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Cochaperone that stimulates HSP90 ATPase activity (By similarity).
Showing 10 out of 12 products:
Human AHSA1 Protein expressed in Escherichia coli (E. coli) - ABIN1686715
Hainzl, Lapina, Buchner, Richter: The charged linker region is an important regulator of Hsp90 function. in The Journal of biological chemistry 2009
Show all 5 Pubmed References
The chaperone proteins Ahsa1 and Hsp90 (show HSP90 Proteins) promote severe craniofacial phenotypes in zebrafish model of HDR (show GATA3 Proteins) syndrome.
Aha1 colocalized with tau pathology in brain tissue, and this association positively correlated with Alzheimer disease progression.
These results suggest that differences in the middle domain of Hsp90alpha (show HSP90AA2 Proteins) and Hsp90beta (show HSP90AB1 Proteins) may be responsible for the isoform-specific interactions with selected proteins.
Aha1 may promote disposal of folding defective proteins by the cellular protein quality control.
a monoallelic mutation of p53 (show TP53 Proteins) was sufficient to activate the Aha1/Hsp90 (show HSP90 Proteins) ATPase axis leading to stimulation of Wnt (show WNT2 Proteins) signaling and increased expression of Wnt (show WNT2 Proteins) target genes.
Modulation of Hsp90 (show HSP90 Proteins) activity by AHA1 regulates VEGF (show VEGFA Proteins) signaling to eNOS (show NOS3 Proteins) and angiogenesis.
The interaction of Aha1 with Hsp90 (show HSP90 Proteins) and its co-chaperones in rabbit reticulocyte lysate (RRL) and in HeLa cell extracts, was characterized.
Hsp90 phosphorylation on tyrosine313 promotes recruitment of AHA1, which stimulates Hsp90 ATPase activity, furthering the chaperoning process.
Data propose a model for Aha1 in the Hsp90 ATPase cycle where Aha1 regulates dwell time of Hsp90, and suggest Aha1 activity integrates chaperone function with client folding energetics by modulating ATPase sensitive dimer structural transitions.
stimulates the inherent ATPase activity of Hsp90 (show HSP90 Proteins)
Hsp90 (show HSP90 Proteins) cochaperones modulate Hsp90 (show HSP90 Proteins)-dependent stability of CFTR (show CFTR Proteins) protein folding in the endoplasmic reticulum
Cochaperone that stimulates HSP90 ATPase activity (By similarity). May affect a step in the endoplasmic reticulum to Golgi trafficking.
activator of heat shock 90kDa protein ATPase homolog 1
, AHA1, activator of heat shock 90kDa protein ATPase homolog 1 (yeast)
, AHA1, activator of heat shock 90kDa protein ATPase homolog 1
, AHA1, activator of heat shock protein ATPase homolog 1
, activator of heat shock 90kDa protein ATPase homolog 1-like
, activator of 90 kDa heat shock protein ATPase homolog 1-like
, activator of 90 kDa heat shock protein ATPase homolog 1
, uncharacterized protein LOC681996