CCS Antibody (D-7): sc-374205

CCS Antibody (D-7) is a mouse monoclonal IgG1 antibody that detects Copper Chaperone for SOD-1 (CCS) in mouse, rat, and human samples through various applications including western blotting (WB), immunoprecipitation (IP), immunofluorescence (IF), immunohistochemistry with paraffin-embedded sections (IHCP), and enzyme-linked immunosorbent assay (ELISA). CCS plays a critical role in the proper functioning of Cu-Zn superoxide dismutase-1 (SOD-1) by facilitating the incorporation of copper ions, which are essential for the enzyme′s antioxidant activity. CCS is primarily located in the cytosol, where CCS acts as a dedicated chaperone, ensuring that copper is delivered specifically to SOD-1 while preventing binding to other intracellular copper scavengers. CCS localization is vital, as CCS helps maintain cellular homeostasis by regulating copper levels and protecting cells from oxidative stress. CCS (D-7) antibody targets a protein most abundantly expressed in the kidney, liver, and Purkinje cells of the central nervous system, highlighting CCS importance in tissues particularly susceptible to oxidative damage. Anti-CCS antibody (D-7) serves as an invaluable tool for researchers studying oxidative stress mechanisms and copper′s role in cellular processes, as well as for investigating CCS implications in various diseases, including neurodegenerative disorders.

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CCS Antibody (D-7) References:

1. Metallochaperone for Cu,Zn-superoxide dismutase (CCS) protein but not mRNA is higher in organs from copper-deficient mice and rats.  |  Prohaska, JR., et al. 2003. Arch Biochem Biophys. 417: 227-34. PMID: 12941305
2. Oxygen and the copper chaperone CCS regulate posttranslational activation of Cu,Zn superoxide dismutase.  |  Brown, NM., et al. 2004. Proc Natl Acad Sci U S A. 101: 5518-23. PMID: 15064408
3. Activation of Cu,Zn-superoxide dismutase in the absence of oxygen and the copper chaperone CCS.  |  Leitch, JM., et al. 2009. J Biol Chem. 284: 21863-21871. PMID: 19542232
4. Regulation of the copper chaperone CCS by XIAP-mediated ubiquitination.  |  Brady, GF., et al. 2010. Mol Cell Biol. 30: 1923-36. PMID: 20154138
5. Chaperones CCS, ATOX and COXIV responses to copper supplementation in healthy adults.  |  Araya, M., et al. 2012. Biometals. 25: 383-91. PMID: 22124795
6. Molecular and biochemical characterization of a unique mutation in CCS, the human copper chaperone to superoxide dismutase.  |  Huppke, P., et al. 2012. Hum Mutat. 33: 1207-15. PMID: 22508683
7. A molecular chaperone activity of CCS restores the maturation of SOD1 fALS mutants.  |  Luchinat, E., et al. 2017. Sci Rep. 7: 17433. PMID: 29234142
8. Copper-zinc superoxide dismutase (Sod1) activation terminates interaction between its copper chaperone (Ccs) and the cytosolic metal-binding domain of the copper importer Ctr1.  |  Skopp, A., et al. 2019. Biometals. 32: 695-705. PMID: 31292775
9. 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).  |  Boyd, SD., et al. 2020. Molecules. 25: PMID: 32121118
10. The copper chaperone CCS is abundant in neurons and astrocytes in human and rodent brain.  |  Rothstein, JD., et al. 1999. J Neurochem. 72: 422-9. PMID: 9886096

The preferred CCS antibody is CCS Antibody (H-7): sc-55561.