| 纯度 | >95%SDS-PAGE. |
| 种属 | Escherichia coli |
| 靶点 | ppa |
| Uniprot No | P0A7A9 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-176aa |
| 氨基酸序列 | MGSSHHHHHHSSGLVPRGSHMSLLNVPAGKDLPEDIYVVIEIPANADPIK YEIDKESGALFVDRFMSTAMFYPCNYGYINHTLSLDGDPVDVLVPTPYPL QPGSVIRCRPVGVLKMTDEAGEDAKLVAVPHSKLSKEYDHIKDVNDLPEL LKAQIAHFFEHYKDLEKGKWVKVEGWENAEAAKAEIVASFERAKNK |
| 预测分子量 | 22 kDa i |
| 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PPA(苯丙氨酸解氨酶)重组蛋白的模拟参考文献示例(注：文献为虚构，仅供示例参考)：
1. **《高效表达重组苯丙氨酸解氨酶的大肠杆菌工程菌构建》**
作者：Zhang Y, Liu X, Wang J
摘要：研究通过密码子优化和启动子调控，在大肠杆菌中高效表达PPA重组蛋白，酶活达到120 U/mg，为工业化生产提供基础。
2. **《酵母表达系统生产PPA重组蛋白及其治疗苯丙酮尿症的潜力》**
作者：Johnson R, Smith T
摘要：利用毕赤酵母分泌表达PPA，纯化蛋白在小鼠模型中显著降低血苯丙氨酸水平，展示其作为酶替代疗法的应用前景。
3. **《PPA重组蛋白的固定化及其在食品工业中的应用》**
作者：Chen L, Kim H
摘要：将重组PPA固定于纳米磁珠，在酸性条件下保持80%活性，成功用于脱除果汁中的苯丙氨酸，提升产品安全性。
4. **《分子改造提升PPA重组蛋白的热稳定性研究》**
作者：Garcia M, Patel S
摘要：通过定点突变获得突变体PPA-D198H，其在50℃下半衰期延长至4小时，拓展了其在高温加工环境中的应用场景。
(提示：实际文献需通过PubMed、ScienceDirect等平台检索关键词"recombinant phenylalanine ammonia-lyase"或"PAL expression"。)
**Background of PPA Recombinant Proteins**
Recombinant proteins, engineered through genetic modification, have revolutionized biomedical research and therapeutic development. PPA (Pseudomonas aeruginosa protease A) recombinant proteins, in particular, are derived from the pathogenic bacterium *Pseudomonas aeruginosa*, a common opportunistic pathogen associated with hospital-acquired infections, especially in immunocompromised individuals. PPA is a zinc-metalloprotease known for its role in degrading host tissues, evading immune responses, and facilitating bacterial invasion. Its enzymatic activity disrupts proteins like collagen, elastin, and immunoglobulins, contributing to tissue damage and chronic infections.
The development of PPA recombinant proteins emerged from efforts to study its pathogenic mechanisms and devise targeted therapies. By cloning the *ppa* gene into expression systems like *E. coli* or yeast, researchers produce purified PPA for structural and functional analyses. This has enabled detailed studies of its substrate specificity, catalytic mechanisms, and interaction with host proteins. Additionally, recombinant PPA serves as an antigen for antibody production, aiding in diagnostic assays and vaccine development.
In therapeutics, inhibiting PPA activity is a potential strategy to mitigate *P. aeruginosa* virulence. Recombinant PPA is used to screen small-molecule inhibitors or design neutralizing antibodies. Beyond infectious diseases, its proteolytic properties have been explored in industrial applications, such as bio-detergents or peptide synthesis. Challenges remain in ensuring protein stability, scalability, and minimizing endotoxin contamination during production. Advances in protein engineering and expression technologies continue to refine PPA recombinant tools, highlighting their dual role in understanding pathogenesis and enabling translational innovations.
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