| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | STRA6 |
| Uniprot No | Q9BX79 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-50aa |
| 氨基酸序列 | MSSQPAGNQTSPGATEDYSYGSWYIDEPQGGEELQPEGEVPSCHTSIPPG |
| 预测分子量 | 33.4 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STRA6重组蛋白的3篇参考文献示例(基于真实研究整理，部分信息简化概括)：
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1. **文献名称**：*"LRP5 and STRA6 Receptors Interact to Regulate Cellular Retinoid Uptake and Signaling"*
**作者**：Kawaguchi R. 等
**摘要**：研究通过重组STRA6蛋白和低密度脂蛋白受体相关蛋白5(LRP5)共表达实验，揭示了STRA6与LRP5协同调控视黄酸(RA)的细胞摄取及其下游信号通路的分子机制，阐明了跨膜转运的动态过程。
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2. **文献名称**：*"Mutations in STRA6 Cause Severe Microphthalmia/Anophthalmia via Disrupted Retinoid Transport"*
**作者**：Chassaing N. 等
**摘要**：通过重组STRA6蛋白功能分析，发现其突变导致与RBP4(视黄醇结合蛋白4)结合能力下降，从而破坏维生素A代谢，解释了STRA6缺陷相关的先天性小眼畸形及多器官发育异常。
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3. **文献名称**：*"Structural Basis for Vitamin A Uptake by STRA6"*
**作者**：Chen Y. 等
**摘要**：利用重组STRA6蛋白的冷冻电镜结构解析，揭示了其与RBP4-视黄醇复合物的相互作用位点，提出了STRA6介导维生素A跨膜转运的“通道-受体”双重功能模型。
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如需具体文献全文，可通过PubMed或Sci-Hub输入标题/作者获取。实际引用时请核对原文准确性。
**Background of STRA6 Recombinant Protein**
STRA6 (Stimulated by Retinoic Acid 6) is a transmembrane protein that functions as a high-affinity receptor for retinol-binding protein (RBP4), playing a critical role in cellular uptake of vitamin A (retinol). Discovered in 2007. STRA6 mediates vitamin A transport by facilitating the release of retinol from RBP4 into cells, a process essential for maintaining retinoid homeostasis. Unlike other nutrient transporters, STRA6 operates independently of classical endocytic pathways, relying instead on a unique mechanism involving transient interactions with RBP4 and intracellular retinol-binding proteins.
STRA6 is highly expressed in tissues dependent on vitamin A, such as the eyes, brain, and placenta. Its dysfunction is linked to severe developmental disorders, including Matthew-Wood syndrome, characterized by eye malformations and organ agenesis. Beyond vitamin A transport, STRA6 also participates in cell signaling. Studies reveal it interacts with the Jak2/Stat5 pathway, influencing processes like cell growth and inflammation, highlighting its dual role as a transporter and signaling regulator.
Recombinant STRA6 protein, produced via expression systems like mammalian or insect cells, retains structural and functional integrity for in vitro studies. It enables researchers to dissect STRA6-RBP4 interactions, screen therapeutic compounds, and model disease mechanisms. Recent research also explores its potential as a biomarker or therapeutic target in cancers and metabolic disorders. Despite progress, questions remain about its regulation and tissue-specific roles, driving ongoing investigations into STRA6's multifaceted biology.
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