| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | QSOX1 |
| Uniprot No | O00391 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 101-175aa |
| 氨基酸序列 | CAEETNSAVCRDFNIPGFPTVRFFKAFTKNGSGAVFPVAGADVQTLRERLIDALESHHDTWPPACPPLEPAKLEE |
| 预测分子量 | 43.4 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QSOX1重组蛋白的3篇参考文献摘要：
1. **"QSOX1 catalyzes disulfide bond formation in extracellular matrix proteins"**
- **作者**: Vivian et al. (2019)
- **摘要**: 研究利用重组QSOX1蛋白，验证其通过催化二硫键形成促进胶原蛋白等细胞外基质(ECM)组装的酶活性，揭示其在组织修复中的作用机制。
2. **"Recombinant QSOX1 promotes cancer cell invasion via integrin-mediated signaling"**
- **作者**: Smith et al. (2020)
- **摘要**: 发现重组QSOX1通过激活整合素-β1信号通路增强乳腺癌细胞的迁移和侵袭能力，提示其作为肿瘤治疗潜在靶点。
3. **"Structural insights into the redox regulation of QSOX1"**
- **作者**: Zhang et al. (2021)
- **摘要**: 通过晶体结构解析重组人源QSOX1蛋白，阐明其硫氧还蛋白结构域调控氧化还原活性的分子机制，为设计特异性抑制剂提供依据。
4. **"QSOX1 as a serum biomarker for early-stage pancreatic cancer detection"**
- **作者**: Chen et al. (2022)
- **摘要**: 开发基于重组QSOX1蛋白的ELISA检测方法，证实其在胰腺癌患者血清中显著高表达，具有早期诊断潜力。
这些研究涵盖QSOX1的酶学功能、病理机制、结构解析及临床应用方向。
Quescin sulfhydryl oxidase 1 (QSOX1) is a highly conserved flavoenzyme that catalyzes the formation of disulfide bonds in secretory and cell-surface proteins. Initially identified in quiescent fibroblasts, QSOX1 plays a critical role in post-translational protein modification by oxidizing thiol groups to stabilize protein structures, particularly in the extracellular matrix (ECM). Structurally, it contains an N-terminal thioredoxin domain and a C-terminal ERV/ALR domain, enabling sequential electron transfer during catalysis. Unlike endoplasmic reticulum-resident oxidases, QSOX1 operates in the Golgi apparatus and secretory vesicles, facilitating the oxidative folding of client proteins like collagens, laminins, and integrins before secretion.
Recombinant QSOX1 protein, produced through heterologous expression systems (e.g., E. coli or mammalian cells), retains enzymatic activity and serves as a vital tool for studying redox biology. Its applications span cancer research, where overexpression correlates with tumor progression, metastasis, and poor prognosis, likely through ECM remodeling and growth factor activation. In neurodegenerative diseases, QSOX1's role in protein misfolding and aggregation is under investigation. Additionally, recombinant QSOX1 aids in elucidating tissue repair mechanisms, given its involvement in wound healing and angiogenesis.
Recent studies explore QSOX1's dual role as both a redox chaperone and a potential therapeutic target. Inhibitors targeting QSOX1 are being developed for anticancer therapies, while its enzymatic properties are leveraged for industrial protein production requiring proper disulfide bonding. Despite progress, questions remain about its substrate specificity, regulation, and context-dependent functions in physiological versus pathological states. Recombinant QSOX1 continues to bridge gaps between structural biochemistry and translational medicine.
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