| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | AST |
| Uniprot No | P17174 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-413aa |
| 氨基酸序列 | MAPPSVFAEVPQAQPVLVFKLTADFREDPDPRKVNLGVGAYRTDDCHPWVLPVVKKVEQKIANDNSLNHEYLPILGLAEFRSCASRLALGDDSPALKEKRVGGVQSLGGTGALRIGADFLARWYNGTNNKNTPVYVSSPTWENHNAVFSAAGFKDIRSYRYWDAEKRGLDLQGFLNDLENAPEFSIVVLHACAHNPTGIDPTPEQWKQIASVMKHRFLFPFFDSAYQGFASGNLERDAWAIRYFVSEGFEFFCAQSFSKNFGLYNERVGNLTVVGKEPESILQVLSQMEKIVRITWSNPPAQGARIVASTLSNPELFEEWTGNVKTMADRILTMRSELRARLEALKTPGTWNHITDQIGMFSFTGLNPKQVEYLVNEKHIYLLPSGRINVSGLTTKNLDYVATSIHEAVTKIQ |
| 预测分子量 | 48 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AST(天冬氨酸氨基转移酶)重组蛋白研究的模拟参考文献示例(非真实文献，仅供格式参考)：
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1. **《Expression and Purification of Recombinant Aspartate Aminotransferase in E. coli》**
*作者：Smith J, et al.*
**摘要**：研究利用大肠杆菌表达系统高效生产重组AST蛋白，优化了诱导条件与纯化步骤，获得高活性酶，为肝脏疾病诊断试剂的开发提供基础。
2. **《Structural Analysis of Mutant AST Enzymes for Improved Catalytic Efficiency》**
*作者：Li X, Wang Y.*
**摘要**：通过定点突变技术改造AST蛋白结构，分析其催化活性变化，发现特定氨基酸替换可显著提升酶反应速率，为工业酶应用提供新策略。
3. **《Recombinant AST as a Biomarker in Drug-Induced Liver Injury Models》**
*作者：Chen R, et al.*
**摘要**：评估重组AST蛋白在小鼠药物性肝损伤模型中的诊断价值，证实其血清水平与肝细胞损伤程度高度相关，优于传统检测方法。
4. **《Large-Scale Production of Recombinant AST Using Yeast Expression Systems》**
*作者：Garcia M, et al.*
**摘要**：开发基于毕赤酵母的重组AST规模化生产工艺，实现低成本、高纯度蛋白制备，推动其在生物医药领域的广泛应用。
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注：以上内容为模拟生成，实际文献需通过PubMed、Google Scholar等平台检索关键词(如"recombinant aspartate aminotransferase")获取。
**Background of AST Recombinant Proteins**
Recombinant protein technology, developed in the 1970s, revolutionized biotechnology by enabling the production of specific proteins through genetically engineered organisms. AST (aspartate aminotransferase) recombinant proteins are a product of this innovation, designed to replicate the structure and function of naturally occurring AST enzymes. AST, a key enzyme in cellular metabolism, catalyzes the transfer of amino groups between aspartate and glutamate, playing critical roles in the urea cycle, amino acid metabolism, and gluconeogenesis.
Traditionally, AST enzymes for research or clinical use were extracted from tissues, but this method faced challenges like low yield, batch variability, and contamination risks. Recombinant AST proteins overcome these limitations by using expression systems (e.g., *E. coli*, yeast, or mammalian cells*) to produce highly pure, standardized enzymes. These systems allow precise control over post-translational modifications, ensuring functionality akin to native proteins.
The development of AST recombinant proteins has significant applications. In diagnostics, they serve as reliable standards for measuring AST levels in blood tests, aiding in the assessment of liver and heart health. In research, they facilitate studies on metabolic disorders, drug toxicity, and enzyme mechanisms. Additionally, recombinant AST is explored for therapeutic potential, such as mitigating oxidative stress or metabolic imbalances.
Despite advancements, challenges persist, including optimizing expression systems for complex eukaryotic modifications and scaling production cost-effectively. Ongoing research focuses on engineering AST variants with enhanced stability or tailored catalytic properties. Overall, AST recombinant proteins exemplify the synergy between molecular biology and practical applications, driving progress in biomedicine and industrial biotechnology.
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