纯度 | >90%SDS-PAGE. |
种属 | Human |
靶点 | LXRb |
Uniprot No | P55055 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 1-460aa |
氨基酸序列 | MSSPTTSSLD TPLPGNGPPQ PGAPSSSPTV KEEGPEPWPG GPDPDVPGTD EASSACSTDW VIPDPEEEPE RKRKKGPAPK MLGHELCRVC GDKASGFHYN VLSCEGCKGF FRRSVVRGGA RRYACRGGGT CQMDAFMRRK CQQCRLRKCK EAGMREQCVL SEEQIRKKKI RKQQQESQSQ SQSPVGPQGS SSSASGPGAS PGGSEAGSQG SGEGEGVQLT AAQELMIQQL VAAQLQCNKR SFSDQPKVTP WPLGADPQSR DARQQRFAHF TELAIISVQE IVDFAKQVPG FLQLGREDQI ALLKASTIEI MLLETARRYN HETECITFLK DFTYSKDDFH RAGLQVEFIN PIFEFSRAMR RLGLDDAEYA LLIAINIFSA DRPNVQEPGR VEALQQPYVE ALLSYTRIKR PQDQLRFPRM LMKLVSLRTL SSVHSEQVFA LRLQDKKLPP LLSEIWDVHE |
预测分子量 | 50,9 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LXRβ重组蛋白的3篇示例文献(内容基于公开研究主题,具体作者和标题为模拟示例):
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1. **文献名称**:*Expression and Purification of Functional Human LXRβ Recombinant Protein in E. coli*
**作者**:Peet DJ et al.
**摘要**:该研究报道了人源LXRβ全长蛋白在大肠杆菌中的重组表达与纯化方法,并证实纯化后的蛋白具有与天然配体(如氧化固醇)结合的活性,为体外受体功能研究提供了工具。
2. **文献名称**:*Crystal Structure of the Ligand-Binding Domain of LXRβ in Complex with a Synthetic Agonist*
**作者**:Svensson S et al.
**摘要**:通过X射线晶体学解析了重组LXRβ配体结合域与合成激动剂(如T0901317)的复合物结构,揭示了配体结合的关键氨基酸残基,为靶向药物设计提供了结构基础。
3. **文献名称**:*Recombinant LXRβ as a Tool for High-Throughput Screening of Cholesterol-Modulating Compounds*
**作者**:Repa JJ et al.
**摘要**:利用昆虫细胞系统表达重组LXRβ蛋白,开发了一种基于受体激活的高通量筛选平台,成功鉴定出多个调控胆固醇代谢的小分子化合物。
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**备注**:以上文献信息为示例性质,实际引用时需通过PubMed或Google Scholar核对准确标题、作者及摘要内容。
Liver X Receptor beta (LXRβ), a member of the nuclear receptor superfamily, is a ligand-activated transcription factor that plays a critical role in lipid metabolism, inflammation, and glucose homeostasis. Discovered in the mid-1990s, LXRβ (encoded by the *NR1H2* gene) is ubiquitously expressed, unlike its isoform LXRα, which is predominantly found in metabolic tissues. Both LXRs form heterodimers with retinoid X receptors (RXRs) and regulate gene expression by binding to LXR response elements in target genes, including those involved in cholesterol efflux (e.g., *ABCG1*, *ABCG5/8*), fatty acid synthesis, and anti-inflammatory pathways.
Recombinant LXRβ proteins are engineered for research and therapeutic exploration, typically produced using bacterial (e.g., *E. coli*) or mammalian expression systems. These proteins retain functional domains, including the DNA-binding domain (DBD) and ligand-binding domain (LBD), enabling studies on receptor-ligand interactions, structural dynamics, and drug screening. Purification methods often involve affinity tags (e.g., His-tag, GST) and chromatography techniques.
LXRβ has garnered attention as a potential therapeutic target for metabolic disorders, atherosclerosis, neurodegenerative diseases, and cancer. Its activation promotes cholesterol reverse transport and inhibits inflammation, but concerns about side effects (e.g., hypertriglyceridemia) drive interest in isoform-selective or tissue-specific modulators. Structural studies using recombinant LXRβ, including X-ray crystallography and cryo-EM, have elucidated mechanisms of ligand binding, co-regulator recruitment, and dimerization with RXR. These insights guide the design of synthetic agonists/antagonists. Ongoing research also explores LXRβ's role in immune regulation and cancer progression, highlighting its multifaceted biological relevance. Recombinant LXRβ remains a vital tool for dissecting LXR signaling and developing next-generation therapeutics.
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