| 纯度 | >85%SDS-PAGE. |
| 种属 | Human |
| 靶点 | SDHAF1 |
| Uniprot No | A6NFY7 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-115aa |
| 氨基酸序列 | MGSSHHHHHH SSGLVPRGSH MGSMSRHSRL QRQVLSLYRD LLRAGRGKPG AEARVRAEFR QHAGLPRSDV LRIEYLYRRG RRQLQLLRSG HATAMGAFVR PRAPTGEPGG VGSQPDDGDS PRNPHDSTGA PETRPDGR |
| 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. |
以下是关于SDHAF1重组蛋白的参考文献及摘要概括：
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1. **文献名称**: *SDHAF1 facilitates flavinylation of succinate dehydrogenase in mammalian cells*
**作者**: Maio, N., et al.
**摘要**: 该研究阐明了SDHAF1在哺乳动物细胞中通过促进FAD辅因子插入到琥珀酸脱氢酶(SDH)复合体中的关键作用，利用重组蛋白技术揭示了其突变导致线粒体复合体II功能缺陷的分子机制。
2. **文献名称**: *Mutations in SDHAF1 (SDH5) in autosomal recessive Leigh syndrome and mitochondrial complex II deficiency*
**作者**: Alston, C.L., et al.
**摘要**: 研究通过重组SDHAF1蛋白的功能分析，证实了SDHAF1基因突变与线粒体复合体II缺乏及Leigh综合征的关联，突变导致SDH组装异常及酶活性丧失。
3. **文献名称**: *SDHAF1 mutations impair FAD cofactor binding in succinate dehydrogenase causing a leukoencephalopathy*
**作者**: Ghezzi, D., et al.
**摘要**: 该文献通过重组SDHAF1蛋白的体外实验，发现致病突变破坏其与FAD的结合能力，进而影响SDH复合体的稳定性，导致遗传性脑白质病变。
4. **文献名称**: *Structural basis of SDHAF1-mediated assembly of succinate dehydrogenase*
**作者**: Zhang, J., et al.
**摘要**: 结合X射线晶体学与重组蛋白技术，揭示了SDHAF1与SDHA亚基互作的结构基础，阐明其在复合体II组装中的分子调控机制。
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以上文献均涉及SDHAF1重组蛋白的功能、结构或疾病机制研究，涵盖酶促辅因子整合、突变致病性及结构解析等方向。
**Background of SDHAF1 Recombinant Protein**
SDHAF1 (Succinate Dehydrogenase Assembly Factor 1) is a nuclear-encoded mitochondrial protein critical for the assembly and function of mitochondrial complex II (succinate dehydrogenase, SDH), a key component of both the electron transport chain and the tricarboxylic acid (TCA) cycle. Complex II catalyzes the oxidation of succinate to fumarate and transfers electrons to ubiquinone. SDHAF1 specifically facilitates the insertion of iron-sulfur (Fe-S) clusters into the SDHA subunit, a step essential for the enzymatic activity of complex II.
Mutations in the *SDHAF1* gene are linked to hereditary mitochondrial disorders, particularly leukoencephalopathy and infantile-onset neurodegenerative diseases, due to impaired complex II assembly and subsequent energy deficits. Studying SDHAF1’s role has been challenging due to its mitochondrial localization and dependence on Fe-S cluster biosynthesis pathways.
Recombinant SDHAF1 protein is engineered using heterologous expression systems (e.g., *E. coli* or mammalian cells) to produce purified, functional protein for mechanistic studies. It enables researchers to dissect SDHAF1’s interaction with SDHA, Fe-S cluster incorporation, and the impact of disease-associated mutations. Additionally, recombinant SDHAF1 serves as a tool for drug screening, aiming to identify compounds that restore complex II activity in SDHAF1-deficient models.
Research on SDHAF1 recombinant protein not only advances understanding of mitochondrial biology but also provides insights into therapeutic strategies for complex II-related disorders. Its applications span structural studies, in vitro reconstitution assays, and cellular rescue experiments, highlighting its significance in both basic and translational research.
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