AHA1 Protein

Human Recombinant AHA1 Protein

Product Specifications

Background

AHA1 (Activator of HSP90 ATPase 1) is a co-chaperone that enhances the ATPase activity of HSP90, accelerating its chaperone cycle and modulating the folding of client proteins. In the nervous system, AHA1 plays a critical role in regulating the stability and function of proteins involved in synaptic signaling, neuronal development, and stress responses. In neurodegenerative diseases, AHA1 has been implicated in the processing of aggregation-prone proteins such as tau and huntingtin. By stimulating HSP90 activity, AHA1 can influence the folding and degradation of these proteins, potentially affecting their accumulation and toxicity. Dysregulation of AHA1 expression or function may contribute to proteostasis imbalance, a hallmark of disorders like Alzheimer’s and Huntington’s disease. AHA1’s role in modulating the chaperone machinery makes it a promising target for therapeutic strategies aimed at restoring protein homeostasis in neurodegeneration. Its activity may also serve as a biomarker for cellular stress and chaperone system dynamics in the aging brain.

Product Name Alternative

AHSA1, AHA1, HSPC322, p38, C14orf3, LOC10598, Activator of Hsp90 ATPase activity 1, Activator of 90 kDa heat shock protein ATPase homolog 1

UNSPSC

12352202

UN Code

Non-hazardous

Hazard Statement

Non-hazardous

Gene ID

10598

Swiss Prot

O95433

Accession Number

NP_036243.1

Cellular Locus

Cytoplasm

Expression System

E. coli

Host

E. coli

Origin Species

Human

Target

AHA1

Conjugation

No tag

Nature

Recombinant

Sequence

SHMAKWGEGDPRWIVEERADATNVNNWHWTERDASNWSTDKLKTLFLAVQVQNEEGKCEVTEVSKLDGEASINNRKGKLIFFYEWSVKLNWTGTSKSGVQYKGHVEIPNLSDENSVDEVEISVSLAKDEPDTNLVALMKEEGVKLLREAMGIYISTLKTEFTQGMILPTMNGESVDPVGQPALKTEERKAKPAPSKTQARPVGVKIPTCKITLKETFLTSPEELYRVFTTQELVQAFTHAPATLEADRGGKFHMVDGNVSGEFTDLVPEKHIVMKWRFKSWPEGHFATITLTFIDKNGETELCMEGRGIPAPEEERTRQGWQRYYFEGIKQTFGYGARLF

Applications

WB | SDS-PAGE | Functional Assay

Field of Research

Cancer | Heat Shock | Cell Signaling | Protein Trafficking | Chaperone Proteins

Purification Method

Multi-Step Purified

Purification

Multi-Step Purified

Limit Of Detection

This product has been certified >90% pure using SDS PAGE analysis. 2uM SPR-300 generated a 9-fold ATPase activation of 2uM HSP90 (His-tagged HSP90 beta) in 33mM Hepes pH7.2, 30mM NaCl, 5mM MgCl2, 1mM DTT, 1.5mM ATP in a 100ul reaction at 37 degrees C. (This is an enzyme-linked ATP regeneration assay tracking loss of NADH absorbance at 340nm.)

Concentration

Lot/batch specific. See included datasheet.

Purity

>90%

Weight

0.05

Buffer

20mM HEPES buffer pH7.2, 80mM NaCl, 10% glycerol

Molecular Weight

~38 kDa

Precautions

Not for use in humans. Not for use in diagnostics or therapeutics. For research use only.

References & Citations

1. Hainzl O., Lapina M.C., Buchner J., Richter K. (2009) J Biol Chem. Epub. 2. Harst A., Lin H., Obermann W.M. (2005) Biochem J. 387 (pt.3): 789-796. 3. Lotz G.P., Brychzy A., Heinz S., Obermann W.M. (2008) J Cell Sci. 121(pt.5): 717-723. 4. Holmes J.L., Sharp S.Y., Hobbs S., Workman P. (2008) Cancer Res. 68(4): 1188-1197.

Shipping Conditions

Blue Ice or 4ºC

Storage Conditions

-20ºC

Background Reference 01

1. Hainzl O., Lapina M.C., Buchner J., Richter K. (2009) J Biol Chem. Epub. 2. Harst A., Lin H., Obermann W.M. (2005) Biochem J. 387 (pt.3) : 789-796. 3. Lotz G.P., Brychzy A., Heinz S., Obermann W.M. (2008) J Cell Sci. 121 (pt.5) : 717-723. 4. Holmes J.L., Sharp S.Y., Hobbs S., Workman P. (2008) Cancer Res. 68 (4) : 1188-1197.