Heat Shock Protein 90 (HSP90) antibody

Antigen: Heat Shock Protein 90 (HSP90)

Synonyms: swo1, hsp90, HSP90, htpG, SCBAC25F8.08, 23.m06066, 17.m07646, HSP90-1

Clonality: Monoclonal (H9010)

Host: Mouse

Reactivity: Human, Rabbit, Chicken

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

Catalog no.: ABIN361717

Additional Information

Characteristics: Detects 90kDa proteins corresponding to the molecular mass of Hsp90beta.

Alternative name: Hsp90

Gene ID: 3326

Swiss-Prot: P08238

Immunogen: Recombinant human Hsp90beta

Format: Liquid

Isotype: IgG2a  (Matching secondary antibodies)

Clone: H9010

Description: Hsp90 is a highly conserved and essential stress protein that is expressed in all eukaryotic cells. From a functional perspective, hsp90 participates in the folding, assembly, maturation, and stabilization of specific proteins as an integral component of a chaperone complex (1-4). 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 (5-6). 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: Hsp84, Hsp90, Hsp90 beta, Hsp90B, HspC2, HSPCB

Specificity: Detects 90kD proteins corresponding to the molecular mass of hsp90beta. Species cross-reactivity: Human (beta-specific), Rabbit (beta-specific), Chicken (alpha/beta), Rat, Canine.

Sensitivity: 1 µg/mL of SMC-107 was sufficient for detection of Hsp90beta in 20µg of heat shocked HeLa cell lysate by colorimetric immunoblot analysis using Goat anti-mouse IgG:HRP as the secondary antibody.

Application Details

Concentration: 1 mg/mL

Purification: Protein G Purified

Buffer: PBS pH7.2, 50% glycerol

Storage: -20 °C

Storage Shipping Temp Max: Blue Ice or 4 °C

Research Area: Cancer, Heat Shock Proteins

Restrictions: For Research Use only

Images

Hsp90 (H9010) Human Colon Cancer Amplifier

Hsp90 (H9010)Human Colon Cancer 1 IN 100,000 IF, Amplifier

Hsp90 (H9010) Human Colon Cancer, Amplifer

Publications

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).

Barent, Nair, Carr et al.: "Analysis of FKBP51/FKBP52 chimeras and mutants for Hsp90 binding and association with progesterone receptor complexes." in: Molecular endocrinology (Baltimore, Md.), Vol. 12, Issue 3, pp. 342-54, 1998 (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).

Loo, Jensen, Cui et al.: "Perturbation of Hsp90 interaction with nascent CFTR prevents its maturation and accelerates its degradation by the proteasome." in: The EMBO journal, Vol. 17, Issue 23, pp. 6879-87, 1999 (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).