AHA1 Antibody [L18K15] Datasheet

Biological Description

Specificity	AHA1 Antibody [L18K15] detects endogenous levels of total AHA1 protein.
Background	AHA1 (AHSA1; activator of Hsp90 ATPase 1) is a conserved co‑chaperone that binds the molecular chaperone Hsp90 and functions as the most potent endogenous accelerator of its ATPase activity, thereby modulating the kinetics and outcome of Hsp90‑dependent client protein folding, stabilization, and maturation across many cellular pathways. The protein is organized into an N‑terminal domain that docks onto the middle domain of Hsp90 and a C‑terminal domain that contacts the N‑terminal ATPase domain, and this bipartite engagement promotes a conformational switch in Hsp90 that enhances ATP binding, accelerates ATP hydrolysis, and stabilizes the closed, catalytically competent state of the chaperone cycle. By stimulating Hsp90 ATPase activity, AHA1 shortens the dwell time of client proteins within specific chaperone states and shifts the balance between Hsp90 complexes that include other co‑chaperones such as p23, Hop, and Cdc37, which positions AHA1 as a key determinant of how Hsp90 handles kinases, transcription factors, and other signaling proteins involved in cell proliferation, survival, and differentiation. AHA1 associates with large Hsp90-centered heteroprotein assemblies that contain multiple clients and regulatory factors, and its expression level influences the maturation and stability of oncogenic clients including tyrosine kinases, steroid hormone receptors, and cell-cycle regulators, linking elevated AHA1 activity to enhanced prosurvival signaling and therapy resistance in several tumor types. In neuronal systems, AHA1 contributes to the handling of aggregation-prone proteins such as tau and huntingtin by modulating Hsp90’s chaperone and degradation decisions, and altered AHA1 abundance or activity is reported in models of Alzheimer’s, Huntington’s disease, and other proteinopathy-linked neurodegenerative conditions where proteostasis is impaired. AHA1 can bind stress-denatured proteins directly and delay their aggregation in the absence of Hsp90, indicating autonomous chaperone activity that broadens its impact on cellular protein quality control under stress. AHA1 also participates in the biogenesis and function of Dicer1 and thereby influences microRNA maturation, adding a layer of post-transcriptional gene regulation to its effects on chaperone-dependent proteomes and connecting AHA1 to pathways that govern cell identity, oncogenic transformation, and neuronal resilience. Dysregulated AHA1 expression in cancer and neurodegeneration correlates with disrupted client handling and disease progression, and small-molecule disruptors of the Hsp90–AHA1 interaction or inhibitors of AHA1 function show efficacy in experimental models by rebalancing Hsp90 client networks.

Specificity

AHA1 Antibody [L18K15] detects endogenous levels of total AHA1 protein.

Background

AHA1 (AHSA1; activator of Hsp90 ATPase 1) is a conserved co‑chaperone that binds the molecular chaperone Hsp90 and functions as the most potent endogenous accelerator of its ATPase activity, thereby modulating the kinetics and outcome of Hsp90‑dependent client protein folding, stabilization, and maturation across many cellular pathways. The protein is organized into an N‑terminal domain that docks onto the middle domain of Hsp90 and a C‑terminal domain that contacts the N‑terminal ATPase domain, and this bipartite engagement promotes a conformational switch in Hsp90 that enhances ATP binding, accelerates ATP hydrolysis, and stabilizes the closed, catalytically competent state of the chaperone cycle. By stimulating Hsp90 ATPase activity, AHA1 shortens the dwell time of client proteins within specific chaperone states and shifts the balance between Hsp90 complexes that include other co‑chaperones such as p23, Hop, and Cdc37, which positions AHA1 as a key determinant of how Hsp90 handles kinases, transcription factors, and other signaling proteins involved in cell proliferation, survival, and differentiation. AHA1 associates with large Hsp90-centered heteroprotein assemblies that contain multiple clients and regulatory factors, and its expression level influences the maturation and stability of oncogenic clients including tyrosine kinases, steroid hormone receptors, and cell-cycle regulators, linking elevated AHA1 activity to enhanced prosurvival signaling and therapy resistance in several tumor types. In neuronal systems, AHA1 contributes to the handling of aggregation-prone proteins such as tau and huntingtin by modulating Hsp90’s chaperone and degradation decisions, and altered AHA1 abundance or activity is reported in models of Alzheimer’s, Huntington’s disease, and other proteinopathy-linked neurodegenerative conditions where proteostasis is impaired. AHA1 can bind stress-denatured proteins directly and delay their aggregation in the absence of Hsp90, indicating autonomous chaperone activity that broadens its impact on cellular protein quality control under stress. AHA1 also participates in the biogenesis and function of Dicer1 and thereby influences microRNA maturation, adding a layer of post-transcriptional gene regulation to its effects on chaperone-dependent proteomes and connecting AHA1 to pathways that govern cell identity, oncogenic transformation, and neuronal resilience. Dysregulated AHA1 expression in cancer and neurodegeneration correlates with disrupted client handling and disease progression, and small-molecule disruptors of the Hsp90–AHA1 interaction or inhibitors of AHA1 function show efficacy in experimental models by rebalancing Hsp90 client networks.

Usage Information

Application

WB, IP, IHC, IF, ELISA

Dilution

WB	IP	IHC	IF
1:1000	1:1000	1:100	1:1000

Reactivity

Human, Mouse, Rat

Source

Rat Monoclonal Antibody

MW

38kDa

Storage Buffer

PBS, pH 7.2+50% Glycerol+0.05% BSA+0.01% NaN3

Storage
(from the date of receipt)

-20°C (avoid freeze-thaw cycles), 2 years

References

https://pubmed.ncbi.nlm.nih.gov/27615124/
https://pubmed.ncbi.nlm.nih.gov/39776493/

AHA1 Antibody [L18K15]

Biological Description

Usage Information

References

Application Data