| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | G6PC |
| Uniprot No | P35575 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 82-117aa |
| 氨基酸序列 | QRPYWWVLDTDYYSNTSVPLIKQFPVTCETGPGSPS |
| 预测分子量 | 17.1 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G6PC重组蛋白的3篇代表性文献摘要(注：文献标题与作者为模拟示例，实际需根据具体文献调整)：
1. **标题**：*Expression and Characterization of Recombinant Human Glucose-6-Phosphatase in E. coli*
**作者**：Smith A, et al.
**摘要**：研究成功在大肠杆菌中表达了重组人源G6PC蛋白，通过亲和层析纯化并验证其酶活性，发现其催化葡萄糖-6-磷酸水解的能力与天然酶相似，为后续酶动力学研究提供基础。
2. **标题**：*Functional Analysis of G6PC Mutants Using Recombinant Protein Expression in Mammalian Cells*
**作者**：Lee B, et al.
**摘要**：通过在HEK293细胞中表达野生型和突变型G6PC重组蛋白，揭示了糖原贮积症Ia型(GSD-Ia)相关突变(如R83C)导致酶活性丧失的分子机制，为疾病诊断提供依据。
3. **标题**：*Optimization of Recombinant G6PC Purification for Drug Screening Applications*
**作者**：Chen X, et al.
**摘要**：开发了一种高效重组G6PC蛋白纯化工艺，结合冷冻电镜分析其三维结构，筛选出小分子抑制剂，为靶向G6PC的代谢性疾病治疗策略奠定基础。
**提示**：实际文献需通过PubMed或Web of Science以关键词“G6PC recombinant protein”检索，重点关注表达系统(原核/真核)、疾病关联(如GSD-Ia、糖尿病)及结构功能研究。
**Background of G6PC Recombinant Protein**
G6PC (glucose-6-phosphatase catalytic subunit) is a key enzyme in glucose homeostasis, primarily expressed in the liver, kidney, and intestine. It catalyzes the final step of gluconeogenesis and glycogenolysis by hydrolyzing glucose-6-phosphate (G6P) to release free glucose into the bloodstream, a critical process for maintaining blood sugar levels. Dysregulation of G6PC activity is linked to metabolic disorders, notably glycogen storage disease type Ia (GSD-Ia or von Gierke disease), caused by mutations in the *G6PC* gene.
Recombinant G6PC protein is engineered using biotechnological platforms (e.g., bacterial, yeast, or mammalian expression systems) to produce the enzyme in vitro. This approach enables large-scale production of functional G6PC for research and therapeutic applications. Studying recombinant G6PC helps elucidate its structural and mechanistic properties, including its interaction with the endoplasmic reticulum membrane and regulatory partners like the glucose-6-phosphate transporter.
Therapeutic development focuses on enzyme replacement therapy (ERT) or gene therapy for GSD-Ia, as current treatments (dietary management) are palliative. Recombinant G6PC also serves as a tool for drug screening, enzyme activity assays, and understanding metabolic pathways. Challenges remain in ensuring protein stability, proper post-translational modifications, and efficient delivery to target tissues. Advances in protein engineering and delivery systems continue to enhance the potential of recombinant G6PC in addressing unmet clinical needs in metabolic diseases.
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