Hsp90 Complex antibody

Details for Product No. ABIN361732
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Antigen
Reactivity
Human, Rat (Rattus), Rabbit
(1), (1), (1)
Host
Mouse
(1)
Clonality (Clone)
Monoclonal ()
Application
Immunoprecipitation (IP)
(1)
Pubmed 7 references available
Quantity 200 μg
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Catalog No. ABIN361732
497.20 $
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Immunogen Ah receptor (Aryl hydrocarbon receptor)
Clone 8D3
Isotype IgM
Specificity Immunoprecipitates 90 kDa proteins corresponding to the molecular mass of Hsp90. Co-immunoprecipitates Hsp90 complexes, including Hsp70, Hop, Ah receptors, glucocorticoid receptors, heme-regulated eukaryotic initiation factor 2alpha (eIF-2alpha) kinase (HRI).
Sensitivity Goat anti-mouse IgM was used to bind 25 myl of protein G-Sepharose. SMC-109 IgM from 0.5 ml of high speed supernatant medium was loaded onto the IgG resin and incubated with 100 myl of rabbit reticulocyte lysate for 30 min. at 30C. After washing (4X1 ml), bound proteins were resolved on SDS PAGE, including hsp90, hsp70 and Hop.
Purification PEG Purified
Background Hsp90 is a highly conserved and essential stress protein that is expressed in all eukaryotic cells. From afunctional 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 house keeping functions – including controlling the activity, turnover, andtrafficking 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. 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 outimmuno-adsorption 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 asgeldanamycin and radicicol, inhibit hsp90 function.
Gene ID 3326
NCBI Accession NP_031381
UniProt P08238
Research Area Heat Shock Proteins
Restrictions For Research Use only
Concentration 1 mg/mL
Buffer PBS, 50 % glycerol, 0.09 % sodium azide
Preservative Sodium azide
Precaution of Use This product contains sodium azide: a POISONOUS AND HAZARDOUS SUBSTANCE which should be handled by trained staff only.
Storage -20 °C
Supplier Images
anti-Hsp90 Complex antibody Hsp90 complex (8D3) isolation, IP (rabbit reticulocyte lysate) SDS PAGE Coomassie.
Background publications Dalman, Bresnick, Patel et al.: "Direct evidence that the glucocorticoid receptor binds to hsp90 at or near the termination of receptor translation in vitro." in: The Journal of biological chemistry, Vol. 264, Issue 33, pp. 19815-21, 1989 (PubMed).

Perdew: "Association of the Ah receptor with the 90-kDa heat shock protein." in: The Journal of biological chemistry, Vol. 263, Issue 27, pp. 13802-5, 1988 (PubMed).

Uma, Hartson, Chen et al.: "Hsp90 is obligatory for the heme-regulated eIF-2alpha kinase to acquire and maintain an activable conformation." in: The Journal of biological chemistry, Vol. 272, Issue 17, pp. 11648-56, 1997 (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).

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).

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