Superoxide Dismutase Copper Chaperone

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CCS; Copper Chaperone For Superoxide Dismutase

Superoxide Dismutase Copper Chaperone

Copper (Cu) is required for aerobic life and yet, paradoxically, is highly toxic. This apparent contradiction has been rationalized by assuming that Cu, like other redox-active metals, is sequestered in nonreactive forms as it is transported into cells and moves through cellular compartments. Culotta et al. (1997) determined that one such Cu chaperone protein, Lys7, specifically delivers Cu to copper/zinc superoxide dismutase (Sod1) in S. cerevisiae. By searching EST databases, they identified cDNAs encoding the human Lys7 homolog, which they named CCS (copper chaperone for SOD1). The predicted 274-amino acid human protein is 28% identical to Lys7. CCS complemented a yeast Lys7 mutation, demonstrating that CCS is a functional homolog of Lys7.

Organism species: Homo sapiens (Human)

CATALOG NO. PRODUCT NAME APPLICATIONS
Proteins RPA596Hu01 Recombinant Superoxide Dismutase Copper Chaperone Positive Control; Immunogen; SDS-PAGE; WB.
APA596Hu01 Active Superoxide Dismutase Copper Chaperone Cell culture; Activity Assays.
Antibodies PAA596Hu01 Polyclonal Antibody to Superoxide Dismutase Copper Chaperone WB,IHC
MAA596Hu21 Monoclonal Antibody to Superoxide Dismutase Copper Chaperone WB; IHC; ICC; IP.
Assay Kits SEA596Hu ELISA Kit for Superoxide Dismutase Copper Chaperone Enzyme-linked immunosorbent assay for Antigen Detection.

Organism species: Mus musculus (Mouse)

CATALOG NO. PRODUCT NAME APPLICATIONS
Proteins RPA596Mu01 Recombinant Superoxide Dismutase Copper Chaperone Positive Control; Immunogen; SDS-PAGE; WB.
APA596Mu01 Active Superoxide Dismutase Copper Chaperone Cell culture; Activity Assays.
Antibodies PAA596Mu01 Polyclonal Antibody to Superoxide Dismutase Copper Chaperone WB; IHC; ICC; IP.
Assay Kits n/a CLIA Kit for Superoxide Dismutase Copper Chaperone CLIA Kit Customized Service Offer
n/a ELISA Kit for Superoxide Dismutase Copper Chaperone ELISA Kit Customized Service Offer

Organism species: Rattus norvegicus (Rat)

CATALOG NO. PRODUCT NAME APPLICATIONS
Proteins RPA596Ra01 Recombinant Superoxide Dismutase Copper Chaperone Positive Control; Immunogen; SDS-PAGE; WB.
APA596Ra01 Active Superoxide Dismutase Copper Chaperone Cell culture; Activity Assays.
Antibodies PAA596Ra01 Polyclonal Antibody to Superoxide Dismutase Copper Chaperone WB; IHC; ICC; IP.
MAA596Ra21 Monoclonal Antibody to Superoxide Dismutase Copper Chaperone WB; IHC; ICC; IP.
Assay Kits SEA596Ra ELISA Kit for Superoxide Dismutase Copper Chaperone Enzyme-linked immunosorbent assay for Antigen Detection.
  1. "The copper chaperone for superoxide dismutase."J. Biol. Chem. 272:23469-23472(1997) [PubMed] [Europe PMC] [Abstract]
  2. "Initial characterization of the human central proteome."BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
  3. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
  4. "Mechanistic aspects of hSOD1 maturation from the solution structure of Cu(I) -loaded hCCS domain 1 and analysis of disulfide-free hSOD1 mutants."ChemBioChem 14:1839-1844(2013) [PubMed] [Europe PMC] [Abstract]
  5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
  6. "The copper chaperone CCS directly interacts with copper/zinc superoxide dismutase."J. Biol. Chem. 273:23625-23628(1998) [PubMed] [Europe PMC] [Abstract]
  7. "Cysteine-to-serine mutants of the human copper chaperone for superoxide dismutase reveal a copper cluster at a domain III dimer interface."Biochemistry 44:3143-3152(2005) [PubMed] [Europe PMC] [Abstract]
  8. "Cu,Zn superoxide dismutase maturation and activity are regulated by COMMD1."J. Biol. Chem. 285:28991-29000(2010) [PubMed] [Europe PMC] [Abstract]
  9. "Regulation of the copper chaperone CCS by XIAP-mediated ubiquitination."Mol. Cell. Biol. 30:1923-1936(2010) [PubMed] [Europe PMC] [Abstract]
  10. "Molecular and biochemical characterization of a unique mutation in CCS, the human copper chaperone to superoxide dismutase."Hum. Mutat. 33:1207-1215(2012) [PubMed] [Europe PMC] [Abstract]
  11. "Crystal structure of the second domain of the human copper chaperone for superoxide dismutase."Biochemistry 39:1589-1595(2000) [PubMed] [Europe PMC] [Abstract]
  12. "The apo form of HMA domain of copper chaperone for superoxide dismutase."Submitted (NOV-2005) to the PDB data bank