Analytical Data
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Gene name
ATOX1
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简介
ATOX1 Protein plays a crucial role in cellular copper transport, binding to and delivering cytosolic copper to copper ATPase proteins. This process is integral to cellular antioxidant defense mechanisms. ATOX1 functions as a homodimer, supported by research findings. It interacts with ATP7B and ATP7A. In its dimer form, ATOX1 interacts with SLC31A1, contributing to its stability and controlling intracellular Cu(I) levels. ATOX1 Protein, Human (His) is the recombinant human-derived ATOX1 protein, expressed by E. coli , with N-His labeled tag.
- Application
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Alternative Names
Copper transport protein ATOX1; Metal transport protein ATX1; HAH1
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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 95% as determined by SDS-PAGE.
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Uniprot
O00244
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Expression Region
M1-E68
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Protein Length
Full Length
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Molecular Weight
9 kDa
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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
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Protein Description
ATOX1, a member of the copper chaperone family, plays a pivotal role in cellular copper homeostasis by mediating the transport of copper ions to target proteins, particularly in the context of copper delivery to the enzyme cytochrome c oxidase. As a highly conserved protein, ATOX1 is expressed in various tissues and has been identified as a key player in oxidative stress responses and cellular signaling pathways. Recent studies have highlighted its involvement in cancer biology, specifically in tumor progression and metastasis, due to its ability to regulate copper-dependent processes. The recombinant expression of ATOX1 allows for detailed investigations into its biochemical properties, interactions, and regulatory mechanisms. By producing ATOX1 as a recombinant protein, researchers can elucidate its function and potential as a therapeutic target in diseases characterized by copper dysregulation, including neurodegenerative disorders and cancer. Understanding the structure-function relationship of ATOX1 through recombinant techniques may pave the way for innovative strategies to modulate its activity, thereby offering insights into novel therapeutic avenues that leverage copper's role in cellular metabolism.
