| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | IPP1 |
| Uniprot No | Q13522 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-171aa |
| 氨基酸序列 | MEQDNSPRKIQFTVPLLEPHLDPEAAEQIRRRRPTPATLVLTSDQSSPEIDEDRIPNPHLKSTLAMSPRQRKKMTRITPTMKELQMMVEHHLGQQQQGEEPEGAAESTGTQESRPPGIPDTEVESRLGTSGTAKKTAECIPKTHERGSKEPSTKEPSTHIPPLDSKGANSV |
| 预测分子量 | 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. |
以下是关于IPP1(无机焦磷酸酶1)重组蛋白的3篇参考文献及其摘要概括：
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1. **文献名称**：*Cloning, Expression, and Characterization of Recombinant Inorganic Pyrophosphatase from Saccharomyces cerevisiae*
**作者**：Chen, Y., et al.
**摘要**：本研究克隆并表达了酿酒酵母IPP1基因，通过大肠杆菌系统成功纯化重组蛋白，验证其酶活性和热稳定性，为焦磷酸代谢研究提供工具。
2. **文献名称**：*Functional Analysis of Human IPP1 through Recombinant Expression in E. coli*
**作者**：Smith, J., & Lee, K.
**摘要**：作者构建了人源IPP1重组表达载体，优化纯化条件后获得高纯度蛋白，并证实其在体外催化焦磷酸水解的功能，为疾病模型研究奠定基础。
3. **文献名称**：*Biotechnological Applications of Thermophilic IPP1: Enhanced Stability and Activity*
**作者**：Zhang, R., et al.
**摘要**：该文献从嗜热菌中克隆IPP1基因，重组蛋白在高温下表现优异活性和稳定性，探索其在工业生物催化及分子诊断中的潜在应用。
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注：以上文献为示例性概括，实际文献需通过数据库(如PubMed、Web of Science)检索确认。
IPP1 (Inorganic Pyrophosphatase 1), also known as inorganic pyrophosphatase, is a conserved enzyme that catalyzes the hydrolysis of inorganic pyrophosphate (PPi) into two orthophosphate (Pi) molecules. This reaction is critical for driving biosynthetic processes, such as nucleic acid synthesis, lipid metabolism, and bone mineralization, by preventing the accumulation of PPi, which can inhibit anabolic pathways. IPP1 plays a pivotal role in cellular energy metabolism and homeostasis, as the hydrolysis of PPi is thermodynamically favorable and supports the irreversibility of ATP-dependent reactions.
Recombinant IPP1 proteins are engineered using genetic cloning techniques, often expressed in bacterial (e.g., *E. coli*) or eukaryotic systems (e.g., yeast or mammalian cells) to ensure high yield and purity. These proteins retain the enzymatic activity of native pyrophosphatases and are widely utilized in biochemical research, industrial applications, and therapeutic development. For instance, recombinant IPP1 is employed in DNA sequencing and PCR protocols to degrade pyrophosphate byproducts, enhancing reaction efficiency. In structural biology, it serves as a model to study enzyme kinetics and metal ion cofactor dependencies (Mg²⁺ or Mn²⁺).
Therapeutic interest in IPP1 arises from its potential to address disorders linked to PPi dysregulation, such as calcium pyrophosphate deposition disease (CPPD) or vascular calcification. Recombinant variants with modified stability or activity are explored for enzyme replacement therapies. Additionally, IPP1 homologs in pathogens (e.g., *Plasmodium* or bacteria) are investigated as drug targets. The production of recombinant IPP1 avoids contaminants from native sources, ensuring reproducibility for research and clinical applications. Its simplicity, stability, and essential catalytic role make IPP1 a versatile tool in both basic science and biotechnology.
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