关键信息
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基因名
dotB
- 应用
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别名
dotB；Dothistromin biosynthesis peroxidase dotB
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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
Q83B70
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表达区间
1-372aa
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氨基酸序列
MIEKSQRYPNEPSRFEPKHIDDLLIYCHRLGASDITIQTGRAVLAEVYGRLQTLTRRELSNAETSDLLNAIYGPNGTTQIMRGEDIDTHYEIRPNRNERFRYRINGTGCHVDGHEGIQITIRAIPAEPPLLSKLDLPAAIVDAIAPQEGVVYVTGATGSGKSTLLAAIIRELAEAPDSHRKILTYEAPIEYVYDSLTTPTASVCQSEIPRHLNSFAAGVRNALRRKPHAILVGEARDNETISAVLEAALTGHPVYTTLHSSGVAETIRRLVGSFPAEERIGRTIDIIETLRLIIWQRLVPSVDGKRVALREFLVFKEEIRDLLLDSDPEQITAAVRRLVAEHGQPMQVDVEAKFKGGLISERLYKILSASQE
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分子量
45.4 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.
质检流程
相关产品
背景信息
The study of dotB recombinant protein is rooted in its critical role in understanding bacterial virulence and pathogenicity, particularly in the context of pathogenic Escherichia coli strains. DotB is a component of the "defective organelle-targeting" (DOT) system, which is employed by certain bacteria to manipulate host cellular processes to their advantage. Investigating dotB and its associated proteins provides insights into the mechanisms of host-pathogen interactions, immune evasion, and the potential development of novel therapeutic strategies against bacterial infections. Given the increasing prevalence of antibiotic-resistant bacteria, understanding the molecular functions of virulence factors such as dotB is essential for the design of effective vaccines and alternative treatments. Additionally, the production and characterization of dotB recombinant protein facilitate the exploration of its structure-function relationships, providing a platform for biochemical studies that can reveal its potential as a target for drug discovery. Overall, this research not only contributes to the fundamental knowledge of bacterial pathogenesis but also underscores the necessity for innovative approaches to combat infectious diseases.
