Analytical Data
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基因名
disA
- Application
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别名
disA；DNA integrity scanning Protein DisA
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种属
E.coli
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表达系统
E. coli
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标签
His tag N-Terminus
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
Q743W9
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表达区间
1-357aa
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氨基酸序列
MTRPTLRETVARLAPGTGLRDGLERILRGRTGALIVLGNDENVEAICDGGFALDVRYAPTRLRELAKMDGAVVLSTDGSRIVRANVQLVPDPSIATDESGTRHRSAERAAIQTGYPVISVSHSMNIVTVYVGGERHVVADSATILSRANQAIATLERYKIRLDEVSRQLSRAEIEDFVTLRDVLTVVQRLELVRRIGQVIDNDVVELGTDGRQLRLQLDELLGGNDNARELIVRDYHASPEQLSEAQMTATLDELDALSDTELLDFTALAKVFGYPTTTEAQDSAVSPRGYRALAGIPRLQFAHADLLVRSFGTLQNVLAASASDLQSIDGIGAMWARHVREGLSQLAESTITDSLS
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分子量
45.9 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
DisA is a protein that plays a crucial role in bacterial signal transduction, specifically in the regulation of the stringent response in organisms such as Bacillus subtilis. Understanding the mechanisms of DisA is important because it links the perception of nutritional stress to the synthesis of the alarmone (p)ppGpp, which modulates various cellular processes, including metabolism, growth, and virulence. The study of DisA involves examining its structural and functional properties, revealing how it senses changes in the intracellular levels of nucleotide pools and translates these signals into appropriate cellular responses. Research has shown that DisA interacts with other proteins and can form oligomers, suggesting a complex regulatory network. Additionally, the insights gained from DisA studies not only enhance our knowledge of bacterial physiology but also have potential applications in developing antibacterial strategies by targeting this regulatory pathway, making it an attractive focus for both fundamental and applied microbiological research. As antibiotic resistance continues to pose a global threat, unraveling the roles of proteins like DisA could lead to innovative therapeutic approaches that disrupt bacterial survival mechanisms.
