Analytical Data
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基因名
LapB
- Application
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别名
Legionella pneumophila subsp. pneumophila (strain Philadelphia 1 / ATCC 33152 / DSM 7513); Aminopeptidase; Hydrolase; Protease
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种属
Human
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表达系统
E. coli
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标签
Tag Free
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
Q5ZZH8
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表达区间
S24-N397
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蛋白长度
Full Length of Mature Protein (with Propeptide)
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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
LapB is a crucial protein involved in bacterial adhesion and biofilm formation, primarily studied in the context of Pseudomonas aeruginosa and other opportunistic pathogens. It plays a significant role in the bacteria's ability to adhere to surfaces and form structured communities, contributing to its virulence and resistance to antibiotics. Biofilms, which consist of densely packed bacterial cells encased in a self-produced extracellular matrix, pose a major challenge in clinical settings as they can lead to chronic infections and are difficult to eradicate. Understanding the biochemical properties and mechanisms of LapB, including its role in cell-surface interactions and its regulatory pathways, is essential for developing new therapeutic strategies to combat biofilm-associated infections. Recent studies have employed various techniques, such as molecular cloning, protein purification, and functional assays, to elucidate the structure-function relationship of LapB and its interactions with other cellular components. Investigating LapB's potential as a target for antibacterial drug development could pave the way for innovative approaches to manage persistent infections caused by biofilm-forming bacteria.
