| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | SLC27A2 |
| Uniprot No | O14975 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 283-620aa |
| 氨基酸序列 | GATLALRTKFSASQFWDDCRKYNVTVIQYIGELLRYLCNSPQKPNDRDHKVRLALGNGLRGDVWRQFVKRFGDICIYEFYAATEGNIGFMNYARKVGAVGRVNYLQKKIITYDLIKYDVEKDEPVRDENGYCVRVPKGEVGLLVCKITQLTPFNGYAGAKAQTEKKKLRDVFKKGDLYFNSGDLLMVDHENFIYFHDRVGDTFRWKGENVATTEVADTVGLVDFVQEVNVYGVHVPDHEGRIGMASIKMKENHEFDGKKLFQHIADYLPSYARPRFLRIQDTIEITGTFKHRKMTLVEEGFNPAVIKDALYFLDDTAKMYVPMTEDIYNAISAKTLKL |
| 预测分子量 | 40.8 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SLC27A2重组蛋白的3篇参考文献示例，涵盖其功能、表达及结构研究：
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1. **文献名称**：*"Functional characterization of recombinant human SLC27A2 as a fatty acid transporter"*
**作者**：Hirsch D. et al.
**摘要**：本研究通过在大肠杆菌中表达并纯化人源SLC27A2重组蛋白，证实其具有长链脂肪酸转运活性，并依赖ATP水解供能。实验揭示了该蛋白在细胞脂肪酸摄取中的关键作用。
2. **文献名称**：*"Purification and structural analysis of SLC27A2 in lipid nanodiscs reveals dimeric assembly"*
**作者**：Wang L. et al.
**摘要**：作者利用昆虫细胞系统表达SLC27A2重组蛋白，结合冷冻电镜技术解析其三维结构，发现该蛋白以二聚体形式存在，跨膜结构域可能参与脂肪酸结合与转运。
3. **文献名称**：*"SLC27A2 mutations alter acyl-CoA synthetase activity in recombinant protein models"*
**作者**：Johnson R.B. et al.
**摘要**：研究构建了携带疾病相关突变的SLC27A2重组蛋白，发现特定突变显著降低其酰基辅酶A合成酶活性，为遗传性代谢紊乱的分子机制提供依据。
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以上文献示例为虚构，实际研究中建议通过PubMed或Web of Science以"SLC27A2 recombinant protein"为关键词检索最新论文。
SLC27A2. a member of the solute carrier family 27 (SLC27), encodes a fatty acid transport protein (FATP2) that plays a critical role in cellular fatty acid uptake and metabolism. This transmembrane protein is primarily localized to the endoplasmic reticulum and peroxisomes, with high expression in tissues such as the liver, intestine, and kidney. It facilitates long-chain fatty acid transport across membranes via ATP-dependent mechanisms and also exhibits acyl-CoA synthetase activity, activating fatty acids for subsequent metabolic processes like β-oxidation or lipid synthesis. Dysregulation of SLC27A2 has been linked to metabolic disorders, including insulin resistance, dyslipidemia, and non-alcoholic fatty liver disease (NAFLD), highlighting its importance in systemic energy homeostasis.
Recombinant SLC27A2 protein is engineered for in vitro studies to elucidate its structural and functional properties. Produced using expression systems like mammalian cells or bacteria, the purified protein retains enzymatic and transport activities, enabling researchers to investigate substrate specificity, kinetic parameters, and interactions with regulatory molecules. Its recombinant form is instrumental in high-throughput drug screening, particularly for therapies targeting metabolic diseases. Additionally, studies using this protein have revealed its involvement in bile acid synthesis, sphingolipid metabolism, and drug detoxification pathways. Recent research also explores its potential role in cancer progression and inflammatory responses, expanding its relevance beyond metabolic contexts. As a tool, recombinant SLC27A2 accelerates mechanistic insights and therapeutic innovation for conditions influenced by lipid dysregulation.
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