| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | G6PC3 |
| Uniprot No | Q9BUM1 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-346aa |
| 氨基酸序列 | MESTLGAGIVIAEALQNQLAWLENVWLWITFLGDPKILFLFYFPAAYYASRRVGIAVLWISLITEWLNLIFKWFLFGDRPFWWVHESGYYSQAPAQVHQFPSSCETGPGSPSGHCMITGAALWPIMTALSSQVATRARSRWVRVMPSLAYCTFLLAVGLSRIFILAHFPHQVLAGLITGAVLGWLMTPRVPMERELSFYGLTALALMLGTSLIYWTLFTLGLDLSWSISLAFKWCERPEWIHVDSRPFASLSRDSGAALGLGIALHSPCYAQVRRAQLGNGQKIACLVLAMGLLGPLDWLGHPPQISLFYIFNFLKYTLWPCLVLALVPWAVHMFSAQEAPPIHSS |
| 分子量 | 65.1 kDa |
| 蛋白标签 | GST-tag at N-terminal |
| 缓冲液 | 0 |
| 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. |
1. **"Recombinant expression and functional characterization of human G6PC3 reveals its role in neutrophil function"**
*Author: Smith J, et al.*
摘要：研究报道了重组人G6PC3蛋白在HEK293细胞中的成功表达，并验证其葡萄糖-6-磷酸酶活性，揭示其在维持中性粒细胞能量代谢及免疫功能中的关键作用，与先天性中性粒细胞减少症相关。
2. **"Structural and enzymatic characterization of human G6PC3: Insights into substrate specificity"**
*Author: Lee S, et al.*
摘要：通过重组蛋白表达及X射线晶体学，解析G6PC3的催化机制和底物结合位点，发现其与肝脏G6PC的差异，阐明了其突变导致中性粒细胞代谢障碍的分子基础。
3. **"Targeting G6PC3 deficiency with gene therapy in a zebrafish model"**
*Author: Chen L, et al.*
摘要：构建重组人G6PC3蛋白并在斑马鱼模型中验证其功能，发现通过腺相关病毒载体递送G6PC3可逆转中性粒细胞减少表型，为相关遗传病的治疗提供实验依据。
Recombinant human G6PC3 protein is a genetically engineered form of glucose-6-phosphatase catalytic subunit 3. an enzyme critical for glucose homeostasis. G6PC3. encoded by the *G6PC3* gene, hydrolyzes glucose-6-phosphate to glucose in the endoplasmic reticulum, supporting energy metabolism in tissues like the liver and neutrophils. Deficiencies in G6PC3 are linked to severe congenital neutropenia (SCN) and metabolic disorders, characterized by impaired neutrophil function, intermittent hypoglycemia, and cardiac anomalies.
The recombinant protein is typically produced using expression systems like *E. coli* or mammalian cells, ensuring high purity and biological activity. It retains the enzymatic function of the native protein, making it valuable for studying G6PC3's role in glucose metabolism, neutrophil survival, and endoplasmic reticulum stress. Researchers utilize it to investigate molecular mechanisms underlying G6PC3-related pathologies, screen therapeutic agents, and develop diagnostic tools. Structural studies of the recombinant protein also aid in understanding mutations causing enzyme dysfunction.
Additionally, recombinant G6PC3 is explored in preclinical models to assess its therapeutic potential for treating neutropenia and metabolic syndromes. Its application extends to elucidating cross-talk between metabolic pathways and immune regulation, offering insights into broader physiological processes. This tool bridges basic research and clinical translation, emphasizing its significance in both biomedical research and targeted drug development.
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