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  4. Recombinant Escherichia coli Chemotaxis protein CheY (cheY)

Recombinant Escherichia coli Chemotaxis protein CheY (cheY)

  • 中文名稱(chēng)：
    Recombinant Escherichia coli Chemotaxis protein CheY (cheY)
  • 貨號(hào)：
    CSB-EP360065ENV
  • 規(guī)格：
    ￥1344
  • 圖片：
    • (Tris-Glycine gel) Discontinuous SDS-PAGE (reduced) with 5% enrichment gel and 15% separation gel.
  • 其他：

產(chǎn)品詳情

  • 純度：
    Greater than 90% as determined by SDS-PAGE.
  • 生物活性：
    Not Test
  • 基因名：
    cheY
  • Uniprot No.：
  • 種屬：
    Escherichia coli (strain K12)
  • 蛋白長(zhǎng)度：
    Full Length of Mature Protein
  • 來(lái)源：
    E.coli
  • 分子量：
    20.9 kDa
  • 表達(dá)區(qū)域：
    2-129aa
  • 氨基酸序列
    ADKELKFLVVDDFSTMRRIVRNLLKELGFNNVEEAEDGVDALNKLQAGGYGFVISDWNMPNMDGLELLKTIRADGAMSALPVLMVTAEAKKENIIAAAQAGASGYVVKPFTAATLEEKLNKIFEKLGM
    Note: The complete sequence may include tag sequence, target protein sequence, linker sequence and extra sequence that is translated with the protein sequence for the purpose(s) of secretion, stability, solubility, etc.
    If the exact amino acid sequence of this recombinant protein is critical to your application, please explicitly request the full and complete sequence of this protein before ordering.
  • 蛋白標(biāo)簽：
    C-terminal 6xHis-tagged
  • 產(chǎn)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.
  • 緩沖液：
    If the delivery form is liquid, the default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. If the delivery form is lyophilized powder, the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
  • 復(fù)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.
  • 儲(chǔ)存條件：
    Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
  • 保質(zhì)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.
  • 貨期：
    Delivery time may differ from different purchasing way or location, please kindly consult your local distributors for specific delivery time.
  • 注意事項(xiàng)：
    Repeated freezing and thawing is not recommended. Store working aliquots at 4℃ for up to one week.
  • Datasheet & COA：
    Please contact us to get it.

產(chǎn)品評(píng)價(jià)

靶點(diǎn)詳情

  • 功能：
    Involved in the transmission of sensory signals from the chemoreceptors to the flagellar motors. In its active (phosphorylated or acetylated) form, CheY exhibits enhanced binding to a switch component, FliM, at the flagellar motor which induces a change from counterclockwise to clockwise flagellar rotation. Overexpression of CheY in association with MotA and MotB improves motility of a ycgR disruption, suggesting there is an interaction (direct or indirect) between the c-di-GMP-binding flagellar brake protein and the flagellar stator.
  • 基因功能參考文獻(xiàn)：
    1. study identified K91 and K109 as the major sites whose acetylation level in vivo increases in response to acetate PMID: 25388160
    2. the enhanced reactivity of CheY DR reflected partial acquisition of catalytic and structural features of HAD phosphatases. PMID: 25928369
    3. Authors observe an apparent decrease and redistribution of mus-ms dynamics of allosteric response upon phosphorylation (and accompanying Mg(2+) saturation) of CheY. PMID: 23648838
    4. The flagellar motor adapts to changes in steady-state level of chemotaxis response regulator CheY-P by adjusting the number of FliM molecules to which CheY-P binds. Extreme motor ultrasensitivity broadens our understanding of allostery mechanisms PMID: 23454041
    5. F214A substitution in P2 of CheA caused 1,000-fold reduction in CheA-CheY binding affinity. PMID: 21642453
    6. motor switching: the largest variations are in the mean counter-clockwise interval, and are attributable to variations in the concentration of the internal signaling molecule CheY-P PMID: 21422514
    7. These results suggest that both phosphorylation and acetylation determine CheY's ability to bind to its target proteins, thus providing two levels of regulation, fast and slow respectively. PMID: 20398208
    8. Chemotaxis signaling protein CheY binds to the rotor protein FliN to control the direction of flagellar rotation in Escherichia coli. PMID: 20439729
    9. turnover of FliM molecules depends on the presence of active CheY, suggesting a potential role in the process of motor switching PMID: 20498085
    10. Data show that CheY is partially acetylated in spite of the absence of acetyl-CoA synthetase, suggesting that CheY can be post-translationally acetylated in vivo by additional means. PMID: 16630631
    11. crystallographic structure of unphosphorylated, magnesium(II)-bound CheY in complex with a synthetic peptide corresponding to the target region of FliM (the 16 N-terminal residues of FliM [FliM(16)]) PMID: 17050923
    12. Study succeeded in detecting CheY acetylation in vivo by three means--Western blotting with a specific anti-acetyl-lysine antibody, mass spectrometry, and radiolabeling with [(14)C]acetate in the presence of protein-synthesis inhibitor. PMID: 18234227
    13. The authors demonstrate that substitutions at two variable active site positions decreased CheY autodephosphorylation up to 40-fold and increased the Spo0F rate up to 110-fold. PMID: 18557815
    14. Data suggest that CheY initially misfolds before accessing the native conformation. PMID: 18619461
    15. Results describe the subdomain competition, cooperativity, and topological frustration in the folding of CheY. PMID: 18644380
    16. Comparison of X-ray crystal structures of five CheY mutants gave strong evidence for steric obstruction of the phosphoryl group from the attacking water molecule as one mechanism to enhance phosphoryl group stability. PMID: 19646451

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  • 亞細(xì)胞定位：
    Cytoplasm.
  • 數(shù)據(jù)庫(kù)鏈接：


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