Analytical Data
-
Gene name
AHA1
- Application
-
Alternative Names
AHA1；C14orf3；Activator of 90 kDa heat shock Protein ATPase homolog 1
-
Species
Human
-
Source
E. coli
-
Tag
His tag N-Terminus
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
O95433
-
Expression Region
1-338aa
-
AA Sequence
SHMAKWGEGDPRWIVEERADATNVNNWHWTERDASNWSTDKLKTLFLAVQ VQNEEGKCEVTEVSKLDGEASINNRKGKLIFFYEWSVKLNWTGTSKSGVQ YKGHVEIPNLSDENSVDEVEISVSLAKDEPDTNLVALMKEEGVKLLREAM GIYISTLKTEFTQGMILPTMNGESVDPVGQPALKTEERKAKPAPSKTQAR PVGVKIPTCKITLKETFLTSPEELYRVFTTQELVQAFTHAPATLEADRGG KFHMVDGNVSGEFTDLVPEKHIVMKWRFKSWPEGHFATITLTFIDKNGET ELCMEGRGIPAPEEERTRQGWQRYYFEGIKQTFGYGARLF
-
Molecular Weight
38 kDa
-
Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
-
Form
Freeze-dried powder
-
Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
-
Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
-
Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
-
Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
-
Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
Related Products
Protein Description
AHA1 (Activating HSP90 ATPase Activity Protein 1) is a co-chaperone that plays a critical role in the regulation of the heat shock protein 90 (HSP90) molecular chaperone complex, which is essential for the proper folding, maturation, and stabilization of a variety of client proteins involved in essential cellular processes, including signal transduction, cell cycle regulation, and apoptosis. Research on AHA1 has surged due to its potential implications in cancer biology, neurodegenerative diseases, and other pathologies characterized by protein misfolding. The protein enhances the ATPase activity of HSP90, promoting client protein maturation, which is crucial for the function of many oncogenic proteins. The overexpression of AHA1 has been associated with poor prognosis in various cancers, making it an attractive target for therapeutic interventions. Due to its significant role in modulating HSP90 activity, AHA1 is also being investigated as a potential biomarker for disease progression and response to HSP90 inhibitors, which are emerging as promising anti-cancer agents. Recent studies have aimed at elucidating the molecular mechanisms underlying AHA1's function, enhancing our understanding of the broader chaperone network, and exploring its interactions with different client proteins. Overall, the study of AHA1 represents a rapidly evolving field that may provide insights into novel therapeutic strategies for cancer and other diseases linked to protein homeostasis.
