| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | TTN |
| Uniprot No | Q8WZ42 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 5398-5604aa |
| 氨基酸序列 | VFKCSVIGIPTPEVKWYKEYMCIEPDNIKYVISEEKGSHTLKIRNVCLSDSATYRCRAVNCVGEAICRGFLTMGDSEIFAVIAKKSKVTLSSLMEELVLKSNYTDSFFEFQVVEGPPRFIKGISDCYAPIGTAAYFQCLVRGSPRPTVYWYKDGKLVQGRRFTVEESGTGFHNLFITSLVKSDEGEYRCVATNKSGMAESFAALTLT |
| 预测分子量 | 26.5kDa |
| 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TTN(Titin)重组蛋白的3篇代表性文献及其摘要概括：
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1. **文献名称**: "Recombinant expression of titin kinase and its interaction with telethonin"
**作者**: Mayans, O. et al.
**摘要**: 该研究成功克隆并表达了TTN的C端激酶结构域(TK)，并解析了其与肌肉蛋白telethonin的相互作用机制，揭示了其在肌节组装中的关键作用。
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2. **文献名称**: "Production of a recombinant titin immunoglobulin domain in Escherichia coli"
**作者**: Improta, S. et al.
**摘要**: 研究团队利用大肠杆菌系统高效表达了TTN的Ig结构域，并通过核磁共振(NMR)验证其正确折叠，为后续研究TTN的结构-功能关系提供工具。
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3. **文献名称**: "Functional analysis of titin mutations in cardiomyopathy using recombinant protein models"
**作者**: Hinson, J.T. et al.
**摘要**: 通过重组表达携带心肌病相关突变的TTN片段，研究揭示了突变如何破坏蛋白机械稳定性，为遗传性心脏病机制研究提供实验依据。
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这些文献涵盖了TTN重组蛋白在结构解析、表达系统开发及疾病机制研究中的应用。如需具体期刊信息或DOI，可进一步检索作者及标题。
**Background of TTN Recombinant Protein**
Titin (TTN), encoded by the largest human gene (*TTN*), is a giant sarcomeric protein critical for skeletal and cardiac muscle structure and function. Spanning over 1 μm in length, titin acts as a molecular spring, providing elasticity, maintaining sarcomere integrity, and regulating mechanochemical signaling in striated muscles. Mutations in *TTN* are linked to various cardiomyopathies (e.g., dilated cardiomyopathy) and skeletal muscle disorders (e.g., limb-girdle muscular dystrophy).
Recombinant TTN proteins are engineered to study titin’s roles in health and disease. Due to the enormous size of full-length titin (~3.7 MDa), researchers often produce truncated or domain-specific recombinant variants. These proteins are typically expressed in heterologous systems (e.g., *E. coli*, insect, or mammalian cells) using cDNA constructs encoding selected regions, such as the Z-disk, I-band (elastic regions), or A-band (stiff domains).
TTN recombinant proteins enable detailed biochemical, structural, and functional analyses. They are used to investigate titin’s interactions with binding partners (e.g., obscurin, calpain-3), its role in passive muscle stiffness, and its response to mechanical stress. Additionally, they serve as tools to model *TTN*-related mutations, screen therapeutic compounds, or develop antibodies for diagnostics.
Challenges in producing TTN recombinant proteins include maintaining stability of large repetitive domains and avoiding aggregation. Despite this, advances in protein engineering and purification have enhanced their utility in deciphering titin’s complexity. Such research holds promise for understanding muscle pathophysiology and developing targeted therapies for TTN-associated diseases.
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