ELISA: 1/35,000 - 1/185,000. Western Blot: 1/500 - 1/3,000. Other applications not tested. Optimal dilutions are dependent on conditions and should be determined by the user.
Beschränkungen
Nur für Forschungszwecke einsetzbar
Konzentration
1.08 mg/mL (by UV absorbance at 280 nm)
Buffer
0.02 M Potassium Phosphate, 0.15 M Sodium Chloride, pH 7.2 containing 0.01 % (w/v) Sodium Azide
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
-20 °C
Target
AHSA1
(Activator of HSP90 ATPase Activity 1 (AHSA1))
ahsa1 antikoerper, MGC52884 antikoerper, MGC132147 antikoerper, MGC80312 antikoerper, AHSA1 antikoerper, MGC89589 antikoerper, wu:fb83b05 antikoerper, zgc:136821 antikoerper, zgc:56075 antikoerper, AHA1 antikoerper, C14orf3 antikoerper, p38 antikoerper, BC023857 antikoerper, AHA1, activator of heat shock 90kDa protein ATPase homolog 1 S homeolog antikoerper, activator of Hsp90 ATPase activity 1 antikoerper, AHA1, activator of heat shock 90kDa protein ATPase homolog 1 L homeolog antikoerper, activator of HSP90 ATPase activity 1 antikoerper, AHA1, activator of heat shock 90kDa protein ATPase homolog 1 antikoerper, AHA1, activator of heat shock protein ATPase homolog 1a antikoerper, AHA1, activator of heat shock 90kDa protein ATPase homolog 1 (yeast) antikoerper, AHA1, activator of heat shock protein ATPase 1 antikoerper, ahsa1.S antikoerper, AHSA1 antikoerper, ahsa1.L antikoerper, ahsa1 antikoerper, ahsa1a antikoerper, Ahsa1 antikoerper
Hintergrund
Activator of Hsp90 ATPase (AHA1) stimulates the inherent ATPase cycle of Hsp90, which is essential for its chaperone activity in vivo. The activation and/or stability of many of the key regulatory and signaling proteins of the eukaryotic cell depend on their interaction with the Hsp90 Molecular chaperone. Hsp90 is assisted and regulated by co-chaperones that participate in an ordered series both to assist clientprotein recruitment or release and to modulate progress through the ATPase coupled chaperone cycle. Structural analysis and mutagenesis show that binding of the N-terminal domain of AHA1 to Hsp90 promotes a conformational switch in the middle-segment catalytic loop (aa 370-390) of Hsp90 that exposes the catalytic Arg380 and enables its interaction with ATP in the N-terminal nucleotide-binding domain of the chaperone. Recent studies show that AHA1 modulates Hsp90-dependent stability of the folding of the cystic fibrosis transmembrane conductance regulator (CFTR) in the endoplasmic reticulum (ER). Down-regulation of AHA1 rescues misfolding of CFTR in cystic fibrosis.Synonyms: Activator of 90 kDa heat shock protein ATPase homolog 1, C14orf3, HSPC322