Analytical Data
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基因名
lasA
- Application
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别名
lasA;PRKACN1;cAMP-dependent Protein kinase inhibitor alpha
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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
P23826
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表达区间
32-68aa
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氨基酸序列
STPVLASVA VSMELLPTAS VLYSDVAGCF KYSAKHHC
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分子量
7.2 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
LasA is a lysin derived from Pseudomonas aeruginosa, a significant opportunistic pathogen associated with various infections, especially in immunocompromised individuals. Understanding LasA and its recombinant forms has garnered substantial attention due to its potential therapeutic applications, particularly in combating antibiotic-resistant bacterial strains. Research on LasA has focused on its role in bacterial cell wall lysis, as it exhibits endopeptidase activity that specifically targets the peptidoglycan layer, promoting cell death in Gram-positive bacteria. Recombinant protein technology has enabled the production of LasA in heterologous systems, facilitating detailed studies of its structure-function relationships and enhancing its potential application in biomedicine. The ability to engineer LasA variants with improved stability and efficacy has opened avenues for developing novel antimicrobial agents, offering alternative treatment strategies against P. aeruginosa infections and other resistant pathogens. Additionally, understanding the mechanisms by which LasA interacts with bacterial cell walls contributes to the broader field of antibacterial drug development and resistance mitigation. Overall, the research on LasA recombinant proteins stands at the intersection of microbiology, biochemistry, and therapeutic development, addressing the urgent need for new antimicrobial solutions in the face of rising resistance challenges.












