Analytical Data
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基因名
ynaB
- Application
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别名
ynaB; BSU17500; Uncharacterized protein YnaB
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种属
Bacillus subtilis
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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
P94480
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表达区间
1-144aa
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分子量
32.8 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
YnaB is a protein of significant interest in bacterial physiology and biochemistry, primarily due to its potential role in stress responses and cellular signaling. Discovered in *Escherichia coli*, YnaB has been implicated in the regulation of biofilm formation and adaptation to changing environmental conditions, such as nutrient availability and temperature fluctuations. The study of YnaB offers insights into the mechanisms through which bacteria respond to external stimuli, which is crucial for understanding pathogenicity and the development of antibiotic resistance. The recombinant expression of YnaB enables researchers to investigate its structural and functional properties in detail, facilitating the exploration of its interactions with other biomolecules. Through techniques such as X-ray crystallography and NMR spectroscopy, scientists aim to elucidate the protein's three-dimensional structure, which can reveal its biochemical pathways and potential as a target for novel therapeutic strategies. Furthermore, understanding YnaB's role could shed light on broader bacterial survival mechanisms, ultimately contributing to advancements in microbial biotechnology and medical research.
