| 纯度 | >90%SDS-PAGE. |
| 种属 | E.col |
| 靶点 | lasA |
| Uniprot No | P23826 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 32-68aa |
| 氨基酸序列 | STPVLASVA VSMELLPTAS VLYSDVAGCF KYSAKHHC |
| 预测分子量 | 7,2 kDa |
| 蛋白标签 | His tag N-Terminus |
| 缓冲液 | PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300. |
| 稳定性 & 储存条件 | Lyophilized protein should be stored at ≤ -20°C, stable for one year after receipt. Reconstituted protein solution can be stored at 2-8°C for 2-7 days. Aliquots of reconstituted samples are stable at ≤ -20°C for 3 months. |
| 复溶 | Always centrifuge tubes before opening.Do not mix by vortex or pipetting. It is not recommended to reconstitute to a concentration less than 100μg/ml. Dissolve the lyophilized protein in distilled water. Please aliquot the reconstituted solution to minimize freeze-thaw cycles. |
以下是关于lasA重组蛋白的3篇参考文献示例(文献信息为虚构，仅供格式参考)：
1. **文献名称**：*Expression and characterization of recombinant LasA protease from Pseudomonas aeruginosa*
**作者**：Smith J, et al.
**摘要**：研究报道了lasA基因在大肠杆菌中的重组表达，纯化后的LasA蛋白表现出对弹性蛋白的高效水解活性，证实其在细菌侵袭宿主过程中的潜在作用。
2. **文献名称**：*Structural analysis of LasA reveals a unique zinc-dependent metalloprotease mechanism*
**作者**：Lee H, et al.
**摘要**：通过X射线晶体学解析了重组LasA蛋白的三维结构，发现其活性位点的锌离子结合模式，为设计针对铜绿假单胞菌的抑制剂提供了结构基础。
3. **文献名称**：*LasA recombinant protein inhibits Staphylococcus aureus biofilm formation in vitro*
**作者**：Chen R, et al.
**摘要**：实验证明纯化的重组LasA蛋白可通过降解金黄色葡萄球菌胞外基质中的特定蛋白，显著抑制其生物膜形成，提示其作为抗菌辅助剂的潜力。
(注：以上内容为模拟示例，实际文献需通过学术数据库检索。)
**Background of Recombinant LasA Protein**
LasA, a secreted protease produced by *Pseudomonas aeruginosa*, is recognized for its role in the bacterium’s virulence and pathogenicity. Originally identified as a staphylolytic enzyme, LasA cleaves glycine-glycine bonds in peptidoglycan, contributing to cell lysis in *Staphylococcus aureus* and other Gram-positive bacteria. In *P. aeruginosa*, LasA works synergistically with other proteases, such as LasB (elastase), to degrade host tissues, evade immune responses, and facilitate biofilm formation—a critical factor in chronic infections. Its activity is linked to the destruction of elastin and collagen, exacerbating conditions like cystic fibrosis, burn wounds, and nosocomial infections.
Recombinant LasA protein is engineered through genetic cloning, typically by inserting the *lasA* gene into expression vectors (e.g., *E. coli* or yeast systems) to enable large-scale production. This approach allows for controlled purification and functional analysis, bypassing challenges associated with native protein extraction from *P. aeruginosa* cultures. Studies on recombinant LasA have clarified its structure-function relationships, including its zinc-dependent catalytic mechanism and substrate specificity.
Research on LasA has therapeutic implications. Inhibiting LasA activity is explored as a strategy to attenuate *P. aeruginosa* infections, particularly in antibiotic-resistant strains. Additionally, recombinant LasA serves as a tool for studying bacterial interactions, host-pathogen dynamics, and biofilm disruption. Its unique enzymatic properties also inspire biotechnological applications, such as engineered antimicrobial agents or biofilm-targeted treatments. Despite progress, understanding LasA’s regulatory networks and host-specific effects remains critical for translational applications.
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