关键信息
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基因名
EsxA
- 应用
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别名
ESAT-6 (esaT6)
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种属
Mycobacterium bovis
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表达系统
E. coli
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标签
N- His & C- Myc
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
P0A565
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表达区间
2-95aa
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分子量
17.2 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.
质检流程
相关产品
背景信息
EsxA, a vital type VII secretion system protein found in mycobacteria, particularly in Mycobacterium tuberculosis, has gained significant attention in the field of microbiology and immunology due to its crucial role in bacterial pathogenicity and immune evasion. This protein is part of a larger family of ESX (Esx-1, Esx-2) secretion systems, which are known to transport effector proteins to the host's immune cells, manipulating host responses to promote bacterial survival and replication. Research on EsxA and its interactions with host immune mechanisms has revealed its potential to modulate immune responses, making it an attractive target for vaccine development and therapeutic interventions. Previous studies highlighted EsxA’s ability to elicit strong T-cell responses, suggesting its role as a promising candidate for subunit vaccines against tuberculosis. Furthermore, understanding the structural and functional characteristics of EsxA is essential for deciphering its mechanism of action and the overall pathogenicity of M. tuberculosis. Investigating EsxA not only enhances our knowledge of mycobacterial virulence factors but also contributes to the broader field of infectious disease research, informing strategies for tackling antibiotic resistance and improving public health outcomes. As the global burden of tuberculosis remains a pressing issue, continued exploration of the EsxA protein is imperative for advancing scientific efforts toward effective prevention and treatment methods.
