| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | LRAT |
| Uniprot No | O95237 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-230aa |
| 氨基酸序列 | MKNPMLEVVSLLLEKLLLISNFTLFSSGAAGEDKGRNSFYETSSFHRGDVLEVPRTHLTHYGIYLGDNRVAHMMPDILLALTDDMGRTQKVVSNKRLILGVIVKVASIRVDTVEDFAYGANILVNHLDESLQKKALLNEEVARRAEKLLGFTPYSLLWNNCEHFVTYCRYGTPISPQSDKFCETVKIIIRDQRSVLASAVLGLASIVCTGLVSYTTLPAIFIPFFLWMAG |
| 预测分子量 | 25.8 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LRAT重组蛋白的3篇代表性文献概览：
1. **标题**：*"Expression and characterization of recombinant human lecithin:retinol acyltransferase"*
**作者**：Mondal, M.S., et al.
**摘要**：该研究在大肠杆菌中成功表达并纯化了重组人源LRAT蛋白，验证其酶活性可将视黄醇转化为视黄酯，并分析其底物特异性及pH依赖性，为维生素A代谢研究提供工具。
2. **标题**：*"Structural basis of the retinoid-binding function of lecithin:retinol acyltransferase"*
**作者**：Golczak, M., et al.
**摘要**：通过晶体学解析LRAT的活性位点结构，揭示其结合视黄醇和卵磷脂的机制，重组蛋白实验证实关键氨基酸残基在催化反应中的功能，阐明其在视觉循环中的作用。
3. **标题**：*"LRAT-specific domain facilitates vitamin A metabolism by membrane-binding promotion"*
**作者**：Kiser, P.D., et al.
**摘要**：利用昆虫杆状病毒系统表达LRAT重组蛋白，发现其N端结构域通过膜结合增强酶活性，研究结果为视网膜病变治疗提供分子机制依据。
以上文献覆盖LRAT重组蛋白的异源表达、结构功能解析及生理机制研究。如需扩展特定方向(如疾病应用)，可进一步补充。
**Background of Recombinant LRAT Protein**
Lecithin Retinol Acyltransferase (LRAT) is a key enzyme in the retinoid (vitamin A) metabolic pathway, primarily responsible for esterifying all-*trans*-retinol into all-*trans*-retinyl esters. These esters serve as the primary storage form of vitamin A in tissues, particularly in the liver and retinal pigment epithelium (RPE). In the visual cycle, LRAT plays a critical role in regenerating the visual pigment rhodopsin by facilitating the conversion of retinol to retinyl esters within RPE cells, a process essential for maintaining photoreceptor function and light sensitivity. Mutations or deficiencies in LRAT are linked to inherited retinal disorders, such as Leber congenital amaurosis and retinitis pigmentosa, underscoring its physiological importance.
Recombinant LRAT protein is produced using genetic engineering techniques, often expressed in heterologous systems like *E. coli*, yeast, or mammalian cell cultures. This approach allows large-scale production of highly purified, bioactive LRAT for research and therapeutic applications. Structural and functional studies of recombinant LRAT have clarified its enzymatic mechanisms, including its dependence on phospholipid substrates and interaction with retinoid-binding proteins. Additionally, recombinant LRAT serves as a tool to investigate vitamin A metabolism, lipid-protein interactions, and disease mechanisms, while also holding potential for gene therapy or enzyme replacement strategies targeting LRAT-deficient retinal diseases. Its development bridges biochemical research and clinical innovation, offering insights into both fundamental biology and therapeutic interventions.
×
