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

Details for Product No. ABIN263945
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Antigen
Synonyms htpG, 86kDa, 89kDa, AL024080, AL024147, Hsp86-1, Hsp89, Hsp90, Hspca, hsp4, Hsp86, HSP90AA1, HSPCA, EL52, HSP86, HSP89A, HSP90A, HSP90N, HSPC1, HSPCAL1, HSPCAL4, HSPN, LAP2, HSP90
Reactivity
Human, Rat (Rattus)
(88), (55), (38), (10), (8), (8), (5), (4), (4), (3), (2), (2), (2), (1), (1), (1), (1)
Host
Mouse
(61), (44), (3), (2)
Clonality (Clone)
Monoclonal ()
Conjugate
Un-conjugated
(2), (1)
Application
Immunohistochemistry (Frozen Sections) (IHC (fro)), Enzyme Immunoassay (EIA), Immunoprecipitation (IP), Western Blotting (WB)
(102), (32), (31), (29), (29), (28), (17), (13), (12), (7), (6), (1)
Pubmed 8 references available
Quantity 25 μg
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Catalog No. ABIN263945
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Immunogen Recombinant Human HSP90 alpha.
Clone Hyb-K41009
Isotype IgG2a
Specificity Detects 90 kDa proteins corresponding to the molecular mass of HSP90alpha.
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 understood to exist in two principal forms alpha and beta, which share 85 % sequence amino acid homology. The two isoforms of Hsp90 are expressed in the cytosolic compartment (1). Despite the similarities, HSP90A exists predominantly as a homodimer while HSP90B exists mainly as a monomer.(2) From a functional perspective, hsp90 participates in the folding, assembly, maturation, and stabilization of specific proteins as an integral component of a chaperone complex. (3-6) Furthermore, Hsp90 is highly conserved between species, having 60 % and 78 % amino acid similarity between mammalian and the corresponding yeast and Drosophila proteins, respectively. Hsp90 is a highly conserved and essential stress protein that is expressed in all eukaryotic cells. 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 (7-8). 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-hhaperones 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 (9).Synonyms: HSP86, HSP90A, HSPC1, HSPCA, Heat shock 86 kDa, Heat shock protein HSP 90-alpha, NY-REN-38
UniProt P07900
Application Notes ELISA (Ref.10). Immunoprecipitation. Immunohistochemistry (Ref.10). Western blot : 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
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
Precaution of Use This product contains sodium azide: a POISONOUS AND HAZARDOUS SUBSTANCE which should be handled by trained staff only.
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).

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