| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | bar |
| Uniprot No | Q8TDU6 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-330aa |
| 氨基酸序列 | MTPNSTGEVPSPIPKGALGLSLALASLIITANLLLALGIAWDRRLRSPPAGCFFLSLLLAGLLTGLALPTLPGLWNQSRRGYWSCLLVYLAPNFSFLSLLANLLLVHGERYMAVLRPLQPPGSIRLALLLTWAGPLLFASLPALGWNHWTPGANCSSQAIFPAPYLYLEVYGLLLPAVGAAAFLSVRVLATAHRQLQDICRLERAVCRDEPSALARALTWRQARAQAGAMLLFGLCWGPYVATLLLSVLAYEQRPPLGPGTLLSLLSLGSASAAAVPVAMGLGDQRYTAPWRAAAQRCLQGLWGRASRDSPGPSIAYHPSSQSSVDLDLN |
| 预测分子量 | 36.8 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BAR结构域重组蛋白的3-4篇代表性文献，内容简明概括：
1. **"BAR domains as sensors of membrane curvature"**
*Author: Kishimoto T. et al.*
摘要：研究BAR结构域通过感知膜曲率调控细胞膜形变的分子机制，利用重组蛋白实验验证了其与脂质膜的相互作用及曲率诱导能力。
2. **"Structural basis of membrane bending by the N-BAR protein endophilin"**
*Author: Frost A. et al.*
摘要：通过三维结构分析和重组N-BAR蛋白实验，揭示endophilin如何通过二聚化和螺旋插入脂质双分子层驱动膜管形成。
3. **"BAR domains expand on a dynamic membrane"**
*Author: Roberts K.L. et al.*
摘要：探讨不同BAR蛋白家族(如F-BAR和I-BAR)通过寡聚化动态改变膜形态，利用重组蛋白证明其曲率选择性与细胞骨架的协同作用。
4. **"Mechanism of endocytosis driven by BAR domain proteins"**
*Author: Gallop J.L. et al.*
摘要：研究BAR蛋白(如SNX9)与动力蛋白协作调控内吞的机制，重组蛋白实验表明其通过膜结合与螺旋聚集产生机械力驱动膜重塑。
注：以上文献名称与作者为示例性质，实际引用时请核对具体论文信息。
BAR (Bin-Amphiphysin-Rvs) domain-containing recombinant proteins are engineered proteins derived from the BAR domain, a conserved structural motif found in diverse eukaryotic proteins involved in membrane remodeling and cellular signaling. First identified in the 1990s in proteins like amphiphysin, sorting nexins, and endophilin, the BAR domain forms a curved, dimeric α-helical bundle that senses and induces membrane curvature. This unique structure enables BAR proteins to participate in critical cellular processes such as vesicle trafficking, organelle shaping, and cytoskeletal organization.
Recombinant BAR proteins are produced using biotechnological methods, typically by cloning BAR domain-coding sequences into expression vectors and purifying the proteins from host systems like *E. coli* or mammalian cells. These engineered proteins retain the membrane-binding and curvature-sensing properties of native BAR domains while offering controlled experimental manipulation. Researchers utilize them as tools to study membrane dynamics in vitro, such as liposome tubulation assays, or to probe BAR domain interactions with lipids and partner proteins in structural studies.
The significance of BAR recombinant proteins extends to disease research, as BAR domain dysfunction is linked to neurological disorders, cancer, and microbial pathogenesis. For example, mutations in the BIN1/amphiphysin 2 BAR domain are associated with centronuclear myopathy, while pathogenic bacteria exploit host BAR proteins during infection. Pharmaceutical applications include screening for small molecules that modulate BAR domain activity, potentially offering therapeutic strategies. Recent advances in cryo-EM and X-ray crystallography have further elucidated BAR domain mechanics, driving demand for high-purity recombinant variants. Their versatility continues to make BAR recombinant proteins indispensable in membrane biology and biomedical research.
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