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

Details for Product anti-HSP90AA1 Antibody No. ABIN263957, Supplier: Log in to see
  • htpG
  • 86kDa
  • 89kDa
  • AL024080
  • AL024147
  • Hsp86-1
  • Hsp89
  • Hsp90
  • Hspca
  • hsp4
  • Hsp86
  • HSP90AA1
  • EL52
  • HSP86
  • HSP89A
  • HSP90A
  • HSP90N
  • HSPC1
  • HSPN
  • LAP2
  • HSP90
  • Heat Shock Protein 90, cytosolic
  • heat shock protein 90A
  • molecular chaperone
  • heat shock protein 90, alpha (cytosolic), class A member 1
  • heat shock protein 90kDa alpha (cytosolic), class A member 1
  • HSP90A
  • hsp90A
  • Hsp90aa1
  • Hsp90a
  • HSP90AA1
anti-Human HSP90AA1 antibody for Western Blotting
Human, Rat (Rattus), Yeast (Saccharomyces cerevisiae), Schizosaccharomyces pombe
Clonality (Clone)
Monoclonal ()
This HSP90AA1 antibody is un-conjugated
Enzyme Immunoassay (EIA), Immunohistochemistry (Frozen Sections) (IHC (fro)), Western Blotting (WB)
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Immunogen Recombinant Human hsp90 alpha
Clone Hyb-K41220A
Isotype IgG2a
Specificity This antibody detects 90 kDa proteins corresponding to the Molecular Mass of HSP90 alpha or beta.
Characteristics Synonyms: HSP90AB1, HSP90B, HSPC2, HSPCB, HSP84, HSP-90, HSP-84, Heat shock protein HSP90-beta, HSP90AA1, HSP90A, HSPC1, HSPCA, HSP86, HSP-86, Renal carcinoma antigenNY-REN-38, Heat shock protein HSP 90-alpha
Purification Affinity Chromatography on Protein G
Alternative Name HSP90AA1 / HSP90 alpha (HSP90AA1 Antibody Abstract)
Background HSP90 is an abundantly and ubiquitously expressed heat shock protein. It is understood to exist in two principal forms α and β, which share 85 % sequence amino acid homology. The two isoforms of Hsp90 are expressed in the cytosolic compartment (1). Despite the similarities, HSP90α exists predominantly as a homodimer while HSP90β 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-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 (9).Synonyms: HSP-84, HSP-86, HSP-90, HSP84, HSP86, HSP90A, HSP90AA1, HSP90AB1, HSP90B, HSPC1, HSPC2, HSPCA, HSPCB, Heat shock protein HSP 90-alpha, Heat shock protein HSP 90-beta, Renal carcinoma antigen NY-REN-38
Gene ID 3320
UniProt P07900
Pathways M Phase
Application Notes ELISA. Western blot: 1 μg/mL was sufficient for detection of Hsp90alpha/beta by Western Blot in20 μg of HeLa lysate. (Ref.1, 10)Immunohistochemistry on Frozen Sections.
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, 0.09 % Sodium Azide, 50 % Glycerol
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 4 °C/-20 °C
Storage Comment Store the antibody undiluted at 2-8 °C for one month or (in aliquots) at -20 °C for longer. Avoid repeated freezing and thawing.
Shelf life: one year from despatch.
Expiry Date 12 months
Supplier Images
Western Blotting (WB) image for anti-HSP90AA1 antibody (Heat Shock Protein 90kDa alpha (Cytosolic), Class A Member 1) (ABIN263957) anti-Heat Shock Protein 90kDa alpha (Cytosolic), Class A Member 1 (HSP90AA1) antibody
Background publications Kishimoto, Fukuma, Mizuno, Nemoto: "Identification of the pentapeptide constituting a dominant epitope common to all eukaryotic heat shock protein 90 molecular chaperones." in: Cell stress & chaperones, Vol. 10, Issue 4, pp. 296-311, 2005 (PubMed).

Arlander, Eapen, Vroman, McDonald, Toft, Karnitz: "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).

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).

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).

Whitesell, Mimnaugh, De Costa, Myers, Neckers: "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).

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).