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Superoxide dismutase copper chaperone Protein (AA 1-274) (His tag)

CCS Origin: Human Host: Escherichia coli (E. coli) Recombinant > 90 % by SDS - PAGE SDS
Catalog No. ABIN667211
  • Target See all Superoxide dismutase copper chaperone (CCS) Proteins
    Superoxide dismutase copper chaperone (CCS) (Copper Chaperone For Superoxide Dismutase (CCS))
    Protein Type
    Recombinant
    Protein Characteristics
    AA 1-274
    Origin
    • 4
    • 3
    • 2
    • 1
    Human
    Source
    • 4
    • 2
    • 2
    • 2
    Escherichia coli (E. coli)
    Purification tag / Conjugate
    This Superoxide dismutase copper chaperone protein is labelled with His tag.
    Application
    SDS-PAGE (SDS)
    Characteristics
    CCS, 1-274aa, Human, His tag, E.coli
    Purity
    > 90 % by SDS - PAGE
  • Restrictions
    For Research Use only
  • Format
    Liquid
    Concentration
    1 mg/ml (determined by Bradford assay)
    Buffer
    Liquid. In 20 mM Tris-HCl buffer (pH8.0) containing 0.2M NaCl 1mM DTT, 10% glycerol
    Storage
    4 °C
  • Target
    Superoxide dismutase copper chaperone (CCS) (Copper Chaperone For Superoxide Dismutase (CCS))
    Alternative Name
    CCS (CCS Products)
    Synonyms
    ccs Protein, MGC82563 Protein, CCS Protein, DDBDRAFT_0189222 Protein, DDBDRAFT_0238038 Protein, DDB_0189222 Protein, DDB_0238038 Protein, ATCCS Protein, COPPER/ZINC SUPEROXIDE DISMUTASE COPPER CHAPERONE Protein, F5O11.26 Protein, F5O11_26 Protein, copper chaperone for SOD1 Protein, Ccsd Protein, copper chaperone for superoxide dismutase L homeolog Protein, copper chaperone for superoxide dismutase Protein, copper chaperone for SOD1 Protein, ccs.L Protein, ccs Protein, CCS Protein, LOC552629 Protein, Ccs Protein
    Background
    CCS is essential for the incorporation of copper into SOD-1, and therefore is necessary for its enzymatic activity. CCS prevents copper ions from binding to intracellular copper scavengers and provides the SOD-1 enzyme with the necessary copper cofactor. CCS escorts copper only to SOD-1 and fails to deliver copper to proteins in the mitochondria, nucleus or secretory pathway. While many tissues express CCS, the chaperone is most abundant in the kidney, liver and Purkinje cells in the neuropil of the central nervous system. Recombinant human CCS protein, fused to His-tag at N-terminus, was expressed in E.coli and purified by using conventional chromatography techniques. Synonyms: Copper chaperone for superoxide dismutase,. NCBI no.: NP_005116
    Molecular Weight
    31.2 kDa (294aa), confirmed by MALDI-TOF
    Pathways
    Transition Metal Ion Homeostasis
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