Analytical Data
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基因名
lpqE
- Application
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别名
lpqE；Putative lipoProtein LpqE
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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
P9WK62
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表达区间
30-182aa
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氨基酸序列
CGAGQISQTANQKPAVNGNRLTINNVLLRDIRIQAVQTSDFIQPGKAVDLVLVAVNQSPDVSDRLVGITSDIGSVTVAGDARLPASGMLFVGTPDGQIVAPGPLPSNQAAKATVNLTKPIANGLTYNFTFKFEKAGQGSVMVPISAGLATPHE
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分子量
23.2 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
The study of lpqE, a gene found in the bacterium Mycobacterium tuberculosis, has gained significant attention due to its potential role in the pathogenicity and survival of this notorious pathogen. LpqE encodes a lipoprotein that is involved in the biogenesis of the bacterial cell envelope and may play a crucial role in immune evasion. Understanding the structure and function of lpqE is essential, as it might serve as a target for novel tuberculosis therapies and vaccine development. Previous research has indicated that lpqE interacts with the host's immune system, potentially influencing the persistence of Mycobacterium tuberculosis in human tissues. The recombinant expression of lpqE allows for detailed analysis of its biochemical properties and interactions, facilitating insights into its function and role in infection. Additionally, isolating the lpqE protein in a controlled environment provides opportunities to study its immunogenicity, which is vital for exploring its potential as a vaccine candidate. Overall, the investigation of lpqE and its recombinant protein form is critical in the broader context of tuberculosis research, aiming to unveil new strategies for combating this global health challenge. As researchers continue to dissect the complex mechanisms underlying mycobacterial infections, lpqE remains a promising focus that could lead to improved diagnostics and therapeutics for tuberculosis.
