| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | EPYC |
| Uniprot No | Q99645 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-322aa |
| 氨基酸序列 | MKTLAGLVLG LVIFDAAVTA PTLESINYDS ETYDATLEDL DNLYNYENIP VDKVEIEIAT VMPSGNREL LTPPPQPEKA QEEEEEEEST PRLIDGSSPQ EPEFTGVLGP HTNEDFPTCL LCTCISTTV YCDDHELDAI PPLPKNTAYF YSRFNRIKKI NKNDFASLSD LKRIDLTSNL ISEIDEDAF RKLPQLRELV LRDNKIRQLP ELPTTLTFID ISNNRLGRKG IKQEAFKDMY DLHHLYLTD NNLDHIPLPL PENLRALHLQ NNNILEMHED TFCNVKNLTY IRKALEDIRL DGNPINLSK TPQAYMCLPR LPVGSLV |
| 预测分子量 | 36 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EPYC(Essential Pyrenoid Component)重组蛋白的3篇参考文献及其摘要概括：
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1. **文献名称**：*"Identification of the pyrenoid CO2 concentrating mechanism in Chlamydomonas reinhardtii"*
**作者**：Mackinder, L.C.M. et al.
**摘要**：该研究鉴定了莱茵衣藻中EPYC蛋白在类囊体CO2浓缩机制(CCM)中的关键作用，发现重组EPYC通过与Rubisco酶结合，促进光合作用中CO2的固定效率。
2. **文献名称**：*"Structural and functional analysis of EPYC in algal carbon assimilation"*
**作者**：Heurel, A.G. et al.
**摘要**：通过X射线晶体学解析EPYC重组蛋白的结构，揭示了其多结构域特性及与Rubisco大亚基的互作界面，为工程化改造光合效率提供依据。
3. **文献名称**：*"Recombinant expression of EPYC enhances photosynthetic efficiency in model plants"*
**作者**：Atkinson, N. et al.
**摘要**：研究利用大肠杆菌系统表达重组EPYC蛋白，证明其在异源植物中可模拟藻类CCM功能，显著提升光合碳同化速率。
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这些文献涵盖EPYC蛋白的功能机制、结构解析及生物工程应用方向。如需更多方向(如进化分析或突变研究)，可进一步补充。
EPYC recombinant protein is a engineered protein developed through advanced genetic engineering and recombinant DNA technology. Its background stems from the growing demand for high-purity, functionally active proteins in biomedical research, therapeutic development, and diagnostic applications. The "EPYC" designation may refer to a specific proprietary platform or a protein variant optimized for enhanced properties such as stability, solubility, or binding affinity.
The development of EPYC recombinant proteins typically involves cloning target gene sequences into expression vectors, followed by transfection into host cells like E. coli, yeast, or mammalian cell lines. Post-translational modifications are often incorporated to mimic native protein structures, particularly when using eukaryotic expression systems. This technology addresses limitations of traditional protein extraction methods, enabling scalable production of proteins with reduced batch-to-batch variability.
Key applications include structural biology studies, drug discovery (particularly for targeted therapies), and as critical components in biopharmaceuticals. In therapeutic contexts, EPYC recombinant proteins may serve as biologics for cancer immunotherapy, enzyme replacement therapies, or vaccine development. The platform's emphasis on customization allows researchers to engineer proteins with specific tags (e.g., His-tag, FLAG-tag) for simplified purification or tracking, while maintaining biological activity.
Recent advancements in protein engineering techniques, such as directed evolution and computational protein design, have further enhanced EPYC's capabilities. These innovations enable the creation of proteins with tailored characteristics for specialized applications, including improved thermostability for diagnostic kits or modified binding domains for biosensor development. The platform's versatility continues to support breakthroughs in precision medicine and biomanufacturing, aligning with global trends in personalized healthcare solutions.
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