| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | THRa |
| Uniprot No | P10827 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-490aa |
| 氨基酸序列 | MEQKPSKVECGSDPEENSARSPDGKRKRKNGQCSLKTSMSGYIPSYLDKDEQCVVCGDKATGYHYRCITCEGCKGFFRRTIQKNLHPTYSCKYDSCCVIDKITRNQCQLCRFKKCIAVGMAMDLVLDDSKRVAKRKLIEQNRERRRKEEMIRSLQQRPEPTPEEWDLIHIATEAHRSTNAQGSHWKQRRKFLPDDIGQSPIVSMPDGDKVDLEAFSEFTKIITPAITRVVDFAKKLPMFSELPCEDQIILLKGCCMEIMSLRAAVRYDPESDTLTLSGEMAVKREQLKNGGLGVVSDAIFELGKSLSAFNLDDTEVALLQAVLLMSTDRSGLLCVDKIEKSQEAYLLAFEHYVNHRKHNIPHFWPKLLMKEREVQSSILYKGAAAEGRPGGSLGVHPEGQQLLGMHVVQGPQVRQLEQQLGEAGSLQGPVLQHQSPKSPQQRLLELLHRSGILHARAVCGEDDSSEADSPSSSEEEPEVCEDLAGNAASP |
| 预测分子量 | 68.8 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3-4条关于 **THRα(甲状腺激素受体α)重组蛋白** 的虚构参考文献示例，内容基于典型研究方向概括：
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1. **文献名称**: *"Expression and Purification of Recombinant Human Thyroid Hormone Receptor Alpha in Escherichia coli"*
**作者**: Zhang L., et al.
**摘要**: 研究报道了在大肠杆菌中高效表达带有His标签的人源THRα配体结合域(LBD)的方法，通过优化诱导条件和镍柱纯化获得高纯度蛋白，并验证其与甲状腺激素(T3)的结合活性，为体外受体功能研究提供基础材料。
2. **文献名称**: *"Structural Insights into the Ligand Binding Mechanism of THRα by X-ray Crystallography"*
**作者**: Thompson R., et al.
**摘要**: 利用重组THRα蛋白的晶体结构解析，揭示了T3激素与其配体结合域的特异性相互作用位点，阐明了受体构象变化对转录激活的关键影响，为靶向THRα的药物设计提供结构依据。
3. **文献名称**: *"Functional Characterization of a THRα Mutant in Coactivator Recruitment Using Recombinant Protein Assays"*
**作者**: Kim S., et al.
**摘要**: 通过体外重组蛋白互作实验，发现THRα的某关键位点突变会显著削弱其与辅激活因子(如SRC-1)的结合能力，表明该结构域在激素依赖性基因调控中的必要性。
4. **文献名称**: *"Development of a Mammalian Cell-Based System for Recombinant THRα Signaling Analysis"*
**作者**: Müller F., et al.
**摘要**: 构建了哺乳动物细胞中过表达重组THRα的荧光报告系统，验证了受体在细胞内的激素响应活性及下游基因调控功能，为高通量筛选THRα激动剂/拮抗剂提供平台。
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*注：以上文献为示例性概括，实际文献需通过PubMed或Google Scholar检索关键词(如 "Thyroid Hormone Receptor alpha recombinant")获取。*
THRa (Thyroid Hormone Receptor alpha) is a member of the nuclear receptor superfamily that mediates the genomic effects of thyroid hormones (T3 and T4). It plays a critical role in regulating gene expression by binding to thyroid hormone response elements (TREs) in target genes, influencing processes such as metabolism, development, and homeostasis. Structurally, THRa contains a DNA-binding domain (DBD) for TRE recognition and a ligand-binding domain (LBD) that interacts with hormones or synthetic ligands. Unlike its isoform THRb, THRa is predominantly expressed in the heart, skeletal muscle, and brain, and is linked to tissue-specific functions.
Recombinant THRa proteins are engineered in vitro using expression systems like *E. coli* or mammalian cells, often fused with tags (e.g., GST, His-tag) for purification and detection. These proteins serve as essential tools for studying thyroid hormone signaling mechanisms, ligand-receptor interactions, and structural dynamics. Researchers utilize recombinant THRa to screen potential therapeutic compounds targeting thyroid-related disorders, including hyperthyroidism, hypothyroidism, and thyroid cancer. Mutations in THRa are associated with resistance to thyroid hormone syndrome (RTHα), characterized by developmental delays and metabolic dysregulation, making the recombinant protein valuable for modeling pathogenic variants.
In drug discovery, THRa is explored for its role in metabolic diseases, cardiovascular health, and cancer progression. Its recombinant form enables high-throughput assays to identify selective modulators that can fine-tune receptor activity without cross-reacting with THRb, minimizing off-target effects. Additionally, studies using recombinant THRa have shed light on its crosstalk with other signaling pathways, such as Wnt/β-catenin and NF-κB, revealing broader regulatory networks. Despite functional overlaps with THRb, THRa-specific ligands are under development to address isoform-specific pathologies, highlighting its therapeutic relevance. Overall, recombinant THRa remains a pivotal resource for both basic research and translational applications in endocrinology and beyond.
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