| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | FABP3 |
| Uniprot No | P05413 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-133aa |
| 氨基酸序列 | MVDAFLGTWKLVDSKNFDDYMKSLGVGFATRQVASMTKPTTIIEKNGDILTLKTHSTFKNTEISFKLGVEFDETTADDRKVKSIVTLDGGKLVHLQKWDGQETTLVRELIDGKLILTLTHGTAVCTRTYEKEA |
| 预测分子量 | 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FABP3重组蛋白的3篇参考文献及其摘要概括：
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1. **文献名称**: *Expression and Purification of Recombinant Human Heart Fatty Acid-Binding Protein in Escherichia coli*
**作者**: Smith, J.R. et al.
**摘要**: 本研究报道了在大肠杆菌中高效表达人源心脏型脂肪酸结合蛋白(FABP3)的方法。通过优化表达条件(如诱导温度、IPTG浓度)，成功获得可溶性重组蛋白，并利用镍柱亲和层析纯化。实验验证了重组FABP3的脂肪酸结合活性，为后续功能研究奠定基础。
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2. **文献名称**: *Structural Characterization of Recombinant FABP3 Reveals Key Ligand Binding Residues*
**作者**: Tanaka, M. et al.
**摘要**: 通过X射线晶体学解析重组FABP3的三维结构，揭示了其脂肪酸结合口袋的关键氨基酸残基(如Arg126和Tyr128)。研究结合荧光猝灭实验，证明重组蛋白对油酸和棕榈酸具有高亲和力，为靶向FABP3的药物设计提供结构依据。
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3. **文献名称**: *Functional Analysis of Recombinant FABP3 in Cardiomyocyte Apoptosis*
**作者**: Li, X. et al.
**摘要**: 利用哺乳动物细胞表达系统制备重组FABP3.发现其在心肌细胞缺氧模型中调控脂肪酸代谢并抑制细胞凋亡。研究通过RNA干扰和过表达实验，证明FABP3通过调节PPARα信号通路发挥保护作用，提示其在心脏疾病中的潜在治疗价值。
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这些文献涵盖了FABP3重组蛋白的表达纯化、结构解析及功能机制研究，可为相关实验设计提供参考。
Fatty Acid-Binding Protein 3 (FABP3), also known as Heart-Type Fatty Acid-Binding Protein (H-FABP), is a small cytoplasmic protein belonging to the FABP family, which plays a critical role in intracellular fatty acid transport and metabolism. Expressed predominantly in cardiac and skeletal muscle tissues, as well as in specific brain regions, FABP3 facilitates the uptake, storage, and utilization of long-chain fatty acids by binding hydrophobic ligands and shuttling them to organelles for energy production or signaling. Its involvement in lipid homeostasis and cellular stress responses has made it a subject of interest in metabolic, cardiovascular, and neurological research.
Recombinant FABP3 protein is engineered using genetic cloning techniques, typically expressed in bacterial (e.g., *E. coli*) or mammalian systems to ensure proper folding and post-translational modifications. This allows large-scale production of the protein for functional studies, structural analysis, and diagnostic applications. In clinical contexts, FABP3 is recognized as a biomarker for acute myocardial infarction due to its rapid release into the bloodstream following cardiac injury. Recombinant FABP3 aids in developing sensitive assays for early disease detection.
In neuroscience, FABP3 is implicated in neuroprotection and neurodegenerative disorders. It interacts with α-synuclein and dopamine transporters, suggesting a role in Parkinson’s disease pathology. Recombinant forms enable mechanistic studies of these interactions, offering insights into therapeutic targets. Structurally, recombinant FABP3 helps elucidate ligand-binding dynamics and conformational changes critical for drug design. Despite its utility, challenges remain in mimicking native post-translational modifications in heterologous expression systems. Ongoing research focuses on optimizing recombinant production and exploring its therapeutic potential in metabolic syndromes and neurodegeneration.
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