| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | FLNC |
| Uniprot No | Q14315 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-265aa |
| 氨基酸序列 | MMNNSGYSDAGLGLGDETDEMPSTEKDLAEDAPWKKIQQNTFTRWCNEHLKCVGKRLTDLQRDLSDGLRLIALLEVLSQKRMYRKFHPRPNFRQMKLENVSVALEFLEREHIKLVSIDSKAIVDGNLKLILGLIWTLILHYSISMPMWEDEDDEDARKQTPKQRLLGWIQNKVPQLPITNFNRDWQDGKALGALVDNCAPGLCPDWEAWDPNQPVENAREAMQQADDWLGVPQVIAPEEIVDPNVDEHSVMTYLSQFPKAKLKPG |
| 预测分子量 | 37.3 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FLNC(Filamin C)重组蛋白的模拟参考文献示例，内容基于常见研究主题概括，供参考：
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1. **文献名称**：*Recombinant Human Filamin C Production and Structural Analysis*
**作者**：Smith A, et al.
**摘要**：本研究报道了通过大肠杆菌表达系统高效表达和纯化重组人源FLNC蛋白的方法，并利用X射线晶体学解析其结构，揭示了其与肌动蛋白结合的关键结构域。
2. **文献名称**：*FLNC Recombinant Protein as a Biomarker in Cardiomyopathy*
**作者**：Zhang L, et al.
**摘要**：通过哺乳动物细胞系表达FLNC重组蛋白，验证其在扩张型心肌病患者血清中的异常表达，提示其可能作为疾病诊断的潜在生物标志物。
3. **文献名称**：*Functional Characterization of FLNC Mutants Using Recombinant Protein Models*
**作者**：Jones R, et al.
**摘要**：构建了携带致病性突变的FLNC重组蛋白，发现突变体导致细胞骨架稳定性受损，为遗传性肌病的分子机制提供了实验依据。
4. **文献名称**：*In Vitro Interaction of Recombinant FLNC with Z-Disk Proteins*
**作者**：Kim H, et al.
**摘要**：利用重组FLNC蛋白进行体外结合实验，证实其与肌联蛋白(Titin)和肌间线蛋白(Desmin)的相互作用，阐明了其在维持肌肉收缩单元完整性中的功能。
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**注**：以上内容为模拟生成的示例，实际文献需通过学术数据库(如PubMed、Google Scholar)检索确认。
**Background of FLNC Recombinant Protein**
Filamin C (FLNC), encoded by the *FLNC* gene, is a cytoskeletal protein belonging to the filamin family, which plays a critical role in maintaining structural integrity and mechanosensing in muscle tissues. FLNC is predominantly expressed in cardiac and skeletal muscles, where it crosslinks actin filaments into dynamic networks, stabilizes sarcomeres, and facilitates force transmission. It also interacts with signaling molecules, integrins, and membrane proteins, linking the cytoskeleton to extracellular matrices and regulating cellular responses to mechanical stress.
Mutations in *FLNC* are associated with myopathies, cardiomyopathies, and muscular dystrophies, highlighting its importance in muscle function. Recombinant FLNC protein, produced via expression systems like *E. coli* or mammalian cells, enables researchers to study its structure-function relationships, mutation-driven pathologies, and interactions with binding partners. These proteins are often engineered with tags (e.g., His-tag) for purification and detection.
Research applications include *in vitro* assays to investigate FLNC’s role in cytoskeletal dynamics, disease modeling using cell cultures, and screening therapeutic compounds. Recombinant FLNC also aids in developing diagnostic tools for FLNC-related disorders. By providing a controlled, scalable source of the protein, it advances mechanistic studies and therapeutic exploration, bridging gaps between genetic insights and clinical interventions in neuromuscular and cardiovascular diseases.
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