| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | EYA2 |
| Uniprot No | O00167 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 244-514aa |
| 氨基酸序列 | MGSSHHHHHH SSGLVPRGSH MGSMERVFVW DLDETIIIFH SLLTGTFASR YGKDTTTSVR IGLMMEEMIF NLADTHLFFN DLEDCDQIHV DDVSSDDNGQ DLSTYNFSAD GFHSSAPAAN LCLGSGVHGG VDWMRKLAFR YRRVKEMYNT YKNNVGGLIG TPKRETWLQL RAELEALTDL WLTHSLKALN LINSRPNCVN VLVTTTQLIP ALAKVLLYGL GSVFPIENIY SATKTGKESC FERIMQRFGR KAVYVVIGDG VEEEQGAKKH NMPFWRISCH ADLEALRHAL ELEYL |
| 预测分子量 | 33 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EYA2重组蛋白的3篇参考文献(基于公开信息模拟整理，非真实文献)：
1. **文献名称**：*Structural and Functional Analysis of Recombinant EYA2 Phosphatase Domain*
**作者**：Smith J, et al.
**摘要**：本研究利用大肠杆菌系统表达并纯化了EYA2重组蛋白的磷酸酶结构域，通过X射线晶体学解析其三维结构，揭示了活性位点的关键氨基酸残基，并验证了其酪氨酸磷酸酶活性在Hippo信号通路调控中的作用。
2. **文献名称**：*EYA2 Recombinant Protein Interacts with SIX1 in Tumor Metastasis*
**作者**：Li Y, Wang X.
**摘要**：文章通过共表达纯化技术获得EYA2/SIX1复合物重组蛋白，证明两者在乳腺癌细胞中形成功能复合体，增强细胞迁移和侵袭能力，提示EYA2重组蛋白可作为癌症治疗的潜在靶点。
3. **文献名称**：*Expression and Characterization of EYA2 Recombinant Protein in Insect Cells*
**作者**：Garcia R, et al.
**摘要**：利用杆状病毒-昆虫细胞系统高效表达全长EYA2重组蛋白，通过质谱和酶活实验证实其翻译后修饰及磷酸酶活性，为后续药物筛选提供了功能活性蛋白原料。
注：以上文献为示例性质，实际研究需通过PubMed、Web of Science等平台检索真实文献。
**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.
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