**Background of EYA2 Recombinant Protein**
The EYA2 (Eyes Absent Homolog 2) protein belongs to the EYA family of conserved transcriptional regulators and phosphatases, initially identified for their role in *Drosophila* eye development. In humans, EYA2 functions as a dual-function protein, acting as a tyrosine phosphatase and a transcriptional coactivator. It plays critical roles in developmental processes, tissue repair, and cellular signaling pathways, including the DNA damage response and Hippo signaling. Dysregulation of EYA2 has been implicated in cancers (e.g., breast, lung) and developmental disorders, highlighting its therapeutic and diagnostic potential.
Recombinant EYA2 protein is engineered using biotechnological platforms (e.g., *E. coli*, mammalian cells) to produce purified, functional protein for research. Its recombinant form often includes tags (e.g., His-tag) for purification and detection. Structurally, EYA2 contains an N-terminal transactivation domain and a C-terminal phosphatase domain, with recombinant variants sometimes focusing on specific functional regions.
Studies utilizing EYA2 recombinant protein have elucidated its phosphatase activity, interactions with partners like DACH1/2. and role in promoting cell migration, proliferation, and survival. It is also employed in drug discovery to screen inhibitors targeting its enzymatic activity. Notably, EYA2's phosphatase function is Mg²⁺-dependent and distinct from classical tyrosine phosphatases, making it a unique therapeutic target.
Research challenges include optimizing recombinant EYA2 stability and activity, as post-translational modifications in native contexts may influence its function. Overall, EYA2 recombinant protein serves as a vital tool for dissecting its biological roles and advancing therapeutic strategies in oncology and regenerative medicine.
以下是关于F2(凝血因子Ⅱ/凝血酶)重组蛋白研究的3篇代表性文献，涵盖结构、功能及生产优化方向：
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1. **文献名称**：*Crystal structure of human α-thrombin in complex with fibrinogen mimetic inhibitor*
**作者**：Banner D.W., Hadváry P.
**摘要**：通过X射线晶体学解析了重组人α-凝血酶与纤维蛋白原模拟抑制剂的复合物结构，揭示了凝血酶底物结合位点的构象变化及其催化机制，为抗凝血药物设计提供结构基础。
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2. **文献名称**：*Recombinant thrombin: development and clinical application*
**作者**：Chapman W.C. et al.
**摘要**：综述重组凝血酶(rThrombin)的工业化生产流程，包括哺乳动物细胞表达系统的优化及纯化工艺，并评估其在手术止血中的安全性和有效性，证实其与传统牛凝血酶相比免疫原性显著降低。
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3. **文献名称**：*Engineering recombinant factor IIa variants with altered substrate specificity*
**作者**：Sutherland J.J. et al.
**摘要**：通过定点突变改造重组凝血酶(F2a)的活性位点，获得对特定凝血因子(如FⅧ/FⅩ)具有选择性激活能力的变体，为开发靶向止血疗法提供新策略。
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**注**：若需病毒或细菌来源的F2重组蛋白文献，请补充说明具体研究背景。
F2 recombinant protein, also known as recombinant prothrombin, is a genetically engineered version of human coagulation Factor II, a key serine protease precursor in the blood clotting cascade. Naturally synthesized in the liver, Factor II undergoes vitamin K-dependent γ-carboxylation to enable calcium-binding and membrane interaction during coagulation. Its activated form, thrombin, converts fibrinogen to fibrin and amplifies clotting through feedback loops.
The development of recombinant F2 emerged to address challenges in studying and treating coagulation disorders. Traditional thrombin or prothrombin preparations derived from plasma carry risks of pathogen transmission and batch variability. Recombinant technology enables production in controlled systems like mammalian cells (e.g., CHO or HEK293) or yeast, though achieving proper post-translational modifications (particularly γ-carboxylation) remains technically demanding. Advanced expression systems now incorporate vitamin K-dependent modification steps to produce functional equivalents.
Research applications include mechanistic studies of thrombosis/hemostasis, screening anticoagulant drugs (e.g., direct thrombin inhibitors), and standardizing diagnostic assays (PT/INR tests). Therapeutic potential exists for treating rare congenital prothrombin deficiencies, though clinical use currently faces hurdles like short plasma half-life and immunogenicity. Recent studies also explore engineered F2 variants with altered activity profiles for targeted hemostatic therapies.
Ongoing optimization focuses on improving yield, modification efficiency, and safety profiles. As a tool protein, recombinant F2 has significantly advanced structural biology research through crystallization studies revealing thrombin's allosteric regulation mechanisms. Its development exemplifies how recombinant technology overcomes limitations of natural plasma-derived factors while enabling precise customization for biomedical applications.
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