HSP90AA1 Antikörper
Kurzübersicht für HSP90AA1 Antikörper (ABIN452367)
Target
Alle HSP90AA1 Antikörper anzeigenReaktivität
Wirt
Klonalität
Konjugat
Applikation
Klon
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Spezifität
- This antibody recognizes 90 kDa proteins corresponding to the molecular mass of hsp90. Hsp90alpha specific for human samples. Can isolate complexes of hsp90, Src kinase and cdc37 (1, 2, 3).
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Kreuzreaktivität (Details)
- Species reactivity (tested):Bovine, Chicken, Human, Mouse, Porcine (Pig), Rat, Rabbit.
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Produktmerkmale
- Synonyms: HSP90A, HSPC1, HSPCA, Heat shock 86 kDa, HSP86, NY-REN-38, Heat shock protein HSP90-alpha
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Aufreinigung
- Purified
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Immunogen
- Full length protein purified from chicken brain, clone D7α
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Isotyp
- IgG1
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Applikationshinweise
- Immunoprecipitation (1, 2, 3): 5 μg with 20 μL Protein A beads. Immunohistochemistry on frozen sections.
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Beschränkungen
- Nur für Forschungszwecke einsetzbar
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Konzentration
- 1.0 mg/mL
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Buffer
- Mouse IgG in PBS buffer, 0.09 % sodium azide and 50 % glycerol
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Konservierungsmittel
- Sodium azide
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Vorsichtsmaßnahmen
- This product contains sodium azide: a POISONOUS AND HAZARDOUS SUBSTANCE which should be handled by trained staff only.
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Lagerung
- 4 °C/-20 °C
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Informationen zur Lagerung
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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. -
Haltbarkeit
- 12 months
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- HSP90AA1 (Heat Shock Protein 90kDa alpha (Cytosolic), Class A Member 1 (HSP90AA1))
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Andere Bezeichnung
- HSP90AA1 / HSP90 alpha
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Hintergrund
- Hsp90 is a highly conserved and essential stress protein that is expressed in all eukaryotic cells. From a functional perspective, hsp90 participates in the folding, assembly, maturation, and stabilization of specific proteins as an integral component of a chaperone complex (4-7). 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 (8-9). The number of proteins now known 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(6). 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 immune-oadsorption 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 (10).Synonyms: HSP86, HSP90A, HSPC1, HSPCA, Heat shock 86 kDa, Heat shock protein HSP 90-alpha, NY-REN-38
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Gen-ID
- 3320
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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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