Analytical Data
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基因名
troA
- Application
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别名
troA；troMP1；Zinc-binding Protein TroA
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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
P96116
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表达区间
23-308aa
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氨基酸序列
FGSKDAAADGKPLVVTTIGMIADAVKNIAQGDVHLKGLMGPGVDPHLYTATAGDVEWLGNADLILYNGLHLETKMGEVFSKLRGSRLVVAVSETIPVSQRLSLEEAEFDPHVWFDVKLWSYSVKAVYESLCKLLPGKTREFTQRYQAYQQQLDKLDAYVRRKAQSLPAERRVLVTAHDAFGYFSRAYGFEVKGLQGVSTASEASAHDMQELAAFIAQRKLPAIFIESSIPHKNVEALRDAVQARGHVVQIGGELFSDAMGDAGTSEGTYVGMVTHNIDTIVAALAR
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分子量
38.2 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
TroA, a critical protein involved in bacterial iron transport, has garnered significant attention due to its role in the pathogenesis of various bacterial infections. This protein functions as a tonB-dependent receptor, facilitating the uptake of iron from the host environment, which is essential for bacterial growth and virulence. Research on TroA is particularly relevant in the context of pathogenic bacteria such as Neisseria meningitidis and Haemophilus influenzae, where iron acquisition mechanisms are key to understanding infection dynamics and developing therapeutic strategies. The ability of TroA to adapt to different environmental iron levels highlights its potential as a target for antibiotic development. Recent advances in recombinant protein technology have enabled the efficient production and purification of TroA, allowing for further investigations into its structure, function, and interaction with other molecular components. By studying the properties of TroA, researchers aim to elucidate its role in bacterial iron metabolism, identify potential inhibitors, and ultimately contribute to the development of novel antimicrobial agents. Understanding the mechanisms underlying TroA's function not only advances our knowledge of microbial physiology but also paves the way for innovative strategies to combat bacterial infections that exploit iron acquisition pathways.
