Concentration Definition: by UV absorbance at 280 nm
Immunogen
This affinity purified antibody was prepared from whole rabbit serum produced by repeated immunizations with a synthetic peptide corresponding to an of human AHA1 protein.
This affinity purified antibody has been tested for use in ELISA and western blotting. Specific conditions for reactivity should be optimized by the end user. Expect a band approximately 38-40 kDa in size corresponding to AHA1 protein by western blotting in the appropriate cell lysate or extract.
Beschränkungen
Nur für Forschungszwecke einsetzbar
Format
Liquid
Konzentration
1.08 mg/mL
Buffer
0.02 M Potassium Phosphate, 0.15 M Sodium Chloride, pH 7.2
Konservierungsmittel
Sodium azide
Vorsichtsmaßnahmen
This product contains sodium azide: a POISONOUS AND HAZARDOUS SUBSTANCE which should be handled by trained staff only.
Lagerung
-20 °C
Xu, Beebe, Chavez, Boysen, Lu, Zuehlke, Keramisanou, Trepel, Prodromou, Mayer, Bruce, Gelis, Neckers: "Hsp90 middle domain phosphorylation initiates a complex conformational program to recruit the ATPase-stimulating cochaperone Aha1." in: Nature communications, Vol. 10, Issue 1, pp. 2574, (2019) (PubMed).
Woodford, Dunn, Blanden, Capriotti, Loiselle, Prodromou, Panaretou, Hughes, Smith, Ackerman, Haystead, Loh, Bourboulia, Schmidt, Marston Linehan, Bratslavsky, Mollapour: "The FNIP co-chaperones decelerate the Hsp90 chaperone cycle and enhance drug binding." in: Nature communications, Vol. 7, pp. 12037, (2018) (PubMed).
Bachman, Keramisanou, Xu, Beebe, Moses, Vasantha Kumar, Gray, Noor, van der Vaart, Neckers, Gelis: "Phosphorylation induced cochaperone unfolding promotes kinase recruitment and client class-specific Hsp90 phosphorylation." in: Nature communications, Vol. 9, Issue 1, pp. 265, (2018) (PubMed).
Prince, Kijima, Tatokoro, Lee, Tsutsumi, Yim, Rivas, Alarcon, Schwartz, Khamit-Kush, Scroggins, Beebe, Trepel, Neckers: "Client Proteins and Small Molecule Inhibitors Display Distinct Binding Preferences for Constitutive and Stress-Induced HSP90 Isoforms and Their Conformationally Restricted Mutants." in: PLoS ONE, Vol. 10, Issue 10, pp. e0141786, (2016) (PubMed).
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
This antibody is designed, produced, and is suitable for Cancer, Immunology and Nuclear Signaling research. 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 client-protein 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: Aha1, Ahsa1 antibody, Activator of Hsp90 ATPase, Activator of 90 kDa heat shock protein ATPase homolog 1 antibody