HSP90AA1 Antikörper (Heat Shock Protein 90kDa alpha (Cytosolic), Class A Member 1) (N-Term)

Details for Product anti-HSP90AA1 Antibody No. ABIN614807, Anbieter: Anmelden zum Anzeigen
Antigen
  • 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
  • Heat Shock Protein 90, cytosolic
  • heat shock protein 90A
  • molecular chaperone
  • heat shock protein 90, alpha (cytosolic), class A member 1
  • heat shock protein 90 alpha family class A member 1
  • HSP90A
  • hsp90A
  • Hsp90aa1
  • HSP90AA1
Epitop
N-Term
8
7
5
3
1
1
1
1
1
1
1
1
1
Reaktivität
Rind (Kuh), Human, Maus
81
51
44
9
9
7
6
5
4
4
4
2
2
2
1
1
1
Wirt
Maus
50
31
1
1
Klonalität (Klon)
Monoklonal ()
Konjugat
Dieser HSP90AA1 Antikörper ist unkonjugiert
2
1
1
Applikation
Immunoprecipitation (IP), Western Blotting (WB)
79
31
26
20
17
15
10
6
6
4
2
2
2
1
Optionen
Hersteller
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Hersteller Produkt- Nr.
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Immunogen Peptide within N-terminal part of human Hsp90
Sequenz EEVHHGEEEV EC
Klon MBH90AB
Isotyp IgG1
Spezifität This antibody recognizes the epitope EEEVE within N-terminal part of ubiquitously expressed Hsp90 alpha and Hsp90 beta proteins with calculated Mw of 84.7 kDa and 83.3 kDa, respectively, however, migrating as 90 kDa bands under reducing SDS-PAGE conditions.
Kreuzreaktivität (Details) Species reactivity (tested):Human, Mouse, Bovine
Reinigung Protein-A affinity chromatography
Reinheit > 95 % pure by SDS-PAGE
Andere Bezeichnung HSP90AA1 / HSP90 alpha (HSP90AA1 Antibody Abstract)
Hintergrund Hsp90 (heat shock protein 90) is one of the most abundant chaperones in the cytosol of eukaryotic cells. It interacts with various proteins, including protein kinases and transcription factors, and either facilitates their stabilization and activation or directs them for proteasomal degradation. Hsp90 thus affects multiple signaling pathways and biological processes and modulation of this single target offers the prospect of simultaneous intervence to various key points of oncogenic transformation. Hsp90 operates as a dimer in a conformational cycle driven by ATP binding and hydrolysis. There are two isoforms, alpha and beta, of vertebrate Hsp90. Whereas Hsp90 beta is expressed constitutively to a high level, Hsp90 alpha is stress-inducible and is overexpressed in many cancerous cells.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
Gen-ID 3320
NCBI Accession NP_005339
UniProt P07900
Pathways M Phase, Regulation of Cell Size, Signaling Events mediated by VEGFR1 and VEGFR2, VEGFR1 Specific Signals
Applikationshinweise Optimal working dilution should be determined by the investigator.
Beschränkungen Nur für Forschungszwecke einsetzbar
Konzentration 1.0 mg/mL
Buffer Phosphate buffered saline (PBS) containing 15 mM sodium azide and 0.2 % (w/v) high-grade protease free Bovine Serum Albumin (BSA) as a stabilizing agent
Konservierungsmittel Sodium azide
Vorsichtsmaßnahmen This product contains sodium azide: a POISONOUS AND HAZARDOUS SUBSTANCE which should be handled by trained staff only.
Handhabung Avoid repeated freezing and thawing.
Lagerung 4 °C/-20 °C
Informationen zur Lagerung Store at 2 - 8 °C for up to one month or (in aliquots) at -20 °C for longer.
Bilder des Herstellers
Western Blotting (WB) image for anti-Heat Shock Protein 90kDa alpha (Cytosolic), Class A Member 1 (HSP90AA1) (N-Term) antibody (ABIN614807) anti-Heat Shock Protein 90kDa alpha (Cytosolic), Class A Member 1 (HSP90AA1) (N-Term) antibody
Allgemeine Veröffentlichungen Pearl, Prodromou, Workman: "The Hsp90 molecular chaperone: an open and shut case for treatment." in: The Biochemical journal, Vol. 410, Issue 3, pp. 439-53, 2008 (PubMed).

Millson, Truman, Rácz, Hu, Panaretou, Nuttall, Mollapour, Söti, Piper et al.: "Expressed as the sole Hsp90 of yeast, the alpha and beta isoforms of human Hsp90 differ with regard to their capacities for activation of certain client proteins, whereas only Hsp90beta generates ..." in: The FEBS journal, Vol. 274, Issue 17, pp. 4453-63, 2007 (PubMed).

Hooven, Yamamoto, Jeffery: "Blind cavefish and heat shock protein chaperones: a novel role for hsp90alpha in lens apoptosis." in: The International journal of developmental biology, Vol. 48, Issue 8-9, pp. 731-8, 2004 (PubMed).

Scheibel, Buchner: "The Hsp90 complex--a super-chaperone machine as a novel drug target." in: Biochemical pharmacology, Vol. 56, Issue 6, pp. 675-82, 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).

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