HSP90AA1 antibody
Quick Overview for HSP90AA1 antibody (ABIN263945)
Target
See all HSP90AA1 AntibodiesReactivity
Host
Clonality
Conjugate
Application
Clone
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Specificity
- Detects 90 kDa proteins corresponding to the molecular mass of HSP90alpha.
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Characteristics
- Synonyms: HSP90A, HSPC1, HSPCA, Heat shock 86 kDa, HSP86, NY-REN-38, Heat shock protein HSP90-alpha
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Purification
- Affinity Chromatography on Protein G.
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Immunogen
- Recombinant Human HSP90 alpha.
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Isotype
- IgG2a
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Application Notes
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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
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Concentration
- 1.0 mg/mL
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Buffer
- PBS pH 7.2 containing 50 % Glycerol as stabilizer and 0.09 % Sodium Azide as preservative.
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Preservative
- Sodium azide
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Precaution of Use
- This product contains sodium azide: a POISONOUS AND HAZARDOUS SUBSTANCE which should be handled by trained staff only.
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Storage
- -20 °C
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Storage Comment
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Store the antibody (in aliquots) at -20 °C.
Shelf life: one year from despatch. -
Expiry Date
- 12 months
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- HSP90AA1 (Heat Shock Protein 90kDa alpha (Cytosolic), Class A Member 1 (HSP90AA1))
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Alternative Name
- HSP90AA1 / HSP90 alpha
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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
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UniProt
- P07900
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Pathways
- M Phase, Regulation of Cell Size, Signaling Events mediated by VEGFR1 and VEGFR2, VEGFR1 Specific Signals
Target
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