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CCS Matched Antibody Pair (202) (APMAB-202LY)


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Specifications

ApplIcation
Sandwich ELISA
Specificity
Human
Capture Antibody
Mouse anti-CCS monoclonal antibody, 100 ug
Detection Antibody
Anti-CCS Rabbit polyclonal antibody, 50 ug
Dilutions
10 ng/ml-100 ng/ml
Format
Liquid
Storage
Aliquot and store at -20°Cor -80°C. Avoid freeze-thaw cycles.
Introduction
CCS (Copper Chaperone For Superoxide Dismutase) is a Protein Coding gene. Diseases associated with CCS include Entropion and Amyotrophic Lateral Sclerosis 1. Among its related pathways are Detoxification of Reactive Oxygen Species and Amyotrophic lateral sclerosis (ALS). Gene Ontology (GO) annotations related to this gene include copper ion binding and copper ion transmembrane transporter activity. An important paralog of this gene is SOD1.
Alternative Names
Copper Chaperone For Superoxide Dismutase; Superoxide Dismutase Copper Chaperone;
Entrez Gene ID
9973
UniProt ID
O14618
More Infomation

Wen, C. Y., Shan, C. L., Sun, W. J., Wan, Y., Lin, R., Chen, B., ... & Yonghui, H. (2021). Copper chaperone for superoxide dismutase expression is down-regulated and correlated with more malignant tumoral features and poor prognosis in human hepatocellular carcinoma.

Grasso, M., Bond, G. J., Kim, Y. J., Boyd, S., Dzebo, M. M., Valenzuela, S., ... & Brady, D. C. (2021). The copper chaperone CCS facilitates copper binding to MEK1/2 to promote kinase activation. Journal of Biological Chemistry, 101314.

Boyd, S. D., Ullrich, M. S., Calvo, J. S., Behnia, F., Meloni, G., & Winkler, D. D. (2020). Mutations in superoxide dismutase 1 (Sod1) linked to familial amyotrophic lateral sclerosis can disrupt high-affinity zinc-binding promoted by the copper chaperone for Sod1 (Ccs). Molecules, 25(5), 1086.

Li, Y., Liang, R., Zhang, X., Wang, J., Shan, C., Liu, S., ... & Zhang, S. (2019). Copper chaperone for superoxide dismutase promotes breast cancer cell proliferation and migration via ROS-mediated MAPK/ERK signaling. Frontiers in pharmacology, 10, 356.

Skopp, A., Boyd, S. D., Ullrich, M. S., Liu, L., & Winkler, D. D. (2019). Copper–zinc superoxide dismutase (Sod1) activation terminates interaction between its copper chaperone (Ccs) and the cytosolic metal-binding domain of the copper importer Ctr1. Biometals, 32(4), 695-705.

Ge, Y., Wang, L., Li, D., Zhao, C., Li, J., & Liu, T. (2019). Exploring the extended biological functions of the human copper chaperone of superoxide dismutase 1. The protein journal, 38(4), 463-471.

Fukuoka, M., Tokuda, E., Nakagome, K., Wu, Z., Nagano, I., & Furukawa, Y. (2017). An essential role of N-terminal domain of copper chaperone in the enzymatic activation of Cu/Zn-superoxide dismutase. Journal of inorganic biochemistry, 175, 208-216.

Luchinat, E., Barbieri, L., & Banci, L. (2017). A molecular chaperone activity of CCS restores the maturation of SOD1 fALS mutants. Scientific reports, 7(1), 1-8.

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

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