| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | alp2 |
| Uniprot No | P87184 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 137-495aa |
| 氨基酸序列 | EDPTVEKSAPWGLARISHRDSLSFGTFNKYLYASEGGEGVDAYTIDTGINVDHVDFEGRAQWGKTIPTDDEDADGNGHGTHCSGTIAGRKYGVAKKANLYAVKVLRSSGSGTMSDVVAGVEWAVKSHLKKVKDAKDGKIKGFKGSVANMSLGGGKSRTLEAAVNAGVEAGLHFAVAAGNDNADACNYSPAAAENPITVGASTLQDERAYFSNYGKCTDIFAPGLNILSTWIGSKHAVNTISGTSMASPHIAGLLAYFVSLQPSKDSAFAVDELTPKKLKKDIIAIATQGALTDIPSDTPNLLAWNGGGSSNYTDIIASGGYKVNASVKDRFEGLVHKAEKLLTEELGAIYSEIHDAAVA |
| 预测分子量 | 45.0 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. |
以下是模拟生成的关于ALP2重组蛋白的参考文献示例(非真实文献，仅作格式参考)：
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1. **文献名称**: *Optimized Expression and Characterization of Recombinant ALP2 in Pichia pastoris*
**作者**: Wang Y, Li H, et al.
**摘要**: 研究利用毕赤酵母系统高效表达重组ALP2蛋白，通过发酵条件优化和糖基化修饰分析，证实其酶活性显著高于原核表达系统，适用于工业化生产。
2. **文献名称**: *Therapeutic Potential of Recombinant ALP2 in Chronic Kidney Disease*
**作者**: Gupta R, Patel S.
**摘要**: 在小鼠模型中验证重组ALP2通过调节磷酸盐代谢缓解慢性肾病症状，揭示了其作为代谢疾病治疗靶点的潜力。
3. **文献名称**: *Cryo-EM Structure of Recombinant ALP2 Reveals Substrate Binding Mechanisms*
**作者**: Müller F, Schmidt D.
**摘要**: 通过冷冻电镜解析重组ALP2的底物结合构象，结合分子动力学模拟阐明催化循环机制，为设计特异性抑制剂提供结构基础。
4. **文献名称**: *Functional Crosstalk Between ALP2 and Inflammatory Pathways in Macrophages*
**作者**: Kim S, Park J.
**摘要**: 发现重组ALP2通过调控NF-κB信号通路抑制巨噬细胞过度炎症反应，提出其在抗炎治疗中的新应用方向。
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以上示例涵盖表达优化、疾病治疗、结构机制及功能研究等方向，供参考文献格式及内容概括使用。如需真实文献，建议通过学术数据库(如PubMed、Web of Science)检索关键词“ALP2 recombinant protein”或结合具体研究背景细化检索策略。
**Background of ALP2 Recombinant Protein**
ALP2. or alkaline phosphatase 2. is a recombinant protein derived from the alkaline phosphatase (ALP) enzyme family, which plays critical roles in phosphate metabolism, including dephosphorylation and mineralization processes. The ALP family is broadly categorized into tissue-specific isoforms (e.g., intestinal, placental) and tissue-nonspecific alkaline phosphatase (TNAP), with ALP2 often associated with the latter. Recombinant ALP2 is engineered using molecular cloning techniques, where the ALP2 gene is inserted into expression systems like *E. coli*, yeast, or mammalian cells to produce a purified, bioactive protein.
The development of recombinant ALP2 addresses challenges in studying native ALP isoforms, such as low natural abundance, purification complexity, and cross-reactivity in assays. Its recombinant form ensures high purity, consistency, and scalability, making it valuable for research and therapeutic applications. Structurally, ALP2 retains key domains essential for enzymatic activity, including metal-binding sites for magnesium and zinc ions required for catalytic function.
In research, recombinant ALP2 is widely used to investigate bone mineralization, cellular signaling, and biomarker detection in diseases like hypophosphatasia (a genetic disorder linked to ALP deficiency). It also serves as a tool in molecular biology for enzyme-linked assays (ELISA, Western blot) and phage display systems. Therapeutically, ALP2 variants are explored for enzyme replacement therapies or as targeting agents in drug delivery due to their substrate-specific activity.
Recent advancements focus on optimizing ALP2’s stability, substrate specificity, and immunocompatibility through protein engineering. These efforts aim to enhance its utility in diagnostics, biomanufacturing, and regenerative medicine. Overall, ALP2 recombinant protein exemplifies the intersection of biotechnology and enzymology, offering versatile solutions for both basic science and clinical innovation.
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