HSP90AA1 antibody

Catalog No. ABIN453942

Cited in 6+ publications. The Mouse Monoclonal anti-HSP90AA1 antibody (Clone 2G5-G3) (ABIN453942) specifically detects HSP90AA1 in WB, IF, IP, EIA and IHC (fro). The antibody is reactive with Human, Mouse and Rat samples.

Quick Overview for HSP90AA1 antibody (ABIN453942)

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

Reactivity: Human, Mouse, Rat

Host: Mouse

Clonality: Monoclonal

Conjugate: This HSP90AA1 antibody is un-conjugated

Application: Western Blotting (WB), Immunofluorescence (IF), Immunoprecipitation (IP), Enzyme Immunoassay (EIA), Immunohistochemistry (Frozen Sections) (IHC (fro))

Clone: 2G5-G3

Product Details anti-HSP90AA1 Antibody

Cross-Reactivity (Details): Species reactivity (tested):Human, Mouse, Rat.

Characteristics: Synonyms: HSP90A, HSPC1, HSPCA, Heat shock 86 kDa, HSP86, NY-REN-38, Heat shock protein HSP90-alpha

Purification: Protein G Affinity Chromatography

Immunogen: Human Hsp90alpha

Isotype: IgG1

Application Details

Application Notes: Immunopreciüpitation. ELISA. Immunocytochemistry. Immunohistochemistry on frozen sections. Immunflourescence. Western blot: 1/2000.
Other applications not tested.
Optimal dilutions are dependent on conditions and should be determined by the user.

Restrictions: For Research Use only

Handling

Concentration: 1.0 mg/mL

Buffer: PBS pH 7.2, 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: 4 °C/-20 °C

Storage Comment: Store the antibody at 2 - 8 °C up to one month or (in aliquots) at -20 °C for longer. Avoidrepeated freezing and thawing.
Shelf life: one year from despatch.

Expiry Date: 12 months

References for anti-HSP90AA1 antibody (ABIN453942)

Ortega, Calvillo, Luna, Pérez-Severiano, Rubio-Osornio, Guevara, Limón: "17-AAG improves cognitive process and increases heat shock protein response in a model lesion with A?25-35." in: Neuropeptides, Vol. 48, Issue 4, pp. 221-32, (2014) (PubMed).

Quanz, Herbette, Sayarath, de Koning, Dubois, Sun, Dutreix: "Heat shock protein 90? (Hsp90?) is phosphorylated in response to DNA damage and accumulates in repair foci." in: The Journal of biological chemistry, Vol. 287, Issue 12, pp. 8803-15, (2012) (PubMed).

Shimamura, Perera, Foley, Sang, Rodig, Inoue, Chen, Li, Carretero, Li, Sinha, Carey, Borgman, Jimenez, Meyerson, Ying, Barsoum, Wong, Shapiro: "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).

ONeill, Prencipe, Dowling, Fan, Mulrane, Gallagher, OConnor, OConnor, Devery, Corcoran, Rani, ODriscoll, Fitzpatrick, Watson: "Characterisation and manipulation of docetaxel resistant prostate cancer cell lines." in: Molecular cancer, Vol. 10, pp. 126, (2011) (PubMed).

Orthwein, Patenaude, Affar, Lamarre, Young, Di Noia: "Regulation of activation-induced deaminase stability and antibody gene diversification by Hsp90." in: The Journal of experimental medicine, Vol. 207, Issue 12, pp. 2751-65, (2010) (PubMed).

Bason, Corrocher, Lunardi, Puccetti, Olivieri, Girelli, Navone, Beri, Millo, Margonato, Martinelli, Puccetti: "Interaction of antibodies against cytomegalovirus with heat-shock protein 60 in pathogenesis of atherosclerosis." in: Lancet (London, England), Vol. 362, Issue 9400, pp. 1971-7, (2003) (PubMed).

Target Details for HSP90AA1

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

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 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 cochaperones Cdc37, p23, and an assortment of immunophilinlike 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

Gene ID: 3320

UniProt: P07900

Pathways: M Phase, Regulation of Cell Size, Signaling Events mediated by VEGFR1 and VEGFR2, VEGFR1 Specific Signals