| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | FABP6 |
| Uniprot No | P51161 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-128aa |
| 氨基酸序列 | MAFTGKFEMESEKNYDEFMKLLGISSDVIEKAHNFKIVTEVQQDGQDFTWSQHYYGGHTMTNKFTVGKESNIQTMGGKTFKATVQMEGGKLVVNFPNYHQTSEIVGDKLVEVSTIGGVTYERVSKRLA |
| 预测分子量 | 41.4kDa |
| 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FABP6重组蛋白的3篇代表性文献的简要概括(注：文献信息为模拟示例，实际需根据具体文献调整)：
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1. **标题**: *Expression and Purification of Recombinant Human FABP6 in Escherichia coli*
**作者**: Zhang L, et al.
**摘要**: 本研究成功构建了FABP6的重组表达载体，利用大肠杆菌系统高效表达可溶性蛋白，并通过镍柱亲和层析纯化获得高纯度蛋白，为后续功能研究奠定基础。
2. **标题**: *Structural Insights into FABP6-Bile Acid Interactions by X-ray Crystallography*
**作者**: Tanaka K, et al.
**摘要**: 通过X射线晶体学解析了FABP6与胆汁酸(如牛磺胆酸)的复合物结构，揭示了其结合口袋的关键氨基酸残基及配体特异性机制。
3. **标题**: *Role of FABP6 in Lipid Metabolism and Intestinal Absorption*
**作者**: Wang Y, et al.
**摘要**: 利用FABP6重组蛋白及基因敲除小鼠模型，证明FABP6通过调控胆汁酸转运促进肠道脂质吸收，缺失该蛋白导致高脂饮食下的脂肪代谢异常。
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如需实际文献，建议在PubMed或SciFinder中检索关键词“FABP6 recombinant protein”或结合具体研究方向筛选。
**Background of FABP6 Recombinant Protein**
Fatty acid-binding protein 6 (FABP6), also known as ileal lipid-binding protein (ILBP) or gastrotropin, is a member of the intracellular lipid-binding protein family. It plays a critical role in facilitating the uptake, transport, and metabolism of fatty acids, bile acids, and other hydrophobic ligands within cells. FABP6 is predominantly expressed in the ileum of the small intestine, where it is involved in the reabsorption of bile acids—a key process for maintaining lipid digestion and cholesterol homeostasis. It is also detected in the liver, ovaries, and certain cancer tissues, suggesting broader physiological and pathological relevance.
Structurally, FABP6 shares a conserved β-barrel fold with other FABP family members, featuring a central ligand-binding pocket. Its high affinity for bile acids, particularly conjugated forms like taurocholic acid, distinguishes it from other FABPs that primarily bind fatty acids. This specificity aligns with its role in the enterohepatic circulation of bile acids, a cycle critical for nutrient absorption and metabolic regulation. Studies indicate that FABP6 expression is regulated by nuclear receptors such as liver X receptor (LXR) and farnesoid X receptor (FXR), linking it to lipid-sensing and bile acid signaling pathways.
Recombinant FABP6 protein is produced using heterologous expression systems (e.g., *E. coli* or mammalian cells*) to enable functional studies. Its purified form allows researchers to investigate ligand-binding kinetics, protein interactions, and structural dynamics. Additionally, recombinant FABP6 serves as a tool for exploring its association with diseases, including metabolic disorders, colorectal cancer, and inflammatory bowel diseases, where altered bile acid metabolism or lipid signaling is implicated. Recent research also highlights its potential as a diagnostic biomarker or therapeutic target, driving interest in engineered variants or inhibitors to modulate its activity.
Overall, FABP6 recombinant protein bridges molecular insights into lipid trafficking mechanisms and their implications in health and disease.
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