Analytical Data
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基因名
yihF
- Application
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别名
yihF; b3861; JW5574; Uncharacterized protein YihF
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种属
Escherichia coli
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表达系统
E. coli
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标签
N- His-SUMO
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
P32128
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表达区间
25-476aa
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分子量
66.1 kDa
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内毒素
< 1.0 EU per μg protein as determined by the LAL method.
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性状
Freeze-dried powder
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缓冲液
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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复溶方法
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- 个性化定制
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稳定性测试
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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保存条件 & 期限
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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运输条件
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
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Protein Description
YihF is a well-characterized protein in Escherichia coli that has garnered significant interest due to its role in regulating bacterial motility and biofilm formation. Research has shown that YihF functions as a regulatory protein in the bacterial signaling pathways, particularly in response to environmental stresses. It is believed to inhibit flagellar gene expression, thus influencing the switch between motile and sessile lifestyles in E. coli. Insights into its structure and function are critical for understanding bacterial adaptive mechanisms and could potentially inform the development of novel antimicrobial strategies. Recombination techniques to express YihF as a recombinant protein provide a valuable tool for studying its biochemical properties and interactions with other cellular components. Characterizing YihF's structure through methods such as X-ray crystallography or NMR spectroscopy can reveal important details about its functional domains and regulatory mechanisms. Furthermore, studying YihF in various conditions helps elucidate its role in pathogenesis and bacterial communication, making it a target of interest in the field of microbiology and biotechnology. Understanding YihF's activities and regulatory networks could illuminate broader aspects of microbial ecology and the evolution of bacterial behavior. Overall, the recombinant expression and study of YihF could contribute significantly to our understanding of bacterial biology and lead to practical applications in combating bacterial infections.












