Recombinant Human F2 protein

**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.

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.