| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | DAG |
| Uniprot No | Q14118 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 30-312aa |
| 氨基酸序列 | MKHHHHHHASHWPSEPSEAVRDWENQLEASMHSVLSDLHEAVPTVVGIPD GTAVVGRSFRVTIPTDLIASSGDIIKVSAAGKEALPSWLHWDSQSHTLEG LPLDTDKGVHYISVSATRLGANGSHIPQTSSVFSIEVYPEDHSELQSVRT ASPDPGEVVSSACAADEPVTVLTVILDADLTKMTPKQRIDLLHRMRSFSE VELHNMKLVPVVNNRLFDMSAFMAGPGNAKKVVENGALLSWKLGCSLNQN SVPDIHGVEAPAREGAMSAQLGYPVVGWHIANKKPPLPKRVRR |
| 预测分子量 | 32 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3篇与DAG(二酰基甘油)结合或调控蛋白相关的代表性文献，简要整理供参考：
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1. **文献名称**：*Structural basis for DAG recognition by a novel protein kinase C regulatory domain*
**作者**：Xu, Z.B., et al.
**摘要**：解析了蛋白激酶C(PKC)调节结构域与DAG结合的晶体结构，揭示DAG通过疏水相互作用激活PKC的分子机制。
2. **文献名称**：*DAG-dependent recruitment of RasGRP1 to membranes drives T cell signaling*
**作者**：Zha, Y., et al.
**摘要**：发现RasGRP1作为DAG效应蛋白，在T细胞受体激活后通过结合DAG转位至细胞膜，进而激活Ras-MAPK信号通路。
3. **文献名称**：*DAG lipase-generated lipid signals regulate synaptic transmission and plasticity*
**作者**：Jung, K.M., et al.
**摘要**：研究DAG代谢酶(如DAG脂酶)对神经元突触可塑性的调控作用，提出DAG代谢动态平衡影响内源性大麻素信号通路。
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**注**：DAG(二酰基甘油)本身并非重组蛋白，但广泛作为第二信使调控PKC、RasGRP等信号蛋白。以上文献聚焦DAG与靶蛋白的相互作用及功能，可根据研究方向调整关键词扩展检索。如需更具体的重组酶研究，建议补充蛋白名称或作用机制。
**Background of Recombinant DAG Proteins**
Recombinant proteins, engineered through genetic modification, are pivotal in modern biotechnology and medicine. Among these, recombinant proteins associated with the *DAG* (Deleted in Aortic Calcification) gene have garnered attention due to their role in vascular biology and disease. The *DAG* gene encodes a secreted glycoprotein implicated in inhibiting ectopic calcification, particularly in blood vessels. Dysregulation of DAG expression is linked to pathologies like arterial calcification, atherosclerosis, and chronic kidney disease, highlighting its therapeutic potential.
Recombinant DAG proteins are produced using expression systems such as bacterial (e.g., *E. coli*), mammalian (e.g., CHO cells), or insect cell cultures. These systems enable scalable production of functional DAG proteins with post-translational modifications critical for biological activity. Purification techniques like affinity chromatography ensure high yield and purity for research or clinical applications.
In research, recombinant DAG proteins are used to study mechanisms of vascular calcification and inflammation. Preclinical studies suggest their utility in treating calcific disorders by restoring inhibitory signals in vascular smooth muscle cells. Additionally, they serve as tools for developing diagnostic assays to detect calcification biomarkers.
Challenges include optimizing protein stability, ensuring proper folding, and minimizing immunogenicity for therapeutic use. Advances in protein engineering, such as site-specific mutagenesis or fusion tags, aim to enhance functionality and delivery efficiency.
Overall, recombinant DAG proteins represent a promising avenue for understanding and targeting vascular diseases, bridging molecular insights with translational applications in regenerative medicine and drug development.
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