (PubMed).

Nemoto, Sato, Iwanari et al.: "Domain structures and immunogenic regions of the 90-kDa heat-shock protein (HSP90). Probing with a library of anti-HSP90 monoclonal antibodies and limited proteolysis." in: The Journal of biological chemistry, Vol. 272, Issue 42, pp. 26179-87, 1997 (PubMed).

Pratt: "The hsp90-based chaperone system: involvement in signal transduction from a variety of hormone and growth factor receptors." in: Proceedings of the Society for Experimental Biology and Medicine. Society for Experimental Biology and Medicine (New York, N.Y.), Vol. 217, Issue 4, pp. 420-34, 1998 (PubMed).

Pearl, Prodromou: "Structure, function, and mechanism of the Hsp90 molecular chaperone." in: Advances in protein chemistry, Vol. 59, pp. 157-86, 2002 (PubMed).

Neckers: "Hsp90 inhibitors as novel cancer chemotherapeutic agents." in: Trends in molecular medicine, Vol. 8, Issue 4 Suppl, pp. S55-61, 2002 (PubMed).

Pratt, Toft: "Regulation of signaling protein function and trafficking by the hsp90/hsp70-based chaperone machinery." in: Experimental biology and medicine (Maywood, N.J.), Vol. 228, Issue 2, pp. 111-33, 2003 (PubMed).

Arlander, Eapen, Vroman et al.: "Hsp90 inhibition depletes Chk1 and sensitizes tumor cells to replication stress." in: The Journal of biological chemistry, Vol. 278, Issue 52, pp. 52572-7, 2003 (PubMed).

Kishimoto, Fukuma, Mizuno et al.: "Identification of the pentapeptide constituting a dominant epitope common to all eukaryotic heat shock protein 90 molecular chaperones." in: Cell stress & chaperones, Vol. 10, Issue 4, pp. 296-311, 2005 (PubMed).