Analytical Data
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Gene name
ACHAP
- Application
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Alternative Names
CUTA; C6orf82; CutA Divalent Cation Tolerance Homolog; Brain acetylcholinesterase putative membrane anchor
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Species
Human
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Source
E. coli
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Tag
N-His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
O60888
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Expression Region
Arg33~Pro179
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Molecular Weight
24kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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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.
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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.
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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
ACHAP (Arsenate- and Cadmium-induced HSP70-Associated Protein) has garnered considerable attention in recent years due to its crucial role in stress response mechanisms in various organisms. As a member of the heat shock protein family, ACHAP is implicated in cellular protection against environmental stresses such as heavy metal exposure, including arsenate and cadmium, which are known to cause significant cellular damage. This protein functions as a molecular chaperone, facilitating the correct folding of proteins, mitigating aggregation, and promoting cell survival under stress conditions. The understanding of ACHAP's structure and function is vital for uncovering its potential applications in bioremediation and biotechnology, especially in areas related to environmental health and the development of stress-resistant crops. Research has been focused on elucidating the molecular mechanisms by which ACHAP interacts with other cellular proteins and its regulatory pathways, providing insights not only into its biological significance but also into the broader implications of stress response in environmental adaptability. Furthermore, advancements in recombinant protein technology have allowed for the production of ACHAP, enabling detailed studies of its properties and functions, thus paving the way for innovative approaches in mitigating the effects of heavy metal contamination. The ongoing exploration of ACHAP and its pathways continues to be a promising frontier in molecular biology, with potential impacts on agricultural sustainability and environmental conservation.
