| 纯度 | >85%SDS-PAGE. |
| 种属 | Saccharomyces cerevisiae |
| 靶点 | GLC8 |
| Uniprot No | P41818 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-229aa |
| 氨基酸序列 | MGGILKNPLA LSPEQLAQQD PETLEEFRRQ VYENTQKNAK LTSHKRNIPG LDNTKEEGEI IGTSSTFLPK DTLSLKHEQD MLAKMTPEER VQWNQRNLAE NEITKKQFQD IHIDEPKTPY QGAVDPHGEY YRVDDDEDED NSDKKPCQVA NDDIDDLSLG EPEFEIKENK QPDFETNDEN DEDSPEARHK KFEEMRKKHY DVRAIFNKKS REALKDEDED EDDSTTKEP |
| 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. |
以下提供的参考文献为模拟示例，因“GLC8重组蛋白”可能为特定领域或非标准命名，实际文献需通过学术数据库核实：
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1. **标题**: *Cloning and Functional Characterization of GLC8 Recombinant Protein in Yeast Glycogen Metabolism*
**作者**: Thompson R, et al.
**摘要**: 本研究成功克隆并表达了酿酒酵母来源的GLC8重组蛋白，证实其作为蛋白磷酸酶1(PP1)的调节亚基参与糖原合成调控，通过体外酶活实验揭示了其磷酸化修饰对代谢通路的影响。
2. **标题**: *Structural Analysis of Recombinant GLC8 and Its Role in Cellular Stress Response*
**作者**: Lee S, et al.
**摘要**: 通过X射线晶体学解析了重组GLC8蛋白的三维结构，结合细胞实验发现其在氧化应激条件下通过PP1复合物调控自噬通路，为疾病治疗提供潜在靶点。
3. **标题**: *High-Yield Expression and Purification of GLC8 Recombinant Protein in E. coli*
**作者**: Chen W, et al.
**摘要**: 优化了大肠杆菌表达系统中GLC8重组蛋白的诱导条件及纯化策略，获得高纯度产物并验证其与天然蛋白的生物学等效性，为工业化生产奠定基础。
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**建议**：若需真实文献，请通过以下方式精准检索：
- 确认蛋白全称及物种来源(如“Human GLC8”或“Saccharomyces cerevisiae GLC8”);
- 使用PubMed/Google Scholar关键词组合：“GLC8 recombinant production”“GLC8 PP1 regulatory subunit”;
- 查阅相关综述的参考文献列表，追踪原始研究。
**Background of GLC8 Recombinant Protein**
GLC8 (Glycogen Level Control 8) is a regulatory protein initially identified in *Saccharomyces cerevisiae* (budding yeast) for its role in modulating glycogen metabolism. It belongs to the phosphatase regulator family and interacts with protein phosphatase 1 (PP1), a key enzyme involved in glycogen synthesis and degradation. GLC8 acts as an activator of PP1. enhancing its phosphatase activity to promote glycogen accumulation under stress conditions, such as nutrient limitation. Structurally, GLC8 contains conserved PP1-binding motifs, enabling direct interaction with PP1 catalytic subunits to form functional complexes.
Recombinant GLC8 protein is produced using heterologous expression systems (e.g., *E. coli* or mammalian cells*) to study its biochemical interactions and regulatory mechanisms. Its recombinant form retains the ability to bind PP1 and modulate enzymatic activity, making it a valuable tool for dissecting glycogen metabolism pathways and phosphatase regulation. Beyond yeast, homologs of GLC8 in higher eukaryotes (e.g., human PPP1R3/PTPA family) share functional similarities, linking GLC8-related studies to broader research on metabolic disorders, such as diabetes, and cellular stress responses.
Research on recombinant GLC8 also contributes to understanding conserved regulatory networks in energy homeostasis, offering potential therapeutic insights for diseases involving glycogen dysregulation. Its application spans *in vitro* enzymatic assays, structural studies, and yeast genetic models, underscoring its significance in both basic and applied biochemistry.
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