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中文名稱:cheY Antibody
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貨號:CSB-PA360065XA01ENV
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規格:¥880
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圖片:
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其他:
產品詳情
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產品名稱:Rabbit anti-Escherichia coli (strain K12) cheY Polyclonal antibody
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Uniprot No.:
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基因名:cheY
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別名:Chemotaxis protein CheY cheY b1882 JW1871
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宿主:Rabbit
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反應種屬:Escherichia coli (strain K12)
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免疫原:Recombinant Escherichia coli (strain K12) cheY protein (2-129aa)
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免疫原種屬:Escherichia coli (strain K12)
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標記方式:Non-conjugated
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克隆類型:Polyclonal
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抗體亞型:IgG
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純化方式:Antigen Affinity Purified
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濃度:It differs from different batches. Please contact us to confirm it.
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保存緩沖液:Preservative: 0.03% Proclin 300
Constituents: 50% Glycerol, 0.01M PBS, pH 7.4 -
產品提供形式:Liquid
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應用范圍:ELISA, WB
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推薦稀釋比:
Application Recommended Dilution WB 1:500-1:5000 -
Protocols:
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儲存條件:Upon receipt, store at -20°C or -80°C. Avoid repeated freeze.
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貨期:Basically, we can dispatch the products out in 1-3 working days after receiving your orders. Delivery time maybe differs from different purchasing way or location, please kindly consult your local distributors for specific delivery time.
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用途:For Research Use Only. Not for use in diagnostic or therapeutic procedures.
相關產品
靶點詳情
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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.
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基因功能參考文獻:
- study identified K91 and K109 as the major sites whose acetylation level in vivo increases in response to acetate PMID: 25388160
- the enhanced reactivity of CheY DR reflected partial acquisition of catalytic and structural features of HAD phosphatases. PMID: 25928369
- 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
- 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
- F214A substitution in P2 of CheA caused 1,000-fold reduction in CheA-CheY binding affinity. PMID: 21642453
- 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
- 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
- Chemotaxis signaling protein CheY binds to the rotor protein FliN to control the direction of flagellar rotation in Escherichia coli. PMID: 20439729
- turnover of FliM molecules depends on the presence of active CheY, suggesting a potential role in the process of motor switching PMID: 20498085
- 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
- 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
- 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
- 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
- Data suggest that CheY initially misfolds before accessing the native conformation. PMID: 18619461
- Results describe the subdomain competition, cooperativity, and topological frustration in the folding of CheY. PMID: 18644380
- 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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亞細胞定位:Cytoplasm.
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數據庫鏈接:
KEGG: ecj:JW1871
STRING: 316385.ECDH10B_2023
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