Analytical Data
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基因名
lecA
- Application
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别名
Galactose-binding lectin
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种属
Pseudomonas aeruginosa
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表达系统
E. coli
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标签
N- His
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
Q05097
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表达区间
2-122aa
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分子量
16.8 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
LecA, a lectin protein originally derived from the pathogen Pseudomonas aeruginosa, has garnered considerable attention in biomedical research due to its significant role in bacterial adhesion, host cell recognition, and biofilm formation. Recognized for its ability to bind specific carbohydrates, LecA participates in the pathogenesis of various infections, making it a potential target for therapeutic interventions. Researchers have focused on recombinant LecA for its utility in various applications, including drug delivery and vaccine development. Understanding the structure-function relationship of LecA has enabled scientists to manipulate its properties for enhanced performance. By producing LecA as a recombinant protein, researchers aim to elucidate its binding mechanisms and explore its potential as an adjuvant in vaccine formulations, ultimately contributing to the design of novel strategies to combat Pseudomonas aeruginosa infections. Additionally, studying LecA offers insights into the broader field of glycoengineering and glycoprotein interactions, highlighting the importance of carbohydrate recognition in microbial pathogenesis and immune responses.
