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Mouse Anti-CCS Recombinant Antibody (11G1) (CBMAB-C2521-LY)

This product is antibody recognizes CCS. The antibody 11G1 immunoassay techniques such as: WB, ELISA.
See all CCS antibodies

Summary

Host Animal
Mouse
Specificity
Human
Clone
11G1
Antibody Isotype
IgG1, κ
Application
WB, ELISA

Basic Information

Immunogen
Recombinant human protein purified from E.coli
Specificity
Human
Antibody Isotype
IgG1, κ
Clonality
Monoclonal
Application Notes
The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.

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

Format
Liquid
Purity
> 95% Purity determined by SDS-PAGE.
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
Copper Chaperone For Superoxide Dismutase
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.
Entrez Gene ID
UniProt ID
Alternative Names
Copper Chaperone For Superoxide Dismutase; Superoxide Dismutase Copper Chaperone;
Function
Delivers copper to copper zinc superoxide dismutase (SOD1).
Biological Process
Cellular response to oxidative stress Source: Reactome
Positive regulation of oxidoreductase activity Source: Ensembl
Protein maturation by copper ion transfer Source: ProtInc
Removal of superoxide radicals Source: GO_Central
Superoxide metabolic process Source: ProtInc
Cellular Location
Cytoplasm
PTM
Ubiquitinion by XIAP/BIRC4 leads to enhancement of its chaperone activity toward its physiologic target, SOD1, rather than proteasomal degradation. XIAP/BIRC4 preferentially ubiquitinates at Lys-241.

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.

Custom Antibody Labeling

We also offer labeled antibodies developed using our catalog antibody products and nonfluorescent conjugates (HRP, AP, Biotin, etc.) or fluorescent conjugates (Alexa Fluor, FITC, TRITC, Rhodamine, Texas Red, R-PE, APC, Qdot Probes, Pacific Dyes, etc.).

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