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Mouse Anti-ATOX1 Recombinant Antibody (S76-8) (CBMAB-AP501LY)


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Summary

Host Animal
Mouse
Specificity
Human, Mouse, Rat
Clone
S76-8
Antibody Isotype
IgG2b
Application
ICC, IF, IHC, IP, WB

Basic Information

Immunogen
Synthetic peptide amino acids 164-197 of mouse Ataxin-1.
Specificity
Human, Mouse, Rat
Antibody Isotype
IgG2b
Clonality
Monoclonal
Application Notes
The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.
ApplicationNote
WB1:1,000
IF(ICC)1:100

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

Format
Liquid
Buffer
PBS, pH 7.4, 50% Glycerol
Preservative
0.1% sodium azide
Concentration
1 mg/ml
Storage
Store at +4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freezethaw cycles.

Target

Full Name
Antioxidant 1 Copper Chaperone
Introduction
This gene encodes a copper chaperone that plays a role in copper homeostasis by binding and transporting cytosolic copper to ATPase proteins in the trans-Golgi network for later incorporation to the ceruloplasmin. This protein also functions as an antioxidant against superoxide and hydrogen peroxide, and therefore, may play a significant role in cancer carcinogenesis. Because of its cytogenetic location, this gene represents a candidate gene for 5q-syndrome. [provided by RefSeq, Jul 2008]
Entrez Gene ID
Human475
Mouse11927
Rat84355
UniProt ID
HumanO00244
MouseO08997
RatQ9WUC4
Alternative Names
Antioxidant 1 Copper Chaperone; Metal Transport Protein ATX1; HAH1; ATX1 (Antioxidant Protein 1, Yeast) Homolog 1; ATX1 Antioxidant Protein 1 Homolog (Yeast); ATX1 Antioxidant Protein 1 Homolog; Copper Transport Protein ATOX1; ATX1;
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
More Infomation

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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