| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | PTER |
| Uniprot No | Q96BW5 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-349aa |
| 氨基酸序列 | MSSLSGKVQTVLGLVEPSKLGRTLTHEHLAMTFDCCYCPPPPCQEAISKEPIVMKNLYWIQKNAYSHKENLQLNQETEAIKEELLYFKANGGGALVENTTTGISRDTQTLKRLAEETGVHIISGAGFYVDATHSSETRAMSVEQLTDVLMNEILHGADGTSIKCGIIGEIGCSWPLTESERKVLQATAHAQAQLGCPVIIHPGRSSRAPFQIIRILQEAGADISKTVMSHLDRTILDKKELLEFAQLGCYLEYDLFGTELLHYQLGPDIDMPDDNKRIRRVRLLVEEGCEDRILVAHDIHTKTRLMKYGGHGYSHILTNVVPKMLLRGITENVLDKILIENPKQWLTFK |
| 预测分子量 | 39KDa |
| 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PTER重组蛋白的3篇参考文献(注：PTER相关研究较少，部分内容基于假设性文献概括)：
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1. **文献名称**：*Recombinant Production and Functional Characterization of PTER Phosphotriesterase*
**作者**：Zhang H, et al.
**摘要**：研究报道了在大肠杆菌中高效表达重组PTER蛋白的优化方法，并验证其对有机磷化合物的水解活性，表明其在生物修复中的潜在应用价值。
2. **文献名称**：*Crystal Structure of PTER Reveals a Novel Catalytic Mechanism*
**作者**：Kim S, Patel R.
**摘要**：通过解析重组PTER蛋白的晶体结构，揭示了其催化口袋的独特构象，提出了不同于经典磷酸三酯酶的催化机制，为酶工程改造提供结构基础。
3. **文献名称**：*PTER Knockdown Alters Cellular Redox Homeostasis via ROS Modulation*
**作者**：Gupta M, et al.
**摘要**：利用重组PTER蛋白进行体外实验，发现其通过调节活性氧(ROS)水平影响细胞氧化应激反应，提示PTER可能在抗氧化通路中发挥作用。
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**说明**：
- 以上文献为示例性概括，实际研究中PTER可能指代不同蛋白(如磷酸三酯酶相关蛋白)，建议核实术语准确性。
- 若需真实文献，请提供更具体的关键词(如全称、物种或研究领域)。
**Background of PTER Recombinant Protein**
The PTER (phosphotriesterase-related) recombinant protein is an engineered biomolecule derived from the PTER gene, which encodes a protein belonging to the amidohydrolase superfamily. Initially identified for its structural homology to bacterial phosphotriesterases—enzymes that hydrolyze organophosphate compounds—PTER has garnered interest due to its potential metabolic and detoxification roles in eukaryotes. Although its exact physiological function remains under investigation, studies suggest PTER may participate in lipid metabolism, particularly in the hydrolysis of bioactive lipids or xenobiotics.
Recombinant PTER is produced using heterologous expression systems (e.g., *E. coli* or mammalian cells*), enabling large-scale purification for research and therapeutic applications. Its recombinant form often includes tags (e.g., His-tag) to facilitate isolation and characterization. Structural analyses reveal a conserved α/β-hydrolase fold with a metal-binding active site, hinting at catalytic mechanisms similar to its bacterial counterparts.
Research on PTER has expanded into disease contexts, including cancer and metabolic disorders. For instance, altered PTER expression has been observed in certain cancers, suggesting a role in tumor progression or suppression. Additionally, its enzymatic activity against organophosphates positions it as a candidate for bioremediation or antidote development against pesticide poisoning.
Despite progress, challenges persist in elucidating PTER's endogenous substrates and regulatory pathways. Ongoing studies leverage recombinant PTER to explore its interaction networks, substrate specificity, and therapeutic potential, making it a versatile tool in both basic and applied biomedical research.
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