CCS Antibody (E-1): sc-55560

CCS Antibody (E-1) is a mouse monoclonal IgG2b antibody that detects Copper Chaperone for SOD-1 (CCS) in human samples through applications such as western blotting (WB), immunoprecipitation (IP), immunofluorescence (IF), and enzyme-linked immunosorbent assay (ELISA). Anti-CCS antibody (E-1) plays a crucial role in studying cellular defense against oxidative stress by facilitating the proper incorporation of copper into Cu-Zn superoxide dismutase-1 (SOD-1), an essential enzyme that protects cells from damage caused by reactive oxygen species. CCS (E-1) antibody enables research on the interaction between CCS and SOD-1, which ensures copper delivery specifically to SOD-1 and prevents copper misallocation to other cellular proteins, maintaining various cellular functions. This specificity is particularly important because improper copper loading can lead to the accumulation of toxic free radicals, contributing to neurodegenerative diseases. CCS monoclonal antibody (E-1) helps identify CCS expression predominantly in the kidney, liver, and Purkinje cells of the central nervous system, highlighting CCS significance in tissues highly susceptible to oxidative damage. Anti-CCS antibody (E-1) serves as an invaluable tool for researchers studying oxidative stress mechanisms and copper homeostasis in cellular health.

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CCS Antibody (E-1) References:

1. 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
2. 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
3. Regulation of the copper chaperone CCS by XIAP-mediated ubiquitination.  |  Brady, GF., et al. 2010. Mol Cell Biol. 30: 1923-36. PMID: 20154138
4. Import, maturation, and function of SOD1 and its copper chaperone CCS in the mitochondrial intermembrane space.  |  Kawamata, H. and Manfredi, G. 2010. Antioxid Redox Signal. 13: 1375-84. PMID: 20367259
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. A molecular chaperone activity of CCS restores the maturation of SOD1 fALS mutants.  |  Luchinat, E., et al. 2017. Sci Rep. 7: 17433. PMID: 29234142
7. 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
8. 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
9. Pathogenic R163W Variant of the Copper Chaperone for Sod1 (Ccs) Functions as an Anti-chaperone.  |  Zhang, B., et al. 2024. Biochemistry. 63: 2051-2062. PMID: 39099176
10. The copper chaperone CCS directly interacts with copper/zinc superoxide dismutase.  |  Casareno, RL., et al. 1998. J Biol Chem. 273: 23625-8. PMID: 9726962

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