| 纯度 | >85%SDS-PAGE. |
| 种属 | Human |
| 靶点 | THY1 |
| Uniprot No | P04216 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 20-130aa |
| 氨基酸序列 | Q KVTSLTACLV DQSLRLDCRH ENTSSSPIQY EFSLTRETKK HVLFGTVGVP EHTYRSRTNF TSKYNMKVLY LSAFTSKDEG TYTCALHHSG HSPPISSQNV TVLRDKLVKC |
| 预测分子量 | 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3-4条关于THY1重组蛋白的参考文献示例(注：以下为模拟文献，实际引用时请核对真实来源)：
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1. **"Functional characterization of recombinant human THY1 in neuronal adhesion and signaling"**
*Authors: Chen L, et al.*
**摘要**: 研究利用HEK293细胞表达重组人源THY1蛋白，证明其通过与神经元表面整合素相互作用，调控突触形成和轴突导向，揭示了THY1在神经发育中的分子机制。
2. **"Expression and purification of soluble mouse THY1 extracellular domain for structural analysis"**
*Authors: Tanaka R, et al.*
**摘要**: 通过杆状病毒-昆虫细胞系统高效表达小鼠THY1胞外域重组蛋白，优化纯化工艺并利用X射线晶体学解析其三维结构，为THY1与配体结合的机制提供结构基础。
3. **"Recombinant THY1-Fc fusion protein attenuates liver fibrosis via modulation of TGF-β signaling"**
*Authors: Park S, et al.*
**摘要**: 构建THY1-Fc融合蛋白并验证其在小鼠肝纤维化模型中的治疗作用，发现其通过抑制TGF-β/Smad通路减少胶原沉积，提示THY1重组蛋白在抗纤维化治疗中的潜力。
4. **"THY1 recombinant protein enhances mesenchymal stem cell differentiation into osteoblasts"**
*Authors: Gupta A, et al.*
**摘要**: 研究表明，添加重组THY1蛋白可激活Wnt/β-catenin通路，显著促进间充质干细胞的成骨分化，为骨组织工程提供新型生物材料开发思路。
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建议通过PubMed或Web of Science以关键词“THY1 recombinant protein”“CD90 expression”检索真实文献，并优先选择近五年内的高影响力期刊研究。
**Background of THY1 Recombinant Protein**
THY1. also known as CD90. is a glycosylphosphatidylinositol (GPI)-anchored cell surface glycoprotein belonging to the immunoglobulin (Ig) superfamily. First identified in thymocytes, THY1 is widely expressed in neurons, fibroblasts, endothelial cells, and certain stem cells. Its structure includes a conserved Ig-like domain involved in cell-cell and cell-matrix interactions, playing roles in cell adhesion, migration, signaling, and immune regulation. THY1’s expression is tissue-specific and developmentally regulated, with notable implications in neural development, T-cell activation, and wound healing. Dysregulation of THY1 has been linked to fibrosis, cancer progression, and neurodegenerative disorders.
Recombinant THY1 protein is engineered *in vitro* using expression systems (e.g., mammalian, insect, or bacterial cells) to produce purified, biologically active forms of the protein. This approach enables precise control over post-translational modifications, such as glycosylation, critical for its functional integrity. Researchers utilize recombinant THY1 to study its interactions with integrins, growth factor receptors, and extracellular matrix components, shedding light on its role in modulating signaling pathways like Wnt and TGF-β.
In therapeutic contexts, recombinant THY1 is explored for tissue engineering and regenerative medicine due to its ability to influence stem cell differentiation and tissue repair. It also serves as a biomarker in cancer research, where elevated THY1 levels correlate with tumor-initiating cells in malignancies like melanoma and glioblastoma. Despite progress, challenges remain in understanding its dual roles in promoting or suppressing diseases, highlighting the need for further structural and functional studies. Overall, recombinant THY1 is a vital tool for deciphering its multifaceted biology and translational potential.
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