| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | AMY1A |
| Uniprot No | P04745 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 16-511aa |
| 氨基酸序列 | QYSSN TQQGRTSIVH LFEWRWVDIA LECERYLAPK GFGGVQVSPP NENVAIHNPF RPWWERYQPV SYKLCTRSGN EDEFRNMVTR CNNVGVRIYV DAVINHMCGN AVSAGTSSTC GSYFNPGSRD FPAVPYSGWD FNDGKCKTGS GDIENYNDAT QVRDCRLSGL LDLALGKDYV RSKIAEYMNH LIDIGVAGFR IDASKHMWPG DIKAILDKLH NLNSNWFPEG SKPFIYQEVI DLGGEPIKSS DYFGNGRVTE FKYGAKLGTV IRKWNGEKMS YLKNWGEGWG FMPSDRALVF VDNHDNQRGH GAGGASILTF WDARLYKMAV GFMLAHPYGF TRVMSSYRWP RYFENGKDVN DWVGPPNDNG VTKEVTINPD TTCGNDWVCE HRWRQIRNMV NFRNVVDGQP FTNWYDNGSN QVAFGRGNRG FIVFNNDDWT FSLTLQTGLP AGTYCDVISG DKINGNCTGI KIYVSDDGKA HFSISNSAED PFIAIHAESK L |
| 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AMY1A重组蛋白的示例参考文献(注：以下为虚构示例，建议通过学术数据库检索真实文献)：
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1. **文献名称**：*Heterologous Expression and Characterization of Recombinant Human AMY1A in Escherichia coli*
**作者**：Zhang, L. et al.
**摘要**：本研究成功在大肠杆菌中表达并纯化了重组人AMY1A蛋白，优化了诱导条件以提高可溶性表达。酶活分析表明，重组AMY1A具有与天然酶相似的淀粉水解能力，适用于工业酶制剂开发。
2. **文献名称**：*Structural Insights into the Catalytic Mechanism of Recombinant AMY1A via X-ray Crystallography*
**作者**：Smith, J.R. et al.
**摘要**：通过X射线晶体学解析了重组AMY1A的三维结构，揭示了其活性位点关键氨基酸残基(如Asp197和Glu233)在底物结合和催化中的作用，为设计高效淀粉酶抑制剂提供了依据。
3. **文献名称**：*Application of Recombinant AMY1A in Starch-Based Biofuel Production*
**作者**：Tanaka, K. et al.
**摘要**：评估了重组AMY1A在高温和酸性条件下对淀粉的降解效率，证明其可显著提升生物乙醇生产中的糖化效率，凸显了其在生物能源领域的应用潜力。
4. **文献名称**：*Comparative Analysis of Glycosylation Patterns on Recombinant AMY1A Expressed in Mammalian and Insect Cells*
**作者**：Lee, S. et al.
**摘要**：比较了哺乳动物和昆虫细胞表达系统生产的重组AMY1A的糖基化修饰差异，发现哺乳动物来源的蛋白因糖基化更完整而具有更高的酶稳定性，为治疗性酶开发提供了参考。
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建议通过PubMed、Google Scholar或Web of Science等平台，以“AMY1A recombinant protein”为关键词检索真实文献。
**Background of AMY1A Recombinant Protein**
AMY1A, or salivary alpha-amylase 1A, is a key enzyme encoded by the *AMY1A* gene in humans. It belongs to the glycosyl hydrolase family and plays a critical role in carbohydrate metabolism by catalyzing the hydrolysis of alpha-1.4-glycosidic bonds in starch and glycogen, producing maltose, maltotriose, and dextrins. Primarily secreted by the salivary glands, AMY1A initiates the digestive process in the mouth. Its expression is influenced by genetic variations, including copy number variations (CNVs), which have been linked to differences in starch digestion efficiency and metabolic disorders such as obesity and diabetes.
The recombinant AMY1A protein is produced using biotechnological methods, often via heterologous expression in bacterial (e.g., *E. coli*) or eukaryotic systems (e.g., yeast or mammalian cells). This allows large-scale production of the purified enzyme for research and industrial applications. Recombinant AMY1A retains the functional properties of the native enzyme, including pH-dependent activity (optimal at pH 6.8–7.0) and calcium ion dependence for structural stability.
In research, recombinant AMY1A is widely used to study enzyme kinetics, substrate specificity, and inhibitor interactions. It also serves as a model for understanding how genetic diversity impacts enzyme function and metabolic health. Industrially, it is applied in food processing, biofuel production, and detergent formulations. Recent studies explore its potential therapeutic roles, such as a biomarker for stress responses or a target for metabolic syndrome management.
Overall, AMY1A recombinant protein bridges fundamental biochemistry with translational applications, offering insights into human evolution, nutrition, and disease mechanisms.
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