| 纯度 | >85%SDS-PAGE. |
| 种属 | Human |
| 靶点 | LAT2 |
| Uniprot No | Q9GZY6 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 27-243aa |
| 氨基酸序列 | MGSSHHHHHH SSGLVPRGSH MRCSRPGAKR SEKIYQQRSL REDQQSFTGS RTYSLVGQAW PGPLADMAPT RKDKLLQFYP SLEDPASSRY QNFSKGSRHG SEEAYIDPIA MEYYNWGRFS KPPEDDDANS YENVLICKQK TTETGAQQEG IGGLCRGDLS LSLALKTGPT SGLCPSASPE EDEESEDYQN SASIHQWRES RKVMGQLQRE ASPGPVGSPD EEDGEPDYVN GEVAATEA |
| 预测分子量 | 26 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LAT2重组蛋白的3篇代表性文献，简要概括其内容：
1. **文献名称**：*Functional characterization of human L-type amino acid transporter 2 (LAT2) in recombinant mammalian cells*
**作者**：Rossier G, et al.
**摘要**：该研究通过将人源LAT2与SLC3A2共表达于哺乳动物细胞(CHO)，验证了LAT2对中性氨基酸的转运活性，并发现其依赖于细胞膜上的异二聚体形成，揭示了pH与底物亲和力的关系。
2. **文献名称**：*Structural insights into the LAT2-4F2hc heterodimer assembly and its transport mechanism*
**作者**：Lee J, et al.
**摘要**：利用冷冻电镜技术解析了重组表达的LAT2与4F2hc(SLC3A2)复合体结构，阐明了跨膜结构域如何协同介导氨基酸转运，并提出底物识别与质子梯度的偶联模型。
3. **文献名称**：*Overexpression of recombinant LAT2 in Pichia pastoris and its role in cancer cell metabolism*
**作者**：Zhang Y, et al.
**摘要**：在毕赤酵母系统中高效表达重组LAT2蛋白，纯化后分析其与肿瘤细胞增殖的关系，发现LAT2通过调控亮氨酸转运促进mTOR通路激活，提示其作为癌症治疗靶点的潜力。
注：以上文献信息为示例，实际引用时需核对具体来源。如需真实文献，建议通过PubMed或Web of Science检索关键词“LAT2 recombinant”或“SLC7A8 expression”。
**Background of LAT2 Recombinant Protein**
The L-type amino acid transporter 2 (LAT2), encoded by the *SLC7A8* gene, is a neutral amino acid transporter belonging to the SLC7 family of solute carriers. It functions as a heterodimeric transporter by forming a complex with the heavy chain subunit SLC3A2 (CD98hc), which is essential for its membrane localization and stability. LAT2 facilitates the sodium-independent exchange of neutral amino acids, such as leucine, phenylalanine, and glutamine, across cellular membranes, playing a critical role in nutrient uptake, cellular metabolism, and interorgan amino acid homeostasis.
LAT2 is broadly expressed in tissues with high metabolic demands, including the kidneys, small intestine, placenta, and blood-brain barrier. Its activity is vital for maintaining physiological processes such as protein synthesis, neurotransmitter production, and immune cell regulation. Dysregulation of LAT2 has been implicated in pathologies like cancer, neurodegenerative disorders, and metabolic syndromes, where altered amino acid transport can influence cell proliferation, survival, and stress responses.
Recombinant LAT2 protein is produced using biotechnological systems (e.g., mammalian or insect cell lines) to enable functional and structural studies. This engineered protein retains the transporter’s native ligand-binding and transport properties, allowing researchers to investigate its kinetics, substrate specificity, and interactions with inhibitors or therapeutic candidates. Studies leveraging LAT2 recombinant protein have advanced understanding of its role in disease mechanisms, drug delivery across biological barriers (e.g., the blood-brain barrier), and potential as a target for therapies targeting nutrient-dependent pathologies. Challenges in LAT2 research include its complex regulation, substrate promiscuity, and the need for advanced models to mimic its physiological microenvironment.
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