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AHA1 Protein

CAT: 0400-SPR-300BSize: 100 µgDry Ice: NoHazardous: No
CAT#:0400-SPR-300BSize:100 µg
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AVAILABILITY: InStock
24/48H Stock Items & 2 to 6 Weeks non Stock Items.
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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.
Description
Human Recombinant AHA1 Protein
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
0.1
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.
Location
Cytoplasm
AA Sequence
SHMAKWGEGDPRWIVEERADATNVNNWHWTERDASNWSTDKLKTLFLAVQVQNEEGKCEVTEVSKLDGEASINNRKGKLIFFYEWSVKLNWTGTSKSGVQYKGHVEIPNLSDENSVDEVEISVSLAKDEPDTNLVALMKEEGVKLLREAMGIYISTLKTEFTQGMILPTMNGESVDPVGQPALKTEERKAKPAPSKTQARPVGVKIPTCKITLKETFLTSPEELYRVFTTQELVQAFTHAPATLEADRGGKFHMVDGNVSGEFTDLVPEKHIVMKWRFKSWPEGHFATITLTFIDKNGETELCMEGRGIPAPEEERTRQGWQRYYFEGIKQTFGYGARLF
Immunogen Species
Human
Product MSDS
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