| 纯度 | > 95 % SDS-PAGE. |
| 种属 | Human |
| 靶点 | BPGM |
| Uniprot No | P07738 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-259aa |
| 氨基酸序列 | SKYKLIMLRHGEGAWNKENRFCSWVDQKLNSEGMEEARNCGKQLKALNFEFDLVFTSVLNRSIHTAWLILEELGQEWVPVESSWRLNERHYGALIGLNREQMALNHGEEQVRLWRRSYNVTPPPIEESHPYYQEIYNDRRYKVCDVPLDQLPRSESLKDVLERLLPYWNERIAPEVLRGKTILISAHGNSSRALLKHLEGISDEDIINITLPTGVPILLELDENLRAVGPHQFLGDQEAIQAAIKKVEDQGKVKQAKK |
| 预测分子量 | 56.9kDa |
| 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BPGM(2.3-双磷酸甘油酸磷酸酶)重组蛋白的3篇代表性文献示例(注：部分为假设性示例，实际引用时请核实)：
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1. **文献名称**: *"Recombinant human bisphosphoglycerate mutase: expression, purification, and functional characterization"*
**作者**: Smith J, et al.
**摘要**: 本研究通过在大肠杆菌中克隆并表达人源BPGM重组蛋白，优化了纯化流程以获得高纯度酶。实验证实重组BPGM具有催化2.3-BPG合成的活性，并揭示了其对pH和金属离子的依赖性，为后续酶动力学研究提供了基础。
2. **文献名称**: *"Structural insights into BPGM deficiency via crystallographic analysis of recombinant enzyme variants"*
**作者**: Lee S, et al.
**摘要**: 通过X射线晶体学解析了重组BPGM及其突变体的三维结构，揭示了关键氨基酸残基在底物结合和催化中的作用。研究阐明了遗传性BPGM缺乏症相关突变的分子机制，为靶向治疗提供结构依据。
3. **文献名称**: *"Role of recombinant BPGM in regulating hemoglobin oxygen affinity during hypoxic adaptation"*
**作者**: Gupta R, et al.
**摘要**: 利用重组BPGM蛋白探究其在低氧条件下调控红细胞内2.3-BPG水平的分子机制。实验证明BPGM活性上调可降低血红蛋白氧亲和力，提示其在高原适应和贫血代偿中的生理意义。
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**注意**：以上文献为示例性质，实际研究中建议通过PubMed、Web of Science等数据库，以关键词“BPGM recombinant”“bisphosphoglycerate mutase expression”等检索最新文献。
BPG mutase (BPGM), a key enzyme in erythrocyte metabolism, regulates oxygen delivery by modulating 2.3-bisphosphoglycerate (2.3-BPG) levels. This 32-34 kDa enzyme catalyzes the conversion of 1.3-bisphosphoglycerate (1.3-BPG) to 2.3-BPG, a potent allosteric effector that reduces hemoglobin's oxygen affinity. Found predominantly in red blood cells, BPGM activity ensures tissue oxygenation under hypoxic conditions by promoting oxygen release. Its dual functionality—acting as both a mutase and phosphatase—enables fine-tuned control of 2.3-BPG concentrations, which critically influence systemic oxygen homeostasis.
Recombinant BPGM production typically employs expression systems like *E. coli* or mammalian cell cultures, enabling large-scale purification for research and therapeutic exploration. Structural studies reveal a homodimeric configuration with distinct catalytic and allosteric sites, informing drug design targeting hemoglobinopathies. Clinically, BPGM dysregulation links to disorders including sickle cell disease, where elevated 2.3-BPG exacerbates sickling, and rare genetic deficiencies causing erythrocytosis. Recombinant variants facilitate mechanistic studies of these pathologies and screen compounds modulating 2.3-BPG metabolism.
Emerging applications include transfusion medicine, where BPGM-modified stored blood could optimize oxygen-carrying capacity, and gene therapy strategies for hemoglobin disorders. However, challenges persist in maintaining enzyme stability *ex vivo* and achieving tissue-specific targeting *in vivo*. Ongoing research leverages recombinant BPGM to decode its redox-sensitive regulation and explore its role beyond erythrocytes, including potential tumor microenvironment interactions. This enzyme's recombinant form thus serves as both a molecular tool and therapeutic candidate, bridging hematology and oxygen biology innovations.
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