Heat Shock Protein 90kDa alpha (Cytosolic), Class B Member 1 (HSP90AB1) antibody

Antigen: Heat Shock Protein 90kDa alpha (Cytosolic), Class B Member 1 (HSP90AB1)

Synonyms: hsp90b

Clonality: Polyclonal

Host: Rabbit

Reactivity: Human, Rat (Rattus), Mouse (Murine)

Conjugate: Un-conjugated

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

Catalog no.: ABIN361849

Additional Information

Alternative name: Hsp90beta

Gene ID: 3326

UniProt: P08238

Immunogen: Full length protein Hsp90

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. 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: Hsp84, Hsp90, Hsp86, Hsp89, Hsp90B, Hsp90BETA, Hsp90N, HSPC2, HSPCA, HSPCAL1, HSPCB, HSPN, LAP2, NY REN 38 antigen

Characteristics: Accession Number: NP_031381.2

Specificity: Hsp90beta. Does not cross-react with Hsp90alpha.

Application Details

Application Notes: 1:20000-40000 (ECL) (WB)

Purification: Rabbit antiserum

Storage: Store at -20° C. Shipping Temperature: 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

Cell line mix, Western Blotting 1 in 2000 Hsp90beta.

Publications

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).

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).