Analytical Data
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Gene name
ATOX1
- Application
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Alternative Names
ATOX1；HAH1；Copper transport Protein ATOX1
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
O00244
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Expression Region
1-68aa
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AA Sequence
MPKHEFSVDM TCGGCAEAVS RVLNKLGGVK YDIDLPNKKV CIESEHSMDT LLATLKKTGK TVSYLGLE
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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 copper chaperone protein, plays a crucial role in cellular copper homeostasis and protection against oxidative stress. Its primary function is to transport copper ions to specific target proteins, ensuring that copper is properly utilized in essential cellular processes, such as respiration and antioxidant defense. Dysregulation of copper metabolism can lead to various diseases, including Wilson's disease and Menkes syndrome, highlighting the importance of understanding ATOX1's mechanisms of action. Recent studies have demonstrated that ATOX1 is involved in the cellular response to oxidative damage, suggesting its potential protective role in neurodegenerative diseases and cancer. Furthermore, the recombinant expression of ATOX1 in model organisms and cell cultures has provided insights into its structure-function relationship and interaction with other proteins. The development of ATOX1 as a therapeutic target or biomarker in disease conditions is an area of growing interest, as enhancing its expression or activity could mitigate copper-related toxicity and oxidative stress. Understanding the biochemical pathways in which ATOX1 is involved will not only shed light on its physiological significance but also offer opportunities for novel therapeutic strategies in copper-related disorders and beyond. This area of research continues to evolve, underscoring the need for further investigation into the roles of ATOX1 in health and disease.
