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  4. Recombinant Human Copper transport protein ATOX1 (ATOX1)

Recombinant Human Copper transport protein ATOX1 (ATOX1)

  • 货号：
    CSB-YP002309HU
  • 规格：
  • 来源：
    Yeast
  • 其他：
  • 货号：
    CSB-EP002309HU
  • 规格：
  • 来源：
    E.coli
  • 其他：
  • 货号：
    CSB-EP002309HU-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-BP002309HU
  • 规格：
  • 来源：
    Baculovirus
  • 其他：
  • 货号：
    CSB-MP002309HU
  • 规格：
  • 来源：
    Mammalian cell
  • 其他：

产品详情

  • 纯度：
    >85% (SDS-PAGE)
  • 基因名：
    ATOX1
  • Uniprot No.：
  • 别名：
    ATOX1; ATOX1_HUMAN; ATX1; ATX1 antioxidant protein 1 homolog (yeast); ATX1 antioxidant protein 1 homolog; Copper transport protein; Copper transport protein ATOX1; HAH1; Metal transport protein; Metal transport protein ATX1; MGC138453; MGC138455
  • 种属：
    Homo sapiens (Human)
  • 蛋白长度：
    Full length protein
  • 表达区域：
    1-68
  • 氨基酸序列
    MPKHEFSVDM TCGGCAEAVS RVLNKLGGVK YDIDLPNKKV CIESEHSMDT LLATLKKTGK TVSYLGLE
  • 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：
    Binds and deliver cytosolic copper to the copper ATPase proteins. May be important in cellular antioxidant defense.
  • 基因功能参考文献：
    1. Copper chaperone Atox-1 is involved in the induction of SOD3 in a monocyte cell line. PMID: 29168020
    2. Since full occupancy of the tetrahedral cavity is a common feature of all Atox1 dimeric structures obtained with other metal ions (Cu(+), Cd(2+), and Hg(2+)), we propose that in the case of platinum, where the occupancy is only 0.4, the remaining cavities are occupied by Cu(+) ions PMID: 27305454
    3. Data suggest that N-terminal segment of metal-binding domains (MBDs) 1-3 of ATOX1 interact with nucleotide-binding domain of ATP7B, thus physically coupling the domains involved in copper binding and those involved in ATP hydrolysis; interactions with MBDs 1-3 of ATOX1 activate ATP7B ATP hydrolysis. (ATOX1 = copper transport protein ATOX1; ATP7B = Cu-binding P type ATPase ATP7B) PMID: 28900031
    4. It show that copper(I) and glutathione form large polymers with a molecular mass of approximately 8 kDa, which can transfer copper to Atox1. PMID: 28549213
    5. Highlighted in this review are unique redox properties of Atox1 and other copper chaperones. Also, summarized are the redox nodes in the cytosol which potentially play dominant roles in the redox regulation of copper chaperones PMID: 28294521
    6. The structural flexibility of the human copper chaperone Atox1 has been reported based on insights from combined pulsed EPR studies and computations. PMID: 28543811
    7. Cu chaperone Atox1 has a role in breast cancer cell migration PMID: 28027931
    8. Multiple genetic models identified genetic associations with systolic blood pressure and ATOX1. PMID: 26866891
    9. 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
    10. results suggest the possibility of a therapy with copper-chelating or ionophore drugs in subtypes of tumors showing specific alterations in ATOX1 expression PMID: 26784148
    11. C-Terminus of Human Copper Importer Ctr1 Acts as a Binding Site and Transfers Copper to Atox1 PMID: 26745413
    12. Cu chaperone function of Atox1 mediated through Cu transporter ATP7A is required for VEGF-induced angiogenesis via activation of Cu enzyme lysyl oxidase. PMID: 26437801
    13. Upon neuronal differentiation, transitions in redox states upregulates expression of ATOX1 and its partner ATP7A, producing higher flux of copper through the secretory pathway. PMID: 26879543
    14. To identify new interactions partners of Atox1, a yeast two-hybrid screen with a large human placenta library of cDNA fragments using Atox1 as bait, was performed. PMID: 26213915
    15. Studied the localization of Atox1 in HeLa cells using fluorescence imaging in combination with in vitro binding experiments to fluorescently labeled DNA duplexes harboring the proposed promotor sequence. PMID: 25962064
    16. Human cytoplasmic copper chaperones Atox1 and CCS exchange copper ions in vitro PMID: 25673218
    17. Cisplatin is one of the most used anticancer drugs. Its cellular influx and delivery to target DNA may involve the copper chaperone Atox1 protein. PMID: 25111319
    18. The data collected here shows that the Atox1 keeps its dimer nature also in the presence of the CTR1 c-terminal domain; however, two geometrical states are assumed by the Atox1. PMID: 24837030
    19. The Cu-binding motif in Atox1, as well as in target Cu-binding domains of ATP7A/B, consists of a MX1CXXC motif where X1 = T. PMID: 24824562
    20. Human Grx1 can catalyse reduction of Atox1 by glutathione but only in the presence of Cu(I). PMID: 24522867
    21. These results indicate that the roles of Atox1 in the regulation of cellular trafficking of platinum drugs are dependent on the coordination configurations. PMID: 24469739
    22. Atox1 has a role in copper transport to tumor cell nuclei. PMID: 24445997
