CCS Antibody, Biotin conjugated

1. In addition to Atox1, the human cytoplasm also contains Cu chaperones for loading of superoxide dismutase 1 (i.e. CCS) and cytochrome c oxidase in mitochondria (i.e. Cox17). [review] PMID: 26745464
2. Human cytoplasmic copper chaperones Atox1 and CCS exchange copper ions in vitro PMID: 25673218
3. Coexpression of hCCS in the presence of copper restores the correct maturation of the SOD1 mutants and prevents the formation of the unstructured species, confirming that hCCS also acts as a molecular chaperone. PMID: 25429517
4. CCS mRNA and protein levels in the serum are not correlated with inflammatory processes. PMID: 24855044
5. CTR1 silencing increased the protein levels of copper chaperone ATOX1 and copper chaperone for superoxide dismutase 1 (CCS-1), but decreased copper chaperone for cytochrome c oxidase (COX17). PMID: 24343031
6. CCS1 serves as a specialized import receptor in mitochondria that facilitates the import and folding of SOD1 and CCS1. PMID: 24026195
7. CCS-dependent copper acquisition and distribution largely occur at membrane interfaces and that this emerging role of the bilayer may reflect a general mechanistic aspect of cellular transition metal ion acquisition. PMID: 24297923
8. CCS-1 facilitates copper trafficking to the mitochondria, but does not affect the transfer of copper to the cytochrome c oxidase. PMID: 23900152
9. The CCS mutation, p.Arg163Trp, causes reduced SOD1 activity and may impair other mechanisms important for normal Cu homeostasis. PMID: 22508683
10. analysis of human superoxide dismutase 1 (hSOD1) maturation through interaction with human copper chaperone for SOD1 (hCCS) PMID: 22869735
11. Loss of copper chaperone for superoxide dismutase (CCS) increases amyloid-beta production in both CCS knockout neurons and CCS small-interfering (si)RNA-treated cultured tumor cells. PMID: 20693630
12. The results of the present study reveal the plasticity of this multi-domain chaperone in solution and are consistent with an indispensable flexibility necessary for executing its dual functions of metal binding and transfer. PMID: 21722094
13. CCS reduces, under non-oxidative conditions, yet facilitates in the presence of H(2)O(2), mitochondrial translocation of inactive SOD1 mutants. PMID: 21354101
14. Results describe the identification of the copper chaperone for superoxide dismutase as a mediator of copper delivery to XIAP in cells. PMID: 20154138
15. No causative mutations for amyotrophic lateral sclerosis (ALS) gene have been detected in the CCS gene in 20 sporadic ALS patients analyzed, but an intragenic single nucleotide polymorphism has been identified. PMID: 11991808
16. Study of site-directed cysteine-to-serine mutants of CCS suggests the formation of a domain III copper cluster within a dimeric or tetrameric protein and further suggest that this cluster may be an important element of CCS copper transfer machinery. PMID: 15736924
17. The copper chaperone CCS is responsible for copper insertion into apo-superoxide dismutasse 1. PMID: 16132821
18. A mechanism determining the abundance of CCS that is competitive with the process of copper delivery to SOD1 is described, revealing a unique post-translational component of intracellular copper homeostasis. PMID: 16531609
19. copper chaperone mRNA levels were reduced in peripheral mononuclear cells after copper supplementation PMID: 17683925
20. Measurements of hCCS-induced SOD1 activation were used to show that the C-terminal CXC sequence is both necessary and sufficient for EZn-SOD maturation. PMID: 18393442
21. copper chaperone for SOD1 (CCS) facilitates maturation of SOD1 and that CCS overexpression ameliorates intracellular aggregation of mutant SOD1 in vivo. PMID: 18552350
22. data suggest that Cys residues in domain 2 of hCCS are involved in the formation, stability, and redox potential of the domain 3 cluster PMID: 19007184
23. Incomplete posttranslational modification of nascent superoxide dismutase (SOD)1 polypeptides via trasnsgenic SOD1 copper chaperone (CCS) may be a characteristic shared by familial SOD1 mutants in amyotrophic lateral sclerosis. PMID: 19227972

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HGNC: 1613

OMIM: 603864

KEGG: hsa:9973

STRING: 9606.ENSP00000436318

UniGene: Hs.502917