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HSP90 antibody (Heat Shock Protein 90)

Details for Product anti-HSP90 Antibody No. ABIN361732, Supplier: Login to see
Antigen
Reactivity
Human, Mouse (Murine), Rabbit, Rat (Rattus)
269
165
158
93
69
36
23
21
21
19
19
18
18
18
9
5
3
3
3
2
2
2
2
2
2
1
1
1
1
1
Host
Mouse
194
110
7
1
Clonality (Clone)
Monoclonal ()
Conjugate
This HSP90 antibody is un-conjugated
11
11
9
9
9
9
9
9
9
9
9
9
9
9
9
9
8
2
2
Application
Immunocytochemistry (ICC), Immunofluorescence (IF), Immunoprecipitation (IP)
276
193
179
166
125
117
37
6
2
2
2
Supplier
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Immunogen Ah receptor (Aryl hydrocarbon receptor)
Clone 8D3
Specificity Detects 90 kDa. Co-immunoprecipitates HSP90 complexes, including HSP70, Hop, Ah receptors, glucocorticoid receptors, heme-regulated eukaryotic initiation factor 2α (eIF-2α) 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
Alternative Name HSP90 (HSP90 Antibody Abstract)
Background 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 (7).
Cellular Localization: Cytoplasm | Melanosome
Gene ID 3326
NCBI Accession NP_031381
UniProt P08238
Pathways
Application Notes Recommended Dilution: ICC/IF (1:100), IP (1:1000), optimal dilutions for assays should be determined by the user.
Restrictions For Research Use only
Format Liquid
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
 image for anti-HSP90 antibody (Heat Shock Protein 90) (ABIN361732) Hsp90 complex (8D3) isolation, IP (rabbit reticulocyte lysate) SDS PAGE Coomassie.
Product cited in: Shimamura, Perera, Foley et al.: "Ganetespib (STA-9090), a nongeldanamycin HSP90 inhibitor, has potent antitumor activity in in vitro and in vivo models of non-small cell lung cancer." in: Clinical cancer research : an official journal of the American Association for Cancer Research, Vol. 18, Issue 18, pp. 4973-85, 2012 (PubMed).

Ardi, Alexander, Johnson et al.: "Macrocycles that inhibit the binding between heat shock protein 90 and TPR-containing proteins." in: ACS chemical biology, Vol. 6, Issue 12, pp. 1357-66, 2011 (PubMed).

Background publications 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).

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).

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

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

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

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).

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).

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).