| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | SDHA |
| Uniprot No | P31040 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 44-293aa |
| 氨基酸序列 | SAKVSDSISAQYPVVDHEFDAVVVGAGGAGLRAAFGLSEAGFNTACVTKL FPTRSHTVAAQGGINAALGNMEEDNWRWHFYDTVKGSDWLGDQDAIHYMT EQAPAAVVELENYGMPFSRTEDGKIYQRAFGGQSLKFGKGGQAHRCCCVA DRTGHSLLHTLYGRSLRYDTSYFVEYFALDLLMENGECRGVIALCIEDGS IHRIRAKNTVVATGGYGRTYFSCTSAHTSTGDGTAMITRAGLPCQDLEFV |
| 预测分子量 | 54 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SDHA重组蛋白相关的示例文献(内容为示例，实际引用请核实原文)：
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1. **文献名称**: "Expression and purification of recombinant human SDHA in Escherichia coli for functional studies"
**作者**: Smith J, et al.
**摘要**: 报道了人源SDHA基因在大肠杆菌中的重组表达及纯化方法，通过体外酶活实验证实其参与琥珀酸氧化及电子传递链功能。
2. **文献名称**: "SDHA-mediated succinate metabolism regulates mitochondrial ROS production in cancer cells"
**作者**: Lee CY, et al.
**摘要**: 利用重组SDHA蛋白及基因敲除模型，揭示了SDHA缺陷导致线粒体活性氧(ROS)积累，并促进肿瘤细胞代谢重编程的机制。
3. **文献名称**: "Structural insights into SDHA mutations associated with mitochondrial diseases"
**作者**: Zhang R, et al.
**摘要**: 通过重组SDHA蛋白的晶体结构解析，阐明了致病性突变对蛋白构象及琥珀酸脱氢酶复合体组装的影响。
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**提示**：实际研究中建议通过PubMed或Web of Science检索最新文献，并优先选择高影响力期刊(如*Nature*、*Cell Metabolism*)或专注于蛋白结构的期刊(如*Protein Science*)。
Succinate dehydrogenase complex subunit A (SDHA) is a critical component of the mitochondrial electron transport chain (ETC) and the tricarboxylic acid (TCA) cycle. As one of four subunits (SDHA-D) forming succinate dehydrogenase (Complex II), SDHA serves as the flavoprotein responsible for catalyzing the oxidation of succinate to fumarate, coupled with the reduction of ubiquinone. This dual role links cellular metabolism (TCA cycle) to energy production (ETC), making SDHA indispensable for aerobic respiration. Structurally, SDHA contains a flavin adenine dinucleotide (FAD) cofactor-binding domain and a succinate-binding site, both essential for its enzymatic activity.
Recombinant SDHA protein is produced using heterologous expression systems, such as *E. coli*, yeast, or mammalian cell lines, to enable large-scale purification for functional and structural studies. Its recombinant form retains the ability to bind FAD and interact with other Complex II subunits, facilitating research into mitochondrial disorders, cancer, and neurodegenerative diseases linked to SDHA mutations. For example, germline SDHA mutations are associated with Leigh syndrome, paragangliomas, and pheochromocytomas, while somatic mutations contribute to gastrointestinal stromal tumors (GISTs) and renal cell carcinomas.
The development of recombinant SDHA has advanced diagnostic tools, drug screening platforms, and antibody production for detecting SDHA deficiency in clinical samples. It also supports mechanistic studies exploring how mutations disrupt enzyme activity or protein stability. Challenges in producing functional recombinant SDHA include preserving post-translational modifications (e.g., FAD incorporation) and ensuring proper folding, often requiring co-expression with chaperones or mitochondrial targeting sequences. Ongoing research leverages recombinant SDHA to design small-molecule therapies targeting metabolic vulnerabilities in cancers or to model mitochondrial dysfunction in neurodegenerative diseases like Parkinson’s. Overall, SDHA recombinant protein serves as a vital tool for dissecting cellular energetics and disease mechanisms.
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