| 纯度 | >90%SDS-PAGE. |
| 种属 | E.col |
| 靶点 | lasB |
| Uniprot No | P14756 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 198-498aa |
| 氨基酸序列 | AEAGGPGGNQKIGKYTYGSDYGPLIVNDRCEMDDGNVITVDMNSSTDDSKTTPFRFACPTNTYKQVNGAYSPLNDAHFFGGVVFKLYRDWFGTSPLTHKLYMKVHYGRSVENAYWDGTAMLFGDGATMFYPLVSLDVAAHEVSHGFTEQNSGLIYRGQSGGMNEAFSDMAGEAAEFYMRGKNDFLIGYDIKKGSGALRYMDQPSRDGRSIDNASQYYNGIDVHHSSGVYNRAFYLLANSPGWDTRKAFEVFVDANRYYWTATSNYNSGACGVIRSAQNRNYSAADVTRAFSTVGVTCPSAL |
| 预测分子量 | 35.2 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lasB重组蛋白的3篇参考文献及其摘要概括：
1. **《Cloning, expression, and characterization of the Pseudomonas aeruginosa elastase (lasB) gene in Escherichia coli》**
- 作者：Kessler E, Safrin M
- 摘要：研究报道了将绿脓杆菌lasB基因克隆至大肠杆菌中并成功表达重组LasB弹性蛋白酶，分析了其酶活性和底物特异性，为后续致病机制研究奠定基础。
2. **《Crystal structure of Pseudomonas aeruginosa elastase LasB》**
- 作者：Bode W, Gomis-Rüth FX
- 摘要：通过X射线晶体学解析了重组LasB蛋白的三维结构，揭示了其锌离子依赖性催化机制及底物结合位点，为设计特异性抑制剂提供结构依据。
3. **《Recombinant LasB protease as a potential vaccine candidate against Pseudomonas aeruginosa infections》**
- 作者：Luna-Ramírez K, et al.
- 摘要：评估了重组LasB蛋白作为疫苗的潜力，动物实验显示其能诱导免疫反应并提高小鼠对绿脓杆菌感染的存活率，表明其在免疫防治中的应用前景。
(注：以上文献信息为示例，实际引用时需核对真实论文数据。若需准确文献，建议通过PubMed或SciHub搜索关键词“lasB recombinant protein”获取最新研究。)
LasB, also known as pseudolysin or elastase, is a key virulence factor produced by the opportunistic pathogen *Pseudomonas aeruginosa*. This zinc-dependent metalloprotease belongs to the M4 peptidase family and is renowned for its broad substrate specificity, enabling the degradation of host proteins such as elastin, collagen, immunoglobulins, and complement components. Its enzymatic activity contributes significantly to tissue damage, immune evasion, and bacterial dissemination during infections, particularly in chronic lung diseases like cystic fibrosis and in wound or burn injuries.
The *lasB* gene encoding this enzyme is regulated by the quorum-sensing (QS) system, aligning its production with bacterial population density. Recombinant LasB protein is commonly expressed in heterologous systems (e.g., *E. coli*) for structural and functional studies, bypassing the need to culture pathogenic *P. aeruginosa*. This approach allows safer, high-yield production and facilitates research into its enzymatic mechanisms, substrate interactions, and role in pathogenesis.
Studies leveraging recombinant LasB have advanced the development of inhibitory compounds and vaccines targeting *P. aeruginosa* infections. Its crystal structure, resolved in the 1990s, revealed a conserved HEXXH zinc-binding motif and a substrate-binding cleft, providing insights for rational drug design. Additionally, LasB serves as a model protease for exploring metalloenzyme catalysis and host-pathogen interactions. Despite its pathogenic role, engineered forms of LasB have potential biotechnological applications, including bioactive peptide synthesis and environmental bioremediation. Overall, recombinant LasB remains a critical tool for understanding bacterial virulence and devising therapeutic strategies against multidrug-resistant *P. aeruginosa* infections.
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