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  4. Recombinant Human Copper chaperone for superoxide dismutase (CCS)

Recombinant Human Copper chaperone for superoxide dismutase (CCS)

  • 货号：
    CSB-YP004854HU
  • 规格：
  • 来源：
    Yeast
  • 其他：
  • 货号：
    CSB-EP004854HU
  • 规格：
  • 来源：
    E.coli
  • 其他：
  • 货号：
    CSB-EP004854HU-B
  • 规格：
  • 来源：
    E.coli
  • 共轭：
    Avi-tag Biotinylated

    E. coli biotin ligase (BirA) is highly specific in covalently attaching biotin to the 15 amino acid AviTag peptide. This recombinant protein was biotinylated in vivo by AviTag-BirA technology, which method is BriA catalyzes amide linkage between the biotin and the specific lysine of the AviTag.

  • 其他：
  • 货号：
    CSB-BP004854HU
  • 规格：
  • 来源：
    Baculovirus
  • 其他：
  • 货号：
    CSB-MP004854HU
  • 规格：
  • 来源：
    Mammalian cell
  • 其他：

产品详情

  • 纯度：
    >85% (SDS-PAGE)
  • 基因名：
    CCS
  • Uniprot No.：
  • 别名：
    CCS; CCS_HUMAN; Copper chaperone for superoxide dismutase; MGC138260; SOD 4; SOD4; Superoxide dismutase copper chaperone
  • 种属：
    Homo sapiens (Human)
  • 蛋白长度：
    Full length protein
  • 表达区域：
    1-274
  • 氨基酸序列
    MASDSGNQGT LCTLEFAVQM TCQSCVDAVR KSLQGVAGVQ DVEVHLEDQM VLVHTTLPSQ EVQALLEGTG RQAVLKGMGS GQLQNLGAAV AILGGPGTVQ GVVRFLQLTP ERCLIEGTID GLEPGLHGLH VHQYGDLTNN CNSCGNHFNP DGASHGGPQD SDRHRGDLGN VRADADGRAI FRMEDEQLKV WDVIGRSLII DEGEDDLGRG GHPLSKITGN SGERLACGII ARSAGLFQNP KQICSCDGLT IWEERGRPIA GKGRKESAQP PAHL
  • 蛋白标签：
    Tag type will be determined during the manufacturing process.
    The tag type will be determined during production process. If you have specified tag type, please tell us and we will develop the specified tag preferentially.
  • 产品提供形式：
    Lyophilized powder
    Note: We will preferentially ship the format that we have in stock, however, if you have any special requirement for the format, please remark your requirement when placing the order, we will prepare according to your demand.
  • 复溶：
    We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20℃/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference.
  • 储存条件：
    Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
  • 保质期：
    The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
    Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.
  • 货期：
    Delivery time may differ from different purchasing way or location, please kindly consult your local distributors for specific delivery time.
    Note: All of our proteins are default shipped with normal blue ice packs, if you request to ship with dry ice, please communicate with us in advance and extra fees will be charged.
  • 注意事项：
    Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
  • Datasheet ：
    Please contact us to get it.

产品评价

靶点详情

  • 功能：
    Delivers copper to copper zinc superoxide dismutase (SOD1).
  • 基因功能参考文献：
    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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  • 亚细胞定位：
    Cytoplasm.
  • 蛋白家族：
    Cu-Zn superoxide dismutase family
  • 组织特异性：
    Ubiquitous.
  • 数据库链接：

    HGNC: 1613

    OMIM: 603864

    KEGG: hsa:9973

    STRING: 9606.ENSP00000436318

    UniGene: Hs.502917