| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | NEBL |
| Uniprot No | O76041 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-1014aa |
| 氨基酸序列 | MRVPVFEDIKDETEEEKIGEEENEEDQVFYKPVIEDLSMELARKCTELISDIRYKEEFKKSKDKCTFVTDSPMLNHVKNIGAFISEAKYKGTIKADLSNSLYKRMPATIDSVFAGEVTQLQSEVAYKQKHDAAKGFSDYAHMKEPPEVKHAMEVNKHQSNISYRKDVQDTHTYSAELDRPDIKMATQISKIISNAEYKKGQGIMNKEPAVIGRPDFEHAVEASKLSSQIKYKEKFDNEMKDKKHHYNPLESASFRQNQLAATLASNVKYKKDIQNMHDPVSDLPNLLFLDHVLKASKMLSGREYKKLFEENKGMYHFDADAVEHLHHKGNAVLQSQVKYKEEYEKNKGKPMLEFVETPSYQASKEAQKMQSEKVYKEDFEKEIKGRSSLDLDKTPEFLHVKYITNLLREKEYKKDLENEIKGKGMELNSEVLDIQRAKRASEMASEKEYKKDLESIIKGKGMQAGTDTLEMQHAKKAAEIASEKDYKRDLETEIKGKGMQVSTDTLDVQRAKKASEMASQKQYKKDLENEIKGKGMQVSMDIPDILRAKRTSEIYSQRKYKDEAEKMLSNYSTIADTPEIQRIKTTQQNISAVFYKKEVGAGTAVKDSPEIERVKKNQQNISSVKYKEEIKHATAISDPPELKRVKENQKNISNLQYKEQNYKATPVSMTPEIERVRRNQEQLSAVKYKGELQRGTAISDPPELKRAKENQKNISNVYYRGQLGRATTLSVTPEMERVKKNQENISSVKYTQDHKQMKGRPSLILDTPAMRHVKEAQNHISMVKYHEDFEKTKGRGFTPVVDDPVTERVRKNTQVVSDAAYKGVHPHIVEMDRRPGIIVDLKVWRTDPGSIFDLDPLEDNIQSRSLHMLSEKASHYRRHWSRSHSSSTFGTGLGDDRSEISEIYPSFSCCSEVTRPSDEGAPVLPGAYQQSHSQGYGYMHQTSVSSMRSMQHSPNLRTYRAMYDYSAQDEDEVSFRDGDYIVNVQPIDDGWMYGTVQRTGRTGMLPANYIEFVN |
| 预测分子量 | 116,4 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NEBL(Nebulette)重组蛋白的3篇代表性文献示例(注：文献为模拟示例，具体内容请根据实际研究补充)：
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1. **文献名称**：*Nebulette: A Versatile Adaptor Protein at the Cardiac Z-disk*
**作者**：Arimura T, et al.
**摘要**：本研究利用重组NEBL蛋白片段进行体外结合实验，发现其C端结构域可与肌动蛋白和α-actinin结合，揭示了NEBL在心肌细胞Z盘中维持细胞骨架稳定性的分子机制。
2. **文献名称**：*Functional Analysis of Nebulette Isoforms in Cardiomyopathy*
**作者**：Bang ML, et al.
**摘要**：通过在大肠杆菌中表达重组人NEBL蛋白，作者验证了其不同剪接变体对肌节组装的影响，发现特定结构域缺失会导致心肌细胞收缩力异常，提示NEBL突变与扩张型心肌病的关联。
3. **文献名称**：*Recombinant Nebulette LIM Domain Modulates Actin Polymerization Dynamics*
**作者**：Ming Y, et al.
**摘要**：该研究纯化了NEBL的LIM结构域重组蛋白，发现其能显著抑制肌动蛋白丝的解聚，并通过荧光显微镜证实其在调控肌节动态组装中的直接作用。
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如需具体文献，建议通过PubMed或Google Scholar以关键词“Nebulette recombinant protein”或“NEBL expression”检索近年研究。
Nebulin (NEBL) is a giant sarcomeric protein predominantly expressed in skeletal and cardiac muscle, playing a critical role in maintaining the structural integrity and functional regulation of striated muscle. It binds to actin filaments, stabilizing thin filaments and modulating their length during sarcomere assembly. This interaction is essential for muscle contraction, force transmission, and mechanosensory signaling. Mutations in the NEBL gene are associated with neuromuscular disorders such as nemaline myopathy and dilated cardiomyopathy, highlighting its importance in muscle health.
Recombinant nebulin proteins are engineered to study its molecular interactions, disease mechanisms, and potential therapeutic strategies. Due to nebulin's massive size (~600-900 kDa) and repetitive domain structure, producing full-length recombinant versions has been technically challenging. Current approaches focus on generating truncated or modular variants using expression systems like mammalian cells or bacteria. These recombinant fragments enable researchers to dissect nebulin's roles in actin dynamics, Z-disc organization, and calcium sensitivity regulation.
In disease modeling, recombinant nebulin aids in deciphering how specific mutations impair sarcomere function, contributing to muscle weakness or cardiac dysfunction. It also serves as a tool for high-throughput drug screening to identify compounds that restore sarcomere stability in genetic myopathies. Additionally, engineered nebulin-derived peptides are being explored as biologics to enhance muscle repair or mitigate pathological remodeling in heart failure.
Despite progress, challenges persist in replicating nebulin’s native conformation and post-translational modifications. Advances in protein engineering, such as modular assembly or hybrid expression platforms, may overcome these limitations, paving the way for deeper mechanistic insights and targeted therapies for nebulin-related disorders.
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