AHA-1 antibody

Cannot supply to this region.

SKU:: GTX48723
Additional Names:: activator of HSP90 ATPase activity 1 , AHA1 , C14orf3 , hAha1 , p38
Application:: ELISA, IHC, WB, IP
Concentration:: 1 mg/ml
Physical State:: Liquid
Species Reactivity:: Human
Purification:: Affinity Purified
Storage Conditions:: -20[o]C Aliquot. Avoid freeze/thaw cycles. Store undiluted., 2-8[o]C Aliquot. Avoid freeze/thaw cycles. Store undiluted., -20[o]C/-70[o]C Aliquot. Avoid freeze/thaw cycles. Store undiluted.
Supplier:: Genetex
Host:: Rabbit
Reactivities:: Human
Buffer:: 20mM Potassium Phosphate, 150mM NaCl, 0.01% Sodium azide.
Immunogen:: Synthetic peptide corresponding to an internal region of human AHA1 protein.
Uniprot:: O95433
Synonyms:: activator of 90 kDa heat shock protein ATPase homolog 1;AHA1;AHA1, activator of heat shock 90kDa protein ATPase homolog 1;C14orf3;hAha1;p38
Extra Details:: 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.

Shipping Conditions:: Blue Ice