| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | FHL1 |
| Uniprot No | Q13642 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-280aa |
| 氨基酸序列 | MAEKFDCHYCRDPLQGKKYVQKDGHHCCLKCFDKFCANTCVECRKPIGAD SKEVHYKNRFWHDTCFRCAKCLHPLANETFVAKDNKILCNKCTTREDSPK CKGCFKAIVAGDQNVEYKGTVWHKDCFTCSNCKQVIGTGSFFPKGEDFYC VTCHETKFAKHCVKCNKAITSGGITYQDQPWHADCFVCVTCSKKLAGQRF TAVEDQYYCVDCYKNFVAKKCAGCKNPITGFGKGSSVVAYEGQSWHDYCF HCKKCSVNLANKRFVFHQEQVYCPDCAKKL |
| 预测分子量 | 57 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3篇关于FHL1重组蛋白研究的参考文献概述：
1. **"Functional characterization of FHL1 recombinant protein in muscular dystrophy models"**
*作者：Smith A, et al. (2015)*
摘要：研究通过重组表达人源FHL1蛋白，发现其能够改善小鼠模型中肌营养不良症的肌肉纤维结构，并证实FHL1通过调控Wnt/β-catenin信号通路发挥保护作用。
2. **"Expression and purification of recombinant FHL1 for structural analysis"**
*作者：Chen L, et al. (2018)*
摘要：报道了一种高效的大肠杆菌表达系统用于生产可溶性FHL1重组蛋白，并通过X射线晶体学解析其三维结构，揭示了其LIM结构域介导蛋白相互作用的分子机制。
3. **"FHL1重组蛋白在心肌细胞肥大中的抑制作用"**
*作者：Zhang Y, et al. (2020)*
摘要：利用HEK293细胞表达FHL1重组蛋白，发现其可通过抑制NF-κB通路显著减轻血管紧张素II诱导的心肌细胞肥大，提示其潜在的心血管疾病治疗价值。
注：以上文献信息为示例性质，实际引用需根据具体论文核实。建议通过PubMed或Web of Science以"FHL1 recombinant protein"为关键词查找最新研究。
**Background of FHL1 Recombinant Protein**
FHL1 (Four and a half LIM domains protein 1) is a member of the LIM-only protein family, characterized by its four complete LIM domains and an N-terminal half LIM domain. These zinc-binding domains mediate protein-protein interactions, enabling FHL1 to function as a scaffolding or adaptor molecule in cellular signaling, structural organization, and transcriptional regulation. Predominantly expressed in skeletal and cardiac muscle, FHL1 is also found in the eyes and other tissues, playing critical roles in mechanotransduction, cytoskeletal organization, and muscle development.
Mutations in the *FHL1* gene are linked to multiple human disorders, including Emery-Dreifuss muscular dystrophy (EDMD), reducing body myopathy (RBM), and hypertrophic cardiomyopathy. These pathologies often manifest as progressive muscle weakness, cardiac conduction defects, or skeletal deformities, underscoring FHL1’s importance in maintaining muscle integrity and function.
Recombinant FHL1 protein, produced via bacterial (e.g., *E. coli*) or mammalian expression systems, retains the native structure and functional domains required for experimental or therapeutic applications. Its production enables detailed studies of FHL1’s interaction partners (e.g., titin, integrins, and transcription factors), disease-associated mutation effects, and signaling pathways. Researchers utilize recombinant FHL1 to investigate mechanisms underlying myopathies, screen potential therapeutic compounds, or develop protein replacement strategies.
In drug discovery, recombinant FHL1 serves as a tool to validate targets in muscle-related diseases or cardiac remodeling. Its role in regulating hypertrophic responses and stress signaling further highlights therapeutic potential. However, challenges remain in optimizing recombinant FHL1’s stability, post-translational modifications, and delivery methods for clinical applications.
Overall, FHL1 recombinant protein bridges molecular insights into muscle biology and translational research, offering avenues to address unmet needs in genetic and acquired musculoskeletal disorders.
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