| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | FABP12 |
| Uniprot No | A6NFH5 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-140aa |
| 氨基酸序列 | MGSSHHHHHH SSGLVPRGSH MGSHMIDQLQ GTWKSISCEN SEDYMKELGI GRASRKLGRL AKPTVTISTD GDVITIKTKS IFKNNEISFK LGEEFEEITP GGHKTKSKVT LDKESLIQVQ DWDGKETTIT RKLVDGKMVV ESTVNSVICT RTYEKVSSNS VSNS |
| 预测分子量 | 18 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FABP12重组蛋白的3篇参考文献的简要列举(注：FABP12相关研究较少，以下为模拟示例，实际文献需通过学术数据库验证)：
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1. **标题**: "Cloning, Expression, and Functional Characterization of Recombinant FABP12 in Lipid Metabolism"
**作者**: Zhang Y, et al.
**摘要**: 研究通过原核系统成功表达并纯化重组FABP12蛋白，证实其与长链脂肪酸的结合能力，并发现其在体外细胞模型中调节脂质储存的作用。
2. **标题**: "Structural Insights into FABP12: X-ray Crystallography of the Recombinant Protein"
**作者**: Smith JL, et al.
**摘要**: 报道了重组人源FABP12蛋白的晶体结构解析，揭示了其独特的脂肪酸结合口袋构象，为理解其与配体相互作用的分子机制提供了基础。
3. **标题**: "Recombinant FABP12 Alleviates Hepatic Steatosis in a Mouse Model of Obesity"
**作者**: Tanaka K, et al.
**摘要**: 利用重组FABP12蛋白干预高脂饮食小鼠，发现其通过促进肝细胞脂肪酸氧化减轻脂肪肝表型，提示潜在治疗代谢疾病的应用价值。
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**提示**：FABP12研究尚处早期，文献相对有限。建议通过PubMed或Web of Science以“FABP12 recombinant”为关键词检索最新进展，或扩展至其他FABP家族蛋白(如FABP4/5)的相关文献参考。
Fatty Acid-Binding Protein 12 (FABP12) is a member of the fatty acid-binding protein family, a group of small intracellular lipid chaperones involved in the uptake, transport, and metabolism of hydrophobic ligands such as fatty acids, retinoids, and other lipid signaling molecules. While the biological functions of many FABP isoforms (e.g., FABP1 in the liver or FABP4 in adipocytes) are well characterized, FABP12 remains relatively understudied. It shares the conserved β-barrel structure typical of FABPs, with a molecular weight of approximately 15-16 kDa, and is thought to play roles in lipid homeostasis and cellular signaling pathways.
FABP12 was initially identified through genomic analyses, with its expression detected in specific tissues such as the testis and retina, suggesting potential tissue-specific functions. Recombinant FABP12 protein is engineered using heterologous expression systems (e.g., *E. coli* or mammalian cells) to enable functional and structural studies. This involves cloning the FABP12 gene into expression vectors, followed by protein purification using affinity chromatography (e.g., His-tag systems) and validation via SDS-PAGE or Western blot.
Current research focuses on elucidating FABP12’s ligand-binding specificity, interactions with cellular receptors, and its relevance to metabolic or degenerative diseases. For instance, its retinal expression hints at a possible role in visual metabolism, while testis-specific expression may link it to reproductive health. Recombinant FABP12 serves as a critical tool for *in vitro* assays, structural analysis (e.g., X-ray crystallography), and antibody production. However, challenges persist in fully mapping its physiological roles, signaling pathways, and therapeutic potential. Further studies are needed to clarify its contribution to lipid-related disorders or its utility as a biomarker or drug target.
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