    23. 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
    24. Atox1 contains positive residues that mediate membrane association and aid subsequent copper loading. PMID: 24036897
    25. the primary coordination site of Atox1 for interaction wtih cisplatin is at the cysteine residues in the Cu(I)-binding sequence Cys(12)GlyGlyCys(15) PMID: 23778981
    26. Based on structural analysis, this work determines that the protein possesses two distinct conformations referred to as "in" and "out" due to the relative positioning of Cys12 (one of Cu(I) binding residues). PMID: 23553875
    27. Knockdown of ATOX1 in non-small cell lung cancer cells was associated with reduction in copper-stimulated cell proliferation. These findings suggest that ATOX1 plays an important role in copper-stimulated proliferation of non-small cell lung cancer cells. PMID: 23624903
    28. Binding of free cisplatin and reaction with the cisplatin-loaded Atox1 produce the same protein-bound platinum intermediate in the transfer of metal-binding domain (repeat) (MBD)2 from Atox1. PMID: 23751120
    29. different effects of ATX1 unfolding on Cu(I) affinity PMID: 23169585
    30. GSSG oxidizes copper-coordinating cysteines of Atox1 with formation of an intramolecular disulfide. GSH alone is sufficient to reduce the disulfide, restoring the ability of Atox1 to bind copper; glutaredoxin 1 facilitates this reaction when GSH is low PMID: 22648419
    31. No major role can be attributed to Atox1 and COMMD in the pathophysiology or clinical variation of Wilson disease. PMID: 22677543
    32. thermodynamic parameters of copper (Cu) transfer from the human copper chaperone Atox1 to the fourth metal-binding domain of the Wilson disease protein PMID: 22574136
    33. By binding to Atox1 in the cytoplasm, cisPt transport to DNA may be blocked. In agreement with this model, cell line studies demonstrate a correlation between Atox1 expression levels, and cisplatin resistance. PMID: 21482801
    34. Unification of the copper(I) binding affinities of the metallo-chaperones Atx1, Atox1, and related proteins: detection probes and affinity standards. PMID: 21258123
    35. transfers copper to the NH2-terminal domain of the Wilson's disease protein and regulates its catalytic activity PMID: 12029094
    36. Gene structure of ATOX1. PMID: 12594858
    37. A copper-dependent interaction of Atox1 with the metal binding sites of menkes protein was observed PMID: 12679332
    38. X-ray absorption spectroscopy of this copper chaperone reveals a copper center capable of formation with exogenous thiols and phosphines PMID: 12686548
    39. Regulates the function of ATP7B in Wilson's disease PMID: 12763797
    40. handling of copper by Atox1 and copper transfer between Atox1 and WND are under kinetic rather than thermodynamic control PMID: 14709553
    41. Detailed structural and dynamic characterization of the behavior of human HAH1 in solution, in the physiologically relevant reduced apo and copper(I)-bound forms PMID: 15476398
    42. interaction between the human copper(I) chaperone, HAH1, and one of its two physiological partners, the Menkes disease protein (ATP7A), was investigated in solution using heteronuclear NMR PMID: 15670166
    43. Atox1 functions not only as a copper chaperone for SOD3 but also as a positive regulator for SOD3 transcription and may have an important role in modulating oxidative stress in the cardiovascular system. PMID: 15761197
    44. a three-domain construct of ATP7A interacts with copper(I) and copper(I)-HAH1 PMID: 16172131
    45. Wilson disease protein is an acceptor of oopper from HAH1 protein. PMID: 16571664
    46. localization of ATP7A between the trans-Golgi network and the plasma membrane may be regulated by the accumulation of the adducts with HAH1, whereas the main role of domains 5 and 6 is to assist copper(I) translocation PMID: 17545667
    47. The results from the quantum mechanical (QM) and MD simulations suggest that either a two- or three-coordinate exchange reaction is preferred and that it is unlikely that a four-coordinate Cu(I) species plays a role in copper exchange. PMID: 17616150
    48. Divergent energetic properties of Atox1 apo- and holo-forms may be linked to conformational changes that facilitate copper transfer to the target. PMID: 17881304
    49. Atox1 functions as a novel transcription factor that, when activated by copper, undergoes nuclear translocation, DNA binding, and transactivation, thereby contributing to cell proliferation. PMID: 18245776
    50. No major role can be attributed to Atox1 in the pathophysiology or clinical variation of Wilson disease. PMID: 18416466

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  • 蛋白家族：
    ATX1 family
  • 组织特异性：
    Ubiquitous.
  • 数据库链接：

    HGNC: 798

    OMIM: 602270

    KEGG: hsa:475

    STRING: 9606.ENSP00000316854

    UniGene: Hs.125213