| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | OXLD1 |
| Uniprot No | Q5BKU9 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 46-147aa |
| 氨基酸序列 | MGSSHHHHHHSSGLVPRGSHMGSPGAQAPDGRRKFGTDHVEVGSQAGADG TRPPKASLPPELQPPTNCCMSGCPNCVWVEYADRLLQHFQDGGERALAAL EEHVADENLKAFLRMEIRLHTRCGG |
| 预测分子量 | 13 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OXLD1重组蛋白的3篇参考文献示例(注：OXLD1相关研究较少，以下内容为模拟文献信息，供参考)：
1. **文献名称**：*"Recombinant OXLD1 Protein Inhibits Tumor Angiogenesis via Blocking VEGF Signaling"*
**作者**：Chen L, et al.
**摘要**：研究团队通过昆虫细胞表达系统成功获得高纯度OXLD1重组蛋白，并发现其通过抑制VEGF信号通路显著降低肿瘤血管生成，为抗肿瘤治疗提供新思路。
2. **文献名称**：*"Expression and Purification of Human OXLD1 in E. coli for Functional Studies"*
**作者**：Wang Y, et al.
**摘要**：报道了一种高效的大肠杆菌表达体系，通过His标签纯化获得活性OXLD1重组蛋白，并验证其与细胞外基质的相互作用，提示其在组织修复中的作用。
3. **文献名称**：*"OXLD1 Recombinant Protein Attenuates Hepatic Fibrosis by Modulating TGF-β Pathway"*
**作者**：Kim S, et al.
**摘要**：利用哺乳动物细胞表达的重组OXLD1蛋白，在小鼠肝纤维化模型中证实其通过调控TGF-β/Smad通路减轻胶原沉积，具有潜在临床应用价值。
**注意**：目前公开数据库中OXLD1(Oxidase-like domain-containing protein 1)的研究较为有限，上述文献为基于相关领域研究的模拟内容。建议通过PubMed或Web of Science以准确关键词(如"OXLD1 recombinant")检索最新文献，或关注该基因的别名及功能相似蛋白的研究进展。
OXLD1 (oxidoreductase-like protein 1) is a member of the NAD(P)-dependent oxidoreductase superfamily, implicated in cellular redox regulation and metabolic processes. Initially identified through genomic sequencing, its gene locus (varies by species) encodes a conserved protein featuring a Rossmann-fold domain typical of nucleotide-binding enzymes. While its precise physiological substrate remains under investigation, structural homology suggests potential roles in detoxification, steroid metabolism, or lipid modification. Dysregulation of OXLD1 has been linked to oxidative stress-related pathologies, including neurodegenerative disorders and cancer, where altered expression correlates with disease progression.
Recombinant OXLD1 protein is typically produced using prokaryotic (e.g., E. coli) or eukaryotic expression systems to enable functional studies. The protein is often purified via affinity tags (e.g., His-tag) followed by size-exclusion chromatography, yielding >90% purity. Active research focuses on characterizing its enzymatic kinetics, substrate specificity, and interactions with redox partners using recombinant variants.
Applications span from in vitro assays exploring its role in reactive oxygen species (ROS) homeostasis to structural biology efforts resolving catalytic mechanisms. Pharmaceutical interest emerges from its potential as a biomarker or therapeutic target, particularly in diseases with redox imbalance. Current challenges include elucidating tissue-specific isoforms and post-translational modifications affecting activity. Ongoing studies employ CRISPR-edited cell models and recombinant OXLD1 to dissect its interplay with signaling pathways like Nrf2/Keap1. advancing its validation as a druggable target.
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