| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | TRDN |
| Uniprot No | Q13061 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-729aa |
| 氨基酸序列 | MTEITAEGNASTTTTVIDSKNGSVPKSPGKVLKRTVTEDIVTTFSSPAAWLLVIALIITWSAVAIVMFDLVDYKNFSASSIAKIGSDPLKLVRDAMEETTDWIYGFFSLLSDIISSEDEEDDDGDEDTDKGEIDEPPLRKKEIHKDKTEKQEKPERKIQTKVTHKEKEKGKEKVREKEKPEKKATHKEKIEKKEKPETKTLAKEQKKAKTAEKSEEKTKKEVKGGKQEKVKQTAAKVKEVQKTPSKPKEKEDKEKAAVSKHEQKDQYAFCRYMIDIFVHGDLKPGQSPAIPPPLPTEQASRPTPASPALEEKEGEKKKAEKKVTSETKKKEKEDIKKKSEKETAIDVEKKEPGKASETKQGTVKIAAQAAAKKDEKKEDSKKTKKPAEVEQPKGKKQEKKEKHVEPAKSPKKEHSVPSDKQVKAKTERAKEEIGAVSIKKAVPGKKEEKTTKTVEQEIRKEKSGKTSSILKDKEPIKGKEEKVPASLKEKEPETKKDEKMSKAGKEVKPKPPQLQGKKEEKPEPQIKKEAKPAISEKVQIHKQDIVKPEKTVSHGKPEEKVLKQVKAVTIEKTAKPKPTKKAEHREREPPSIKTDKPKPTPKGTSEVTESGKKKTEISEKESKEKADMKHLREEKVSTRKESLQLHNVTKAEKPARVSKDVEDVPASKKAKEGTEDVSPTKQKSPISFFQCVYLDGYNGYGFQFPFTPADRPGESSGQANSPGQKQQGQ |
| 预测分子量 | 81,5 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TRDN(Triadin)重组蛋白的3篇代表性文献示例及摘要概括：
1. **文献名称**：*"Expression and functional characterization of recombinant human Triadin in HEK293 cells"*
**作者**：Smith J. et al. (2018)
**摘要**：研究报道了通过HEK293细胞成功表达重组人源TRDN蛋白，并验证其与兰尼碱受体(RyR)的相互作用。通过共免疫沉淀和钙成像技术，证实TRDN在调控肌质网钙释放中的关键作用，为心肌疾病机制研究提供工具。
2. **文献名称**：*"Purification and functional analysis of Triadin recombinant protein in skeletal muscle sarcoplasmic reticulum"*
**作者**：Jones R. et al. (2020)
**摘要**：利用大肠杆菌表达系统制备重组TRDN蛋白，经His标签纯化后，通过体外结合实验证实其与肌钙集蛋白(Calsequestrin, CSQ)的结合能力。研究揭示了TRDN在维持肌质网钙稳态中的结构功能，为相关肌病提供分子机制线索。
3. **文献名称**：*"Recombinant TRDN rescues arrhythmia in a zebrafish model of triadin knockout syndrome"*
**作者**：Zhang Y. et al. (2021)
**摘要**：通过重组TRDN蛋白在斑马鱼模型中的回补实验，证明其可恢复因TRDN缺失导致的心律失常表型。研究为TRDN相关遗传性心律失常的蛋白替代疗法提供了实验依据。
4. **文献名称**：*"Structural insights into Triadin-mediated calcium signaling by cryo-EM analysis of recombinant complexes"*
**作者**：Lee C. et al. (2022)
**摘要**：通过冷冻电镜解析重组TRDN与RyR、CSQ形成的复合物三维结构，阐明TRDN在钙释放通道组装中的构象变化，为靶向TRDN的药物设计奠定结构基础。
(注：以上文献为示例，实际研究中建议通过PubMed或Web of Science检索真实文献。)
The TRDN (triadin) recombinant protein is derived from the human TRDN gene, which encodes a key component of the calcium release machinery in cardiac and skeletal muscle cells. Triadin plays a critical role in regulating excitation-contraction coupling by anchoring the ryanodine receptor (RyR) and calsequestrin within the sarcoplasmic reticulum (SR). This interaction facilitates precise control of calcium ion flux during muscle contraction and relaxation. Mutations in TRDN have been linked to severe cardiac arrhythmias, such as catecholaminergic polymorphic ventricular tachycardia (CPVT), underscoring its physiological importance.
Recombinant TRDN protein is typically produced using heterologous expression systems like Escherichia coli or mammalian cell cultures. These systems enable large-scale production of the protein while retaining its functional domains, such as the coiled-coil regions and calsequestrin-binding sites. Purification often involves affinity tags (e.g., His-tag) and chromatography techniques to ensure high purity and stability.
Research applications of TRDN recombinant protein include structural studies to elucidate its interaction with RyR and calsequestrin, drug screening for arrhythmia therapies, and functional assays to characterize disease-associated mutations. It also serves as an antigen for antibody development and a tool for reconstituting calcium-handling complexes in vitro. Despite progress, challenges remain in mimicking post-translational modifications (e.g., phosphorylation) critical for its native function, necessitating advanced expression systems. Ongoing studies aim to clarify TRDN's role in calcium signaling pathologies and its potential as a therapeutic target.
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