纯度 | >95%SDS-PAGE. |
种属 | Human |
靶点 | PPA1 |
Uniprot No | Q15181 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 1-289aa |
氨基酸序列 | MGSSHHHHHHSSGLVPRGSHMGSHMSGFSTEERAAPFSLEYRVFLKNEKG QYISPFHDIPIYADKDVFHMVVEVPRWSNAKMEIATKDPLNPIKQDVKKG KLRYVANLFPYKGYIWNYGAIPQTWEDPGHNDKHTGCCGDNDPIDVCEIG SKVCARGEIIGVKVLGILAMIDEGETDWKVIAINVDDPDAANYNDINDVK RLKPGYLEATVDWFRRYKVPDGKPENEFAFNAEFKDKDFAIDIIKSTHDH WKALVTKKTNGKGISCMNTTLSESPFKCDPDAARAIVDALPPPCESACTV PTDVDKWFHHQKN |
预测分子量 | 35 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PPA1重组蛋白的假设性参考文献示例(注:内容为模拟生成,非真实文献):
1. **《重组人PPA1蛋白在大肠杆菌中的高效表达及纯化》**
- 作者:Zhang L, Wang Y, Chen H
- 摘要:本研究构建了人源PPA1基因的原核表达载体,通过优化诱导条件在大肠杆菌中实现可溶性表达,并采用离子交换层析获得高纯度重组蛋白,酶活测定显示其具有高效焦磷酸盐水解能力。
2. **《PPA1的晶体结构解析及其催化机制研究》**
- 作者:Smith J, Tanaka K, Müller R
- 摘要:通过X射线晶体学解析了重组PPA1蛋白的3D结构,揭示了其活性中心关键氨基酸残基的构象,结合分子动力学模拟阐明了Mg²⁺依赖性催化反应的分子机制。
3. **《基于PPA1重组酶的ATP再生系统在体外合成中的应用》**
- 作者:Gupta S, Lee T, Park S
- 摘要:开发了一种利用重组PPA1与多聚磷酸激酶耦合的ATP再生系统,显著提高了体外酶法合成代谢产物(如核苷酸)的效率,为生物催化工业化提供了新策略。
(提示:实际文献检索需通过PubMed、Web of Science等学术数据库,以具体研究内容关键词进行查询。)
**Background of PPA1 Recombinant Protein**
Purple acid phosphatase 1 (PPA1), also known as acid phosphatase 1 or uteroferrin-associated phosphatase, is a metalloenzyme belonging to the histidine acid phosphatase family. It is characterized by its conserved active-site motifs and a binuclear metal center, typically containing iron and zinc or manganese ions. PPA1 plays a critical role in cellular metabolism, including phosphate ester hydrolysis, reactive oxygen species (ROS) regulation, and bone resorption. Its expression is observed in diverse tissues, including bone, spleen, and macrophages, and it has been implicated in physiological processes such as immune response, osteoclast differentiation, and iron homeostasis.
The recombinant form of PPA1 is produced using biotechnological platforms, such as *E. coli* or mammalian expression systems, to enable large-scale, high-purity protein production. Recombinant PPA1 retains the enzymatic activity and structural integrity of its native counterpart, making it valuable for biochemical studies, drug discovery, and therapeutic applications. For instance, its role in bone metabolism has spurred research into osteoporosis treatments, while its antioxidant properties are explored for mitigating oxidative stress-related diseases.
PPA1's unique redox-active metal center also positions it as a model for studying metalloenzyme mechanisms. Dysregulation of PPA1 has been linked to pathological conditions, including cancer metastasis and neurodegenerative disorders, highlighting its potential as a biomarker or therapeutic target. Advances in recombinant DNA technology have facilitated structural and functional analyses, deepening insights into PPA1's biological significance and expanding its applications in both basic and applied biomedical research.
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