| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | AMY1B |
| Uniprot No | P0DTE7 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 16-511aa |
| 氨基酸序列 | QYSSNTQQGRTSIVHLFEWRWVDIALECERYLAPKGFGGVQVSPPNENVAIHNPFRPWWERYQPVSYKLCTRSGNEDEFRNMVTRCNNVGVRIYVDAVINHMCGNAVSAGTSSTCGSYFNPGSRDFPAVPYSGWDFNDGKCKTGSGDIENYNDATQVRDCRLSGLLDLALGKDYVRSKIAEYMNHLIDIGVAGFRIDASKHMWPGDIKAILDKLHNLNSNWFPEGSKPFIYQEVIDLGGEPIKSSDYFGNGRVTEFKYGAKLGTVIRKWNGEKMSYLKNWGEGWGFMPSDRALVFVDNHDNQRGHGAGGASILTFWDARLYKMAVGFMLAHPYGFTRVMSSYRWPRYFENGKDVNDWVGPPNDNGVTKEVTINPDTTCGNDWVCEHRWRQIRNMVNFRNVVDGQPFTNWYDNGSNQVAFGRGNRGFIVFNNDDWTFSLTLQTGLPAGTYCDVISGDKINGNCTGIKIYVSDDGKAHFSISNSAEDPFIAIHAESKL |
| 分子量 | 81.84 kDa |
| 蛋白标签 | GST-tag at N-terminal |
| 缓冲液 | 冻干粉 |
| 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. |
以下是关于水稻粳亚种(*Oryza sativa* subsp. *japonica*)α-淀粉酶同工酶C(AMY1B)的参考文献示例，内容基于典型研究方向构建：
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1. **文献名称**：
*"Cloning and Functional Analysis of the α-Amylase Isoenzyme AMY1B in Germinating Rice Seeds"*
**作者**：T. Yamagata, Y. Tanaka
**摘要**：
本研究克隆了粳稻AMY1B基因，发现其在种子萌发早期特异性表达。通过重组蛋白表达验证其α-淀粉酶活性，酶动力学分析表明AMY1B对支链淀粉的亲和力高于其他同工酶，提示其在胚乳淀粉降解中的关键作用。
2. **文献名称**：
*"Biochemical Characterization of Recombinant AMY1B from *Oryza sativa* japonica: pH and Thermal Stability"*
**作者**：H. Chen, L. Wang
**摘要**：
利用大肠杆菌系统重组表达AMY1B蛋白，纯化后分析其最适反应条件(pH 5.5.温度40℃)。研究发现AMY1B在高温下易失活，但其在酸性条件下的稳定性显著高于其他同工酶，为其在食品工业中的应用提供了依据。
3. **文献名称**：
*"Transcriptional Regulation of AMY1B in Rice under Abiotic Stress"*
**作者**：K. Lee, S. Zhang
**摘要**：
通过启动子分析发现AMY1B的表达受脱落酸(ABA)和干旱胁迫诱导。重组AMY1B的酶活性在模拟胁迫条件下显著增强，转基因植株的耐逆性实验表明，AMY1B可能通过调节淀粉-糖代谢平衡参与应激响应。
4. **文献名称**：
*"Structural Insights into AMY1B via Crystallography: Substrate Binding and Catalytic Mechanism"*
**作者**：M. Patel, R. Kumar
**摘要**：
首次解析重组AMY1B蛋白的晶体结构(分辨率2.1 Å)，揭示了其活性中心的关键氨基酸残基(Asp200和Glu230)。分子对接模拟表明，AMY1B通过疏水口袋识别底物，为设计α-淀粉酶抑制剂提供了结构基础。
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这些示例涵盖基因功能、酶学特性、调控机制及结构解析等研究方向，符合AMY1B的研究热点。实际文献需通过学术数据库(如PubMed、ScienceDirect)检索确认。
AMY1B, a key α-amylase isozyme in *Oryza sativa* japonica, plays a critical role in starch metabolism during seed germination. As part of the glycoside hydrolase family 13. it catalyzes the hydrolysis of α-1.4-glucosidic bonds in starch, generating maltose and glucose to fuel early seedling growth. Encoded by the *Amy1B* gene on chromosome 6. this enzyme is predominantly expressed in germinating seeds, regulated by hormonal cues (e.g., gibberellins) and sugar-signaling pathways. Structurally, it shares conserved domains with other plant α-amylases, including a (β/α)₈ barrel catalytic core and calcium-binding sites critical for stability.
Unlike other rice amylases, AMY1B exhibits distinct biochemical properties, including optimal activity at slightly acidic pH and moderate thermostability. Its recombinant form, produced via heterologous expression systems like *E. coli* or yeast, enables detailed functional studies and protein engineering. Research highlights its biotechnological potential in starch processing industries and agricultural applications, such as improving stress tolerance or yield in cereal crops via genetic modulation. Current studies focus on its structure-function relationships and role in nutrient remobilization, offering insights into cereal physiology and crop improvement strategies.
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