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Details for Product No. ABIN263945

Heat Shock Protein 90kDa alpha (Cytosolic), Class A Member 1 (HSP90AA1) antibody

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Antigen
Synonyms HSPCA, htpG
Reactivity
»Alternatives Human, Rat (Rattus)
Host
»Alternatives Mouse
Clonality (Clone) Monoclonal ()
Conjugate
»Alternatives Un-conjugated
Application
»Alternatives Immunohistochemistry (Frozen Sections) (IHC (fro)), ELISA, Immunoprecipitation (IP), Western Blotting (WB)
Pubmed 8 references available
Catalog no. ABIN263945
Quantity 25 µg
Price
242.00 $   Plus shipping costs $45.00
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Availability Will be delivered in 6 to 8 Business Days
Immunogen Recombinant Human HSP90 alpha.
Clone Hyb-K41009
Isotype IgG2a
Characteristics Synonyms: HSP90A, HSPC1, HSPCA, Heat shock 86 kDa, HSP86, NY-REN-38, Heat shock protein HSP90-alpha
Purification Affinity Chromatography on Protein G.
Alternative Name HSP90AA1 / HSP90 alpha
Background HSP90 is an abundantly and ubiquitously expressed heat shock protein. It is understoodto exist in two principal forms alpha and beta, which share 85% sequence amino acidhomology. The two isoforms of Hsp90 are expressed in the cytosolic compartment (1). Despite the similarities, HSP90A exists predominantly as a homodimer while HSP90Bexists mainly as a monomer. (2) From a functional perspective, hsp90 participates in thefolding, assembly, maturation, and stabilization of specific proteins as an integralcomponent of a chaperone complex. (3-6) Furthermore, Hsp90 is highly conservedbetween species, having 60% and 78% amino acid similarity between mammalian and thecorresponding yeast and Drosophila proteins, respectively. Hsp90 is a highly conserved and essential stress protein that is expressed in all eukaryoticcells. Despite its label of being a heat-shock protein, hsp90 is one of the most highlyexpressed proteins in unstressed cells (1-2% of cytosolic protein). It carries out a numberof housekeeping functions - including controlling the activity, turnover, and trafficking of avariety of proteins. Most of the hsp90-regulated proteins that have been discovered todate are involved in cell signaling (7-8). The number of proteins now know to interact withHsp90 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 thehepatitis B virus and telomerase. 5 When bound to ATP, Hsp90 interacts withco-hhaperones Cdc37, p23, and an assortment of immunophilin-like proteins, forming acomplex that stabilizes and protects target proteins from proteasomal degradation. In most cases, hsp90-interacting proteins have been shown to co-precipitate with hsp90when carrying out immunoadsorption studies, and to exist in cytosolic heterocomplexeswith it. In a number of cases, variations in hsp90 expression or hsp90 mutation has beenshown to degrade signaling function via the protein or to impair a specific function of theprotein (such as steroid binding, kinase activity) in vivo. Ansamycin antibiotics, such asgeldanamycin and radicicol, inhibit hsp90 function (9).
UniProt P07900
Application Notes ELISA (Ref.10). Immunoprecipitation. Immunohistochemistry (Ref.10). Western blot (Ref.1): 1 µg/ml was sufficient for detection of HSP90-alpha in 20 µg of HeLalysate. Other applications not tested. Optimal dilutions are dependent on conditions and should be determined by the user.
Restrictions For Research Use only
Format Liquid
Concentration 1.0 mg/mL
Buffer PBS pH 7.2 containing 50% Glycerol as stabilizer and 0.09% Sodium Azide as preservative.
Preservative Sodium azide
Storage -20 °C
Storage Comment Store the antibody (in aliquots) at -20°C. Shelf life: one year from despatch.
Expiry Date 12 months
Background publications Garg, Hassid: "Nitric oxide decreases cytosolic free calcium in Balb/c 3T3 fibroblasts by a cyclic GMP-independent mechanism." in: The Journal of biological chemistry, Vol. 266, Issue 1, pp. 9-12, 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).

Lowe: "Colipase stabilizes the lid domain of pancreatic triglyceride lipase." in: The Journal of biological chemistry, Vol. 272, Issue 1, pp. 9-12, 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).

Nemoto, Roi, Matsusaka et al.: "Isoform-specific monoclonal antibodies against HSP90." in: Biochemistry and molecular biology international, Vol. 42, Issue 5, pp. 881-9, 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).

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).

Alternatives for antigen "Heat Shock Protein 90kDa alpha (Cytosolic), Class A Member 1 (HSP90AA1)", type "Antibodies"
Hosts (56), (34), (3), (2)
Reactivities (75), (49), (31), (12), (9), (8), (6), (5), (5), (2), (2), (2), (2), (1), (1), (1)
Applications (89), (37), (31), (27), (25), (24), (13), (10), (5), (2), (2), (1), (1)
Conjugates (2), (2)
Epitopes (10), (8), (5), (3), (2), (2), (1), (1), (1), (1), (1)
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