CCS Antibody (E-5): sc-365820

CCS Antibody (E-5) is a mouse monoclonal IgG1 antibody that detects Copper Chaperone for SOD-1 (CCS) in mouse, rat, and human samples through applications such as western blotting (WB), immunoprecipitation (IP), immunofluorescence (IF), and enzyme-linked immunosorbent assay (ELISA). Anti-CCS antibody (E-5) 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 monoclonal antibody (E-5) enables research into CCS′s function as a chaperone and specific interaction with SOD-1, as CCS ensures copper ions are delivered exclusively to this enzyme, thereby enhancing activity while preventing copper misallocation to other cellular proteins. This selective delivery is vital because improper copper handling can lead to cellular dysfunction and contribute to neurodegenerative diseases. CCS (E-5) antibody helps researchers study CCS expression in the kidney, liver, and Purkinje cells of the central nervous system, highlighting significance in tissues particularly vulnerable to oxidative damage. Anti-CCS antibody (E-5) enables insights into copper metabolism and oxidative stress response mechanisms, furthering understanding of various pathological conditions.

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CCS Antibody (E-5) References:

1. A gain of superoxide dismutase (SOD) activity obtained with CCS, the copper metallochaperone for SOD1.  |  Schmidt, PJ., et al. 1999. J Biol Chem. 274: 36952-6. PMID: 10601249
2. Human CCS gene: genomic organization and exclusion as a candidate for amyotrophic lateral sclerosis (ALS).  |  Silahtaroglu, AN., et al. 2002. BMC Genet. 3: 5. PMID: 11991808
3. Mechanisms for activating Cu- and Zn-containing superoxide dismutase in the absence of the CCS Cu chaperone.  |  Carroll, MC., et al. 2004. Proc Natl Acad Sci U S A. 101: 5964-9. PMID: 15069187
4. Oxygen-induced maturation of SOD1: a key role for disulfide formation by the copper chaperone CCS.  |  Furukawa, Y., et al. 2004. EMBO J. 23: 2872-81. PMID: 15215895
5. Overexpression of CCS in G93A-SOD1 mice leads to accelerated neurological deficits with severe mitochondrial pathology.  |  Son, M., et al. 2007. Proc Natl Acad Sci U S A. 104: 6072-7. PMID: 17389365
6. Biological effects of CCS in the absence of SOD1 enzyme activation: implications for disease in a mouse model for ALS.  |  Proescher, JB., et al. 2008. Hum Mol Genet. 17: 1728-37. PMID: 18337307
7. 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
8. Effect of CCS on the accumulation of FALS SOD1 mutant-containing aggregates and on mitochondrial translocation of SOD1 mutants: implication of a free radical hypothesis.  |  Kim, HK., et al. 2011. Arch Biochem Biophys. 509: 177-85. PMID: 21354101
9. S-acylation of SOD1, CCS, and a stable SOD1-CCS heterodimer in human spinal cords from ALS and non-ALS subjects.  |  Antinone, SE., et al. 2017. Sci Rep. 7: 41141. PMID: 28120938
10. CRISPR/Cas9 screens unravel miR-3689a-3p regulating sorafenib resistance in hepatocellular carcinoma via suppressing CCS/SOD1-dependent mitochondrial oxidative stress.  |  Lu, Y., et al. 2023. Drug Resist Updat. 71: 101015. PMID: 37924725

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