| 纯度 | >85%SDS-PAGE. |
| 种属 | Human |
| 靶点 | GLRX5 |
| Uniprot No | Q86SX6 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 32-157aa |
| 氨基酸序列 | AGSGAGGGG SAEQLDALVK KDKVVVFLKG TPEQPQCGFS NAVVQILRLH GVRDYAAYNV LDDPELRQGI KDYSNWPTIP QVYLNGEFVG GCDILLQMHQ NGDLVEELKK LGIHSALLDE KKDQDSK |
| 预测分子量 | 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GLRX5重组蛋白的3篇代表性文献及其摘要概括：
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1. **文献名称**：*Expression, purification, and characterization of recombinant human glutaredoxin 5*
**作者**：Ye, H., Rouault, T.A.
**摘要**：该研究报道了人源GLRX5在大肠杆菌中的重组表达与纯化方法，验证了其作为铁硫簇组装蛋白的功能活性，并证明其在体外可结合铁硫复合物，为后续疾病机制研究提供工具。
2. **文献名称**：*Glutaredoxin 5 deficiency causes sideroblastic anemia by specifically impairing heme biosynthesis and depleting cytosolic iron in human erythroblasts*
**作者**：Shi, Y., Ghosh, M.C., et al.
**摘要**：通过构建重组GLRX5蛋白，研究发现其缺陷会导致红细胞胞质铁代谢异常和线粒体铁沉积，揭示了GLRX5突变引发铁粒幼细胞贫血的分子机制。
3. **文献名称**：*The role of glutaredoxin 5 in mitochondrial iron-sulfur protein biogenesis*
**作者**：Rodríguez-Manzaneque, M.T., et al.
**摘要**：利用重组GLRX5蛋白进行功能分析，证明其与ISCA等伴侣蛋白互作，参与线粒体铁硫簇的转移过程，并解析了其保守半胱氨酸残基在此过程中的关键作用。
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以上文献均涉及GLRX5重组蛋白的制备或功能研究，涵盖表达纯化、疾病关联及分子机制方向。
**Background of GLRX5 Recombinant Protein**
Glutaredoxin-5 (GLRX5) is a member of the glutaredoxin family, a class of small redox proteins involved in cellular antioxidant defense, iron-sulfur (Fe-S) cluster assembly, and redox signaling. GLRX5. localized primarily in mitochondria, plays a critical role in Fe-S cluster biogenesis—a process essential for electron transport, enzyme catalysis, and iron homeostasis. Mutations in the *GLRX5* gene are linked to pathological conditions, including sideroblastic anemia (e.g., pyridoxine-refractory autosomal recessive sideroblastic anemia) and mitochondrial dysfunction.
Recombinant GLRX5 protein is produced via genetic engineering, typically using bacterial (e.g., *E. coli*) or mammalian expression systems, followed by purification to achieve high homogeneity. Its recombinant form retains the conserved thioredoxin-fold structure and cysteine residues critical for binding Fe-S clusters and mediating redox reactions. Studies utilize recombinant GLRX5 to dissect molecular mechanisms underlying Fe-S transfer, iron regulation, and mitochondrial pathologies. For instance, it helps model how GLRX5 deficiency disrupts heme synthesis or promotes oxidative stress, insights relevant to neurodegenerative diseases (e.g., Friedreich’s ataxia) and metabolic disorders.
Additionally, recombinant GLRX5 serves as a tool for drug discovery, enabling screening for compounds that modulate Fe-S cluster dynamics or mitigate iron overload. Its applications extend to structural biology (e.g., crystallography) and functional assays exploring interactions with partner proteins like ISCU or ABCB7. Overall, GLRX5 recombinant protein bridges basic research and therapeutic innovation, offering a molecular lens to address iron-related and mitochondrial diseases.
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