| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | PLAP |
| Uniprot No | P05187 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 117-447aa |
| 氨基酸序列 | TATAYLCGVKGNFQTIGLSAAARFNQCNTTRGNEVISVMNRAKKAGKSVGVVTTTRVQHASPAGTYAHTVNRNWYSDADVPASARQEGCQDIATQLISNMDIDVILGGGRKYMFRMGTPDPEYPDDYSQGGTRLDGKNLVQEWLAKRQGARYVWNRTELMQASLDPSVTHLMGLFEPGDMKYEIHRDSTLDPSLMEMTEAALRLLSRNPRGFFLFVEGGRIDHGHHESRAYRALTETIMFDDAIERAGQLTSEEDTLSLVTADHSHVFSFGGYPLRGSSIFGLAPGKARDRKAYTVLLYGNGPGYVLKDGARPDVTESESGSPEYRQQSAV |
| 预测分子量 | 41.9 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3篇关于PLAP(胎盘碱性磷酸酶)重组蛋白的参考文献示例(注：以下为模拟内容，实际文献需根据具体数据库检索)：
1. **文献名称**: *"Expression and Characterization of Recombinant Human Placental Alkaline Phosphatase in E. coli"*
**作者**: Smith J., Brown K.
**摘要**: 研究报道了在大肠杆菌系统中高效表达重组人PLAP的方法，通过优化密码子和纯化步骤获得高活性酶，并验证其在免疫检测中的适用性。
2. **文献名称**: *"Functional Analysis of PLAP Isoenzymes in Cancer Diagnostics"*
**作者**: Lee S., et al.
**摘要**: 探讨重组PLAP同工酶在卵巢癌和精原细胞瘤中的表达差异，证明其作为肿瘤标志物的潜力，并开发了基于重组蛋白的ELISA检测技术。
3. **文献名称**: *"Structural Insights into PLAP Catalytic Mechanism via Site-Directed Mutagenesis"*
**作者**: Garcia R., et al.
**摘要**: 通过重组PLAP的定点突变实验，解析其催化活性中心的结构特征，揭示关键氨基酸残基对酶活性和稳定性的影响。
如需具体文献，建议通过PubMed或Web of Science检索关键词“recombinant placental alkaline phosphatase”获取最新研究。
**Background of Recombinant PLAP Protein**
Placental Alkaline Phosphatase (PLAP) is a tissue-specific isoenzyme belonging to the alkaline phosphatase (ALP) family, primarily expressed in the placenta during pregnancy. It plays a role in nutrient absorption, cellular differentiation, and bone mineralization by catalyzing the hydrolysis of phosphate esters. Unlike other ALP isoforms (e.g., intestinal or tissue-nonspecific ALP), PLAP is distinguished by its heat stability, unique glycosylation patterns, and immunogenicity.
Recombinant PLAP is produced using genetic engineering techniques, where the *ALPP* gene encoding PLAP is inserted into expression systems like *E. coli*, yeast, or mammalian cells (e.g., CHO or HEK293). Mammalian systems are preferred for generating glycosylated, biologically active PLAP, while prokaryotic systems yield non-glycosylated forms suitable for structural studies. The recombinant protein is purified via affinity chromatography, ensuring high purity and consistency.
PLAP has significant research and diagnostic applications. It serves as a biomarker for certain cancers (e.g., ovarian or testicular germ cell tumors) due to its ectopic expression in malignancies. In biotechnology, recombinant PLAP is utilized as a reporter enzyme in immunoassays (e.g., ELISA) or cell-based assays to monitor gene expression or cell viability. Its thermal stability and distinct enzymatic activity make it ideal for multiplex assays where differentiation from other ALPs is critical.
Additionally, recombinant PLAP aids in studying placental development, tumor biology, and alkaline phosphatase function. Its production avoids ethical concerns associated with placental extraction and ensures scalability for industrial or clinical use. Ongoing research explores its therapeutic potential, including enzyme replacement therapies or targeted cancer treatments. Overall, recombinant PLAP bridges biomedical research and clinical applications, leveraging its unique biochemical properties.
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