纯度 | >85%SDS-PAGE. |
种属 | Human |
靶点 | y+LAT1 |
Uniprot No | Q9UM01 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 1-511aa |
氨基酸序列 | MVDSTEYEVASQPEVETSPLGDGASPGPEQVKLKKEISLLNGVCLIVGNMIGSGIFVSPKGVLIYSASFGLSLVIWAVGGLFSVFGALCYAELGTTIKKSGASYAYILEAFGGFLAFIRLWTSLLIIEPTSQAIIAITFANYMVQPLFPSCFAPYAASRLLAAACICLLTFINCAYVKWGTLVQDIFTYAKVLALIAVIVAGIVRLGQGASTHFENSFEGSSFAVGDIALALYSALFSYSGWDTLNYVTEEIKNPERNLPLSIGISMPIVTIIYILTNVAYYTVLDMRDILASDAVAVTFADQIFGIFNWIIPLSVALSCFGGLNASIVAASRLFFVGSREGHLPDAICMIHVERFTPVPSLLFNGIMALIYLCVEDIFQLINYYSFSYWFFVGLSIVGQLYLRWKEPDRPRPLKLSVFFPIVFCLCTIFLVAVPLYSDTINSLIGIAIALSGLPFYFLIIRVPEHKRPLYLRRIVGSATRYLQVLCMSVAAEMDLEDGGEMPKQRDPKSN |
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. |
以下是关于y+LAT1(SLC7A7)重组蛋白的3篇参考文献示例(注:文献信息为模拟示例,实际引用需核对真实来源):
---
1. **标题**:Functional Characterization of Recombinant y+LAT1 Expressed in Mammalian Cells
**作者**:Smith A, et al.
**摘要**:研究通过哺乳动物细胞系统重组表达y+LAT1蛋白,验证其对精氨酸和赖氨酸的转运活性,并发现其pH依赖性转运特性,为溶酶体贮积症机制提供新见解。
2. **标题**:Structural Insights into y+LAT1 Amino Acid Transporter via Heterologous Expression in E. coli
**作者**:Lee B, et al.
**摘要**:利用大肠杆菌系统成功表达并纯化y+LAT1重组蛋白,通过冷冻电镜解析其三维结构,揭示了底物结合位点及突变导致的转运功能缺陷。
3. **标题**:Role of y+LAT1 in Cationic Amino Acid Transport: A Recombinant Protein Study
**作者**:Garcia C, et al.
**摘要**:通过重组y+LAT1蛋白的功能分析,证明其在细胞膜上介导阳离子氨基酸的跨膜转运,并发现其与4F2hc(CD98)蛋白的相互作用对转运活性至关重要。
---
**提示**:实际文献需通过PubMed、Web of Science等平台检索关键词“y+LAT1 recombinant”“SLC7A7 expression”获取。
**Background of y+LAT1 Recombinant Protein**
The y+LAT1 protein, encoded by the *SLC7A7* gene, is a subunit of the heterodimeric amino acid transporter complex formed with 4F2hc (SLC3A2). This transporter belongs to the solute carrier (SLC) family and plays a critical role in cationic amino acid transport, particularly arginine and lysine, across cell membranes. Its activity is sodium-independent but pH-sensitive, distinguishing it from other amino acid transporters. y+LAT1 is ubiquitously expressed but shows prominence in tissues like the small intestine, kidney, and immune cells, highlighting its role in nutrient absorption, metabolic regulation, and immune response modulation.
Recombinant y+LAT1 protein is engineered for in vitro studies to dissect its structural and functional properties. Produced via expression systems (e.g., mammalian or insect cells), the recombinant form retains the ability to dimerize with 4F2hc, enabling researchers to study transport kinetics, substrate specificity, and regulatory mechanisms. Its dysfunction is linked to lysinuric protein intolerance (LPI), a rare genetic disorder characterized by impaired dibasic amino acid transport, leading to metabolic and immunological complications.
Interest in y+LAT1 extends to cancer research, as upregulated expression in tumors correlates with enhanced arginine uptake, supporting proliferative and immunosuppressive microenvironments. Additionally, its role in T-cell activation and nitric oxide synthesis underscores therapeutic potential in autoimmune diseases and immunotherapy. Recombinant y+LAT1 serves as a tool for drug screening, biomarker discovery, and mechanistic studies aiming to target amino acid metabolism in disease contexts. Advances in structural biology, such as cryo-EM, further aid in elucidating its molecular architecture for precision drug design.
In summary, y+LAT1 recombinant protein bridges basic research and translational applications, offering insights into amino acid biology and therapeutic strategies for metabolic, immune, and oncological disorders.
×