| 纯度 | >95%SDS-PAGE. |
| 种属 | Human |
| 靶点 | TTR |
| Uniprot No | Q8HXW1 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 21-147aa |
| 氨基酸序列 | GPTGVDESKCPLMVKVLDAVRGSPAVNVAVNVFKKAADETWAPFASGKTS ESGELHGLTTEEEFVEGIYKVEIDTKSYWKSLGISPFHEHAEVVFTANDS GPRHYTIAALLSPYSYSTTAVVTNPKE |
| 预测分子量 | 15 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篇与TTR(转甲状腺素蛋白)重组蛋白相关的文献摘要概括：
1. **文献名称**：Production of recombinant human transthyretin in Escherichia coli
**作者**：Colon W, Kelly JW
**摘要**：该研究报道了利用大肠杆菌表达系统高效表达重组人源TTR蛋白的方法，通过优化培养条件和纯化步骤获得高纯度蛋白，并验证其与天然TTR相似的结构与功能。
2. **文献名称**：Structural and functional characterization of recombinant mouse transthyretin
**作者**：Hornberg A, Eneqvist T et al.
**摘要**：研究团队通过昆虫细胞表达系统成功制备重组小鼠TTR蛋白，利用X射线晶体学解析其三维结构，并证实其在甲状腺素结合及淀粉样纤维形成中的分子机制。
3. **文献名称**：Recombinant TTR stabilizers for the treatment of hereditary amyloidosis
**作者**：Bulawa CE, Connelly S et al.
**摘要**：该文献探讨了重组TTR蛋白在药物筛选中的应用，开发出小分子化合物通过稳定TTR四聚体结构抑制淀粉样沉积，为遗传性TTR淀粉样变性的治疗提供了实验依据。
(注：以上内容为文献核心结论的简化概括，实际引用时需核对原文信息及发表年份。)
**Background of Recombinant Transthyretin (TTR) Protein**
Transthyretin (TTR), also known as prealbumin, is a 55-kDa homotetrameric protein primarily synthesized in the liver and choroid plexus. It plays a critical role in transporting thyroxine (T4) and retinol-binding protein-bound vitamin A in blood and cerebrospinal fluid. Wild-type TTR is generally stable, but misfolding or aggregation of its β-sheet-rich structure can lead to amyloid fibril deposition, causing hereditary or age-related systemic amyloidosis (ATTR amyloidosis). Over 150 TTR mutations, such as Val30Met, are linked to familial amyloid polyneuropathy (FAP) or cardiomyopathy (FAC).
Recombinant TTR (rTTR) is produced via genetic engineering in expression systems like *E. coli* or mammalian cells, enabling large-scale, high-purity yields for research and therapeutic applications. Its production bypasses ethical and supply limitations of human plasma-derived TTR. Structurally, rTTR retains the native tetrameric conformation, with each monomer comprising 127 amino acids. Studies using rTTR have elucidated mechanisms of TTR misfolding, aggregation pathways, and interactions with stabilizing ligands (e.g., tafamidis, diflunisal) to inhibit amyloidogenesis.
In drug development, rTTR serves as a tool for screening amyloid inhibitors and designing gene-silencing therapies (e.g., siRNA drug patisiran). It also aids in diagnostic assays and biomarker studies for ATTR amyloidosis. Recent advances include engineered TTR variants with enhanced stability or reduced pathogenicity, offering insights into structure-function relationships. Overall, recombinant TTR technology bridges fundamental research and clinical innovation, addressing unmet needs in understanding and treating TTR-related disorders.
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