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| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | FAM132A |
| Uniprot No | Q5T7M4 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 21-302aa |
| 氨基酸序列 | GGVGARREAQ RTQQPGQRAD PPNATASASS REGLPEAPKP SQASGPEFSD AHMTWLNFVR RPDDGALRKR CGSRDKKPRD LFGPPGPPGA EVTAETLLHE FQELLKEATE RRFSGLLDPL LPQGAGLRLV GEAFHCRLQG PRRVDKRTLV ELHGFQAPAA QGAFLRGSGL SLASGRFTAP VSGIFQFSAS LHVDHSELQG KARLRARDVV CVLICIESLC QRHTCLEAVS GLESNSRVFT LQVQGLLQLQ AGQYASVFVD NGSGAVLTIQ AGSSFSGLLL GT |
| 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FAM132A(JCAD)重组蛋白的3篇文献摘要(均为虚构示例，实际文献需通过数据库验证)：
1. **文献名称**: *JCAD promotes angiogenesis in coronary artery disease via PI3K/Akt signaling*
**作者**: Li X, et al. (2020)
**摘要**: 研究通过重组JCAD蛋白体外实验，发现其通过激活PI3K/Akt通路增强内皮细胞迁移和血管生成，提示其在冠心病病理中的作用机制。
2. **文献名称**: *Expression and purification of recombinant FAM132A in E. coli for functional studies*
**作者**: Wang Y, et al. (2018)
**摘要**: 报道了FAM132A重组蛋白在原核系统中的高效表达与纯化方法，并验证其与细胞骨架蛋白的体外结合能力。
3. **文献名称**: *FAM132A interacts with Notch1 intracellular domain to regulate cell proliferation*
**作者**: Chen L, et al. (2021)
**摘要**: 利用重组FAM132A蛋白进行免疫共沉淀实验，证实其与Notch1胞内结构域结合，调控肿瘤细胞增殖。
*注：以上内容为模拟生成，实际文献请通过PubMed/Google Scholar检索关键词“FAM132A”或“JCAD”获取。*
FAM132A, also known as myonectin, is a secreted protein encoded by the FAM132A gene, belonging to the C1q/TNF-related protein (CTRP) family. It is primarily expressed in skeletal muscle and plays a regulatory role in energy metabolism, particularly lipid homeostasis. Myonectin was identified as a myokine, a muscle-derived signaling molecule, that responds to metabolic demands and nutrient availability. Studies suggest it facilitates fatty acid uptake in adipose tissue and liver by promoting lipid storage, acting as a bridge between muscle function and systemic metabolic balance.
The recombinant FAM132A protein is engineered for research to study its structure, function, and therapeutic potential. Produced via bacterial or mammalian expression systems, it retains the native protein’s biological activity, including binding to cell surface receptors and activating downstream signaling pathways such as AMPK and PPARγ. Researchers utilize it to explore its role in metabolic disorders like obesity, insulin resistance, and type 2 diabetes. Emerging evidence also links FAM132A to inflammatory responses and tissue repair, though its mechanisms remain incompletely understood.
Current research focuses on its dual role in lipid metabolism and inflammation, with potential applications in diagnostics or treatments for metabolic syndromes. Challenges include elucidating receptor interactions and tissue-specific effects. Overall, FAM132A represents a promising yet understudied target in understanding muscle-adipose cross-talk and metabolic regulation.
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