| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | pal |
| Uniprot No | P0A913 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 22-173aa |
| 氨基酸序列 | CSSNKNASNDGSEGMLGAGTGMDANGGNGNMSSEEQARLQMQQLQQNNIVYFDLDKYDIRSDFAQMLDAHANFLRSNPSYKVTVEGHADERGTPEYNISLGERRANAVKMYLQGKGVSADQISIVSYGKEKPAVLGHDEAAYSKNRRAVLVY |
| 预测分子量 | 18.8kDa |
| 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PAL(苯丙氨酸解氨酶)重组蛋白的3篇代表性文献摘要：
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1. **文献名称**：*"A different approach to treatment of phenylketonuria: Phenylalanine degradation with recombinant phenylalanine ammonia lyase"*
**作者**：Sarkissian, C. N., et al.
**摘要**：该研究报道了在大肠杆菌中重组表达PAL蛋白的优化策略，并评估其在苯丙酮尿症(PKU)小鼠模型中的治疗效果。实验表明，重组PAL能有效降低血液中苯丙氨酸浓度，且通过聚乙二醇(PEG)修饰可显著延长其体内半衰期。
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2. **文献名称**：*"Structural and functional characterization of a thermostable phenylalanine ammonia-lyase from *Rhodosporidium toruloides*"*
**作者**：Fernández, M., et al.
**摘要**：研究通过基因克隆在酵母中高效表达来源于红酵母的PAL，解析其晶体结构并鉴定关键活性位点。通过理性设计突变体，提高了酶的热稳定性和催化效率，为工业化生产提供理论依据。
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3. **文献名称**：*"Immobilization of recombinant phenylalanine ammonia lyase for repeated degradation of phenylalanine"*
**作者**：Wang, L., et al.
**摘要**：开发了一种基于纳米材料的PAL固定化技术，证明固定化酶在重复使用后仍保持高活性，且对极端pH和温度条件耐受性增强，为生物催化及PKU治疗中的酶再利用提供了新方法。
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注：以上文献为模拟示例，实际引用时建议通过数据库(如PubMed、Web of Science)核实具体信息。
**Background of PAL Recombinant Protein**
The PAL (Peptidoglycan-associated lipoprotein) recombinant protein is a engineered version of a naturally occurring bacterial protein, primarily studied in Gram-negative bacteria like *Escherichia coli*. PAL is anchored to the outer membrane and non-covalently linked to the peptidoglycan layer, playing a critical role in maintaining structural integrity and stabilizing the connection between the outer membrane and the cell wall. Its interaction with the Tol-Pal system, a multiprotein complex, is essential for membrane integrity, cell division, and virulence in pathogenic strains.
Recombinant PAL is produced via genetic engineering, where the *pal* gene is cloned into expression vectors (e.g., plasmids) and expressed in host systems like *E. coli*. This allows large-scale production of purified PAL for research. The protein’s conserved structure and functional domains—such as its N-terminal lipid anchor and peptidoglycan-binding domain—are retained in recombinant forms, enabling studies on bacterial envelope dynamics, host-pathogen interactions, and antibiotic resistance mechanisms.
PAL recombinant protein has become a valuable tool in vaccine development, as it is a potential antigen for targeting bacterial infections. It also aids in structural biology (e.g., crystallography) to elucidate mechanisms of membrane biogenesis. Additionally, its role in bacterial survival under stress conditions makes it a candidate for novel antimicrobial strategies. Research continues to explore its immunogenicity, cross-species conservation, and applications in synthetic biology for engineered bacterial systems.
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