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  4. Recombinant Human Centrin-2 (CETN2)

Recombinant Human Centrin-2 (CETN2)

  • 货号：
    CSB-EP005265HU
  • 规格：
    ￥1344
  • 图片：
    • (Tris-Glycine gel) Discontinuous SDS-PAGE (reduced) with 5% enrichment gel and 15% separation gel.
  • 其他：

产品详情

  • 纯度：
    Greater than 90% as determined by SDS-PAGE.
  • 基因名：
  • Uniprot No.：
  • 别名：
    20kD calcium binding protein; CALT; caltractin; Caltractin isoform 1; CEN2; centrin; centrin; EF hand protein; 2 ; Centrin-2; Centrin2; CETN2; CETN2_HUMAN; EF hand protein 2; EF-hand protein
  • 种属：
    Homo sapiens (Human)
  • 蛋白长度：
    Full Length
  • 来源：
    E.coli
  • 分子量：
    35.7kDa
  • 表达区域：
    1-172aa
  • 氨基酸序列
    MASNFKKANMASSSQRKRMSPKPELTEEQKQEIREAFDLFDADGTGTIDVKELKVAMRALGFEPKKEEIKKMISEIDKEGTGKMNFGDFLTVMTQKMSEKDTKEEILKAFKLFDDDETGKISFKNLKRVAKELGENLTDEELQEMIDEADRDGDGEVSEQEFLRIMKKTSLY
    Note: The complete sequence including tag sequence, target protein sequence and linker sequence could be provided upon request.
  • 蛋白标签：
    N-terminal 6xHis-SUMO-tagged
  • 产品提供形式：
    Liquid or 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.
  • 缓冲液：
    Tris-based buffer,50% glycerol
  • 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：
    Basically, we can dispatch the products out in 1-3 working days after receiving your orders. 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 & COA：
    Please contact us to get it.

产品评价

靶点详情

  • 功能：
    Plays a fundamental role in microtubule organizing center structure and function. Required for centriole duplication and correct spindle formation. Has a role in regulating cytokinesis and genome stability via cooperation with CALM1 and CCP110.; Involved in global genome nucleotide excision repair (GG-NER) by acting as component of the XPC complex. Cooperatively with RAD23B appears to stabilize XPC. In vitro, stimulates DNA binding of the XPC:RAD23B dimer.; The XPC complex is proposed to represent the first factor bound at the sites of DNA damage and together with other core recognition factors, XPA, RPA and the TFIIH complex, is part of the pre-incision (or initial recognition) complex. The XPC complex recognizes a wide spectrum of damaged DNA characterized by distortions of the DNA helix such as single-stranded loops, mismatched bubbles or single-stranded overhangs. The orientation of XPC complex binding appears to be crucial for inducing a productive NER. XPC complex is proposed to recognize and to interact with unpaired bases on the undamaged DNA strand which is followed by recruitment of the TFIIH complex and subsequent scanning for lesions in the opposite strand in a 5'-to-3' direction by the NER machinery. Cyclobutane pyrimidine dimers (CPDs) which are formed upon UV-induced DNA damage esacpe detection by the XPC complex due to a low degree of structural perurbation. Instead they are detected by the UV-DDB complex which in turn recruits and cooperates with the XPC complex in the respective DNA repair.; As a component of the TREX-2 complex, involved in the export of mRNAs to the cytoplasm through the nuclear pores.
  • 基因功能参考文献：
    1. Multidisciplinary approach showed that HsPrp40Ap interacts with centrin in vitro, supporting a coupled functional role for these proteins in pre-mRNA splicing. PMID: 28636910
    2. Cetn3 inhibits Mps1 autophosphorylation at Thr-676, a known site of T-loop autoactivation, and interferes with Mps1-dependent phosphorylation of Cetn2. The cellular overexpression of Cetn3 attenuates the incorporation of Cetn2 into centrioles and centrosome reduplication, whereas depletion of Cetn3 generates extra centrioles. PMID: 26354417
    3. Centrin2 regulates primary ciliogenesis through controlling CP110 levels. PMID: 25753040
    4. co-depletion of centrin 2 and PCID2 leads to blocking rather than delaying nuclear protein export, indicating the dominance of the centrin 2 phenotype. PMID: 24291146
    5. Data indicate that overexpression of the centrin interactor POC5 leads to the assembly of linear, centrin-dependent structures. PMID: 23844208
    6. Cen2 influences the binding of RPA and XPA with damaged DNA. PMID: 22809153
    7. xeroderma pigmentosum complementation group C expression correlates with a decreased amount of CENTRIN 2 transcript and protein PMID: 21676658
    8. The stability of centrin is regulated in part by Aurora A. PMID: 21731694
    9. Mps1-dependent phosphorylation of Cetn2 stimulates the canonical centriole assembly pathway. PMID: 20980622
    10. oxidative radicals induce high proportions of irreversible damages (polymerisation) centrin 2 is highly sensitive to ionising radiation. PMID: 20586543
    11. required for centriole duplication in mammalian cells PMID: 12176356
    12. The solution structure of the long C-terminal fragment of centrin 2 exhibits an open two EF-hand structure, similar to the conformation of related Ca(2+)-saturated regulatory domains. PMID: 12578356
    13. structural characterization of the complex formed by the C-terminal domain of Cen2 with a peptide of xeroderma pigmentosum group C protein PMID: 12890685
    14. Results describe the self-assembly properties of purified human centrin-2 in vitro. PMID: 15356003
    15. Centrin 2 stimulates nucleotide excision repair by interacting with XPC. PMID: 15964821
    16. an 18-residue peptide, from the N-terminal unstructured fragment, has a significant affinity for the isolated C-terminal domain, suggesting an active role in the self-assembly of centrin molecules. PMID: 16411764
    17. the crystal structure of calcium-loaded full-length centrin-2 complexed with a xeroderma pigmentosum group C peptide; a novel binding motif for centrin PMID: 16627479
    18. A complex formed by a Ca2+-bound human centrin 2 with a 17-mer peptide derived from the XPC sequence was crystallized. PMID: 16820684
    19. Centrin 2 is highly sensitive to ionizing radiation, which could have important consequences on its biological functions. PMID: 17603931
    20. The present data confirm that the in vitro structural features of the centrin/XPC peptide complex are highly relevant to the cellular context. PMID: 17897675
    21. CETN2 localizes to the vertebrate nuclear pore and plays a role in mRNA and protein export. PMID: 18172010
    22. NMR analysis indicates that the physical interaction between C-XPC and centrin 2 induces only minor conformational changes into XPC, localized around the 17-mer segment (847-863), showed to be critically involved in the centrin binding. PMID: 18177054
    23. lower centrin levels in oligoasthnozoospermic males resulted in lower pregnancy percentage in this group after ICSI. PMID: 19179680
    24. The nucleocytoplasmic shuttling of centrin-2 depends on the SUMO system. PMID: 19706679
    25. The structure of C-HsCen2 [the C-terminal domain of HsCen2 (T94-Y172)] in complex with R17-hSfi1-20 was determined. PMID: 19857500

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  • 亚细胞定位：
    Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole. Nucleus envelope. Nucleus, nuclear pore complex. Nucleus.
  • 蛋白家族：
    Centrin family
  • 数据库链接：

    HGNC: 1867

    OMIM: 300006

    KEGG: hsa:1069

    STRING: 9606.ENSP00000359300

    UniGene: Hs.82794