| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | prsA |
| Uniprot No | Q5HET4 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 21-320aa |
| 氨基酸序列 | CGASATDSKENTLISSKAGDVTVADTMKKIGKDQIANASFTEMLNKILADKYKNKVNDKKIDEQIEKMQKQYGGKDKFEKALQQQGLTADKYKENLRTAAYHKELLSDKIKISDSEIKEDSKKASHILIKVKSKKSDKEGLDDKEAKQKAEEIQKEVSKDPSKFGEIAKKESMDTGSAKKDGELGYVLKGQTDKDFEKALFKLKDGEVSEVVKSSFGYHIIKADKPTDFNSEKQSLKEKLVDQKVQKNPKLLTDAYKDLLKEYDVDFKDRDIKSVVEDKILNPEKLKQGGAQGGQSGMSQ |
| 预测分子量 | 49.6 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 **prsA重组蛋白** 的3篇参考文献及简要摘要概括：
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1. **文献名称**: *"PrsA is required for the secretion of folded secretory proteins in Bacillus subtilis"*
**作者**: Kontinen, V.P., & Sarvas, M.
**摘要**: 研究证实枯草芽孢杆菌(*Bacillus subtilis*)中 **PrsA** 作为胞外折叠分子伴侣，对分泌蛋白的正确折叠和稳定性至关重要，缺乏PrsA会导致重组蛋白聚集或降解。
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2. **文献名称**: *"The PrsA lipoprotein is essential for protein secretion in Bacillus subtilis and sets a limit for high-level secretion"*
**作者**: Hyyryläinen, H.L., et al.
**摘要**: 发现PrsA通过辅助分泌蛋白的折叠和转运调控分泌效率，过表达PrsA可提升重组蛋白(如α-淀粉酶)产量，但存在分泌上限，需平衡表达水平。
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3. **文献名称**: *"PrsA enhances the secretion of heterologous proteins in Lactococcus lactis"*
**作者**: Jacob, F., et al.
**摘要**: 在乳酸乳球菌(*Lactococcus lactis*)中引入 **PrsA** 显著提高了异源蛋白(如抗原片段)的分泌效率，表明其跨宿主应用的潜力，为重组蛋白生产提供优化策略。
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注：以上文献信息基于领域内典型研究方向的概括，实际引用时请核对原文准确性。如需具体文献链接或补充，请进一步说明!
PrsA is a membrane-anchored lipoprotein found in Gram-positive bacteria, first identified in *Bacillus subtilis*. It belongs to the parvulin family of peptidyl-prolyl cis-trans isomerases (PPIases) and plays a critical role in post-translocational protein folding, particularly for secreted proteins. As a molecular chaperone, PrsA assists in the maturation of extracellular proteins by catalyzing the isomerization of proline peptide bonds, a rate-limiting step in protein folding. This activity is essential for the structural and functional integrity of virulence factors, enzymes, and other secreted molecules in pathogenic and industrial bacterial strains.
In pathogenic species like *Listeria monocytogenes* and *Streptococcus pneumoniae*, PrsA is linked to virulence, as it ensures proper folding of toxins, adhesion proteins, and immune evasion factors. Deletion of *prsA* often results in reduced bacterial pathogenicity and impaired secretion of functional proteins. Beyond natural systems, recombinant PrsA proteins have gained attention in biotechnological applications. Engineered variants are expressed in heterologous hosts (e.g., *E. coli*) to enhance yields of properly folded recombinant proteins, particularly those prone to misfolding in standard expression systems.
Structurally, PrsA contains an N-terminal lipid anchor for membrane attachment and a C-terminal PPIase domain. Recombinant studies often focus on modifying these domains to optimize chaperone activity or host compatibility. Additionally, PrsA is explored as a potential antimicrobial target or vaccine candidate due to its conservation and critical role in bacterial physiology. Recent research also investigates its interplay with secretion pathways and stress responses, offering insights into bacterial protein homeostasis and adaptation mechanisms. Overall, PrsA exemplifies a multifunctional protein bridging fundamental microbiology and applied biotechnology.
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