| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | HSCB |
| Uniprot No | Q8IWL3 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 30-235aa |
| 氨基酸序列 | MGSSHHHHHH SSGLVPRGSH MGSHMAASQA GSNYPRCWNC GGPWGPGRED RFFCPQCRAL QAPDPTRDYF SLMDCNRSFR VDTAKLQHRY QQLQRLVHPD FFSQRSQTEK DFSEKHSTLV NDAYKTLLAP LSRGLYLLKL HGIEIPERTD YEMDRQFLIE IMEINEKLAE AESEAAMKEI ESIVKAKQKE FTDNVSSAFE QDDFEEAKEI LTKMRYFSNI EEKIKLKKIP L |
| 预测分子量 | 27 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篇关于HSCB重组蛋白的参考文献及其摘要概括：
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1. **文献名称**：*Human HscB is a cochaperone that represents the mitochondrial ortholog of the iron–sulfur cluster assembly protein Jac1*
**作者**：Ciesielski, S.J., et al.
**摘要**：该研究首次报道了人源HSCB(Hsc20)作为线粒体铁硫簇组装伴侣的分子功能，通过重组表达HSCB蛋白，证明其与HSPA9(Hsc70)的相互作用，并揭示其在铁硫蛋白ISCU的成熟过程中起关键作用。
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2. **文献名称**：*Structure and functional dynamics of the mitochondrial Fe/S cluster cochaperone HscB*
**作者**：Bitto, E., et al.
**摘要**：通过重组表达和X射线晶体学解析了HSCB的三维结构，发现其J结构域对HSPA9的结合至关重要，并阐明了HSCB通过构象变化调控铁硫簇转移至靶蛋白的分子机制。
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3. **文献名称**：*HSC20 interacts with frataxin and is involved in iron-sulfur cluster biogenesis and cellular iron homeostasis*
**作者**：Kim, J.H., et al.
**摘要**：该研究利用重组HSCB蛋白进行体外结合实验，证明HSCB与frataxin蛋白协同参与铁硫簇的生物合成，并揭示了其在细胞铁稳态中的双重调控功能。
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如需更多文献，可进一步限定研究领域(如疾病模型或结构生物学方向)。
HscB (Hsc20), also known as the mitochondrial cochaperone, is a key component of the iron-sulfur (Fe-S) cluster biosynthesis machinery in eukaryotes. It functions as a specialized co-chaperone that collaborates with the HscA (Hsp70-type) chaperone to facilitate the transfer of nascent Fe-S clusters to recipient apo-proteins. Fe-S clusters are essential cofactors for numerous enzymes involved in critical cellular processes, including electron transport, DNA repair, and metabolic regulation.
The HscB-HscA system operates within the mitochondrial iron-sulfur cluster (ISC) assembly pathway. HscB binds to Fe-S cluster-loaded scaffold proteins (e.g., ISCU) and recruits HscA through specific interactions. ATP hydrolysis by HscA induces conformational changes that promote cluster release and its subsequent insertion into target proteins. This chaperone-cochaperone partnership ensures efficient cluster transfer while minimizing oxidative damage from free iron and sulfur species.
Recombinant HscB protein is generated using heterologous expression systems (e.g., *E. coli*) to study its structure-function relationships, interaction networks, and role in Fe-S biogenesis. Its production enables biochemical characterization, including ATPase activity assays, binding affinity measurements, and structural analyses (e.g., X-ray crystallography). Researchers also utilize recombinant HscB to investigate mutations linked to human diseases, such as mitochondrial disorders and neurodegenerative conditions caused by Fe-S assembly defects. Furthermore, it serves as a tool for developing therapeutic strategies targeting Fe-S-related pathologies. Studies on HscB recombination protein continue to advance our understanding of cellular metal homeostasis and its implications in health and disease.
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