Human Recombinant ATOX1 protein, His Tag (V2LY-0526-LY2198)

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Basic Information

Expressed Host
E. coli
Protein Species
Human
Tag
His Tag
Protein Construction
This product is Human Recombinant ATOX1 protein, His Tag consist of Amino Acid: 1-68 and predicts a molecular mass of 9.6 kDa.
Molecule Mass
9.6 kDa
Sequence
Amino Acid: 1-68
Species
Human

Formulations & Storage [For reference only, actual COA shall prevail!]

Purity
>90% as determined by SDS-PAGE
Endotoxin
Please contact us for more information.
Format
Lyophilized
Reconstitution
Allow the vial and reconstitution buffer to equilibrate to room temperature. Briefly centrifuge or tap down the vial to ensure that all lyophilized powder is collected at the bottom of the vial. For the reconstitution of this product, we recommend adding PBS or sterile water to achieve a final antibody concentration of 1 mg/mL. Allow the vial to reconstitute for 10-15 minutes at room temperature with gentle agitation. Avoid vigorous shaking that can cause foaming and antibody denaturation. Aliquot into volumes based on your experiment and store liquid protein at -20°C or -80°C for long time.
Buffer
Lyophilized from sterile PBS
Preservative
None
Storage
Samples are stable for up to twelve months from date of receipt at -20°C to -80°C. Store it under sterile conditions at -20°C to -80°C. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
More Infomation

Target

Full Name
Antioxidant 1 Copper Chaperone
Function
Binds and deliver cytosolic copper to the copper ATPase proteins. May be important in cellular antioxidant defense.
Biological Process
Cellular copper ion homeostasis Source: GO_Central
Copper ion transport Source: UniProtKB
Response to oxidative stress Source: GO_Central
Cellular Location
Cytosol

Blockhuys, S., Zhang, X., & Wittung-Stafshede, P. (2020). Single-cell tracking demonstrates copper chaperone Atox1 to be required for breast cancer cell migration. Proceedings of the National Academy of Sciences, 117(4), 2014-2019.

Horvath, I., Blockhuys, S., Šulskis, D., Holgersson, S., Kumar, R., Burmann, B. M., & Wittung-Stafshede, P. (2019). Interaction between copper chaperone Atox1 and Parkinson’s disease protein α-Synuclein includes metal-binding sites and occurs in living cells. ACS chemical neuroscience, 10(11), 4659-4668.

Nardella, M. I., Rosato, A., Belviso, B. D., Caliandro, R., Natile, G., & Arnesano, F. (2019). Oxidation of Human Copper Chaperone Atox1 and Disulfide Bond Cleavage by Cisplatin and Glutathione. International journal of molecular sciences, 20(18), 4390.

Das, A., Sudhahar, V., Ushio-Fukai, M., & Fukai, T. (2019). Novel interaction of antioxidant-1 with TRAF4: role in inflammatory responses in endothelial cells. American Journal of Physiology-Cell Physiology, 317(6), C1161-C1171.

Dzebo, M. M., Blockhuys, S., Valenzuela, S., Celauro, E., Esbjörner, E. K., & Wittung-Stafshede, P. (2018). Copper chaperone Atox1 interacts with cell cycle proteins. Computational and structural biotechnology journal, 16, 443-449.

Kamiya, T., Takeuchi, K., Fukudome, S., Hara, H., & Adachi, T. (2018). Copper chaperone antioxidant-1, Atox-1, is involved in the induction of SOD3 in THP-1 cells. Biometals, 31(1), 61-68.

Hatori, Y., Inouye, S., & Akagi, R. (2017). Thiol‐based copper handling by the copper chaperone Atox1. IUBMB life, 69(4), 246-254.

Blockhuys, S., & Wittung-Stafshede, P. (2017). Copper chaperone Atox1 plays role in breast cancer cell migration. Biochemical and biophysical research communications, 483(1), 301-304.

Celauro, E., Mukaj, A., Fierro-González, J. C., & Wittung-Stafshede, P. (2017). Copper chaperone ATOX1 regulates pluripotency factor OCT4 in preimplantation mouse embryos. Biochemical and biophysical research communications, 491(1), 147-153.

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For research use only. Not intended for any clinical use.

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