纯度 | >90%SDS-PAGE. |
种属 | Human |
靶点 | DMBT1 |
Uniprot No | Q9UGM3 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 1377-1485aa |
氨基酸序列 | DYSCGGFLSQPSGDFSSPFYPGNYPNNAKCVWDIEVQNNYRVTVIFRDVQ LEGGCNYDYIEVFDGPYRSSPLIARVCDGARGSFTSSSNFMSIRFISDHS ITRRGFRAE |
预测分子量 | 38 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DMBT1重组蛋白的模拟参考文献示例(非真实文献,仅供参考):
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1. **标题**: *Recombinant DMBT1 Protein Binds Pathogenic Bacteria and Enhances Phagocytosis*
**作者**: Müller A, et al.
**摘要**: 研究通过哺乳动物细胞表达系统纯化DMBT1重组蛋白,发现其SRCR结构域可特异性结合革兰氏阳性菌(如肺炎链球菌),并促进巨噬细胞的吞噬作用,揭示了其在黏膜免疫中的潜在功能。
2. **标题**: *Expression and Functional Analysis of DMBT1 in Colorectal Cancer Cell Invasion*
**作者**: Smith J, et al.
**摘要**: 利用昆虫细胞系统表达重组DMBT1蛋白,证实其通过抑制EGFR/ERK信号通路降低结直肠癌细胞的迁移和侵袭能力,提示其作为肿瘤抑制分子的治疗价值。
3. **标题**: *Glycosylation Modulates DMBT1’s Role in Innate Immunity*
**作者**: Tanaka K, et al.
**摘要**: 比较不同表达体系(原核vs真核)中DMBT1重组蛋白的糖基化差异,发现糖基化修饰显著影响其与流感病毒血凝素的结合能力,强调翻译后修饰对其免疫功能的重要性。
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**注**:以上文献为模拟示例,实际研究中建议通过PubMed、Web of Science等数据库检索关键词“DMBT1 recombinant protein”或结合具体研究方向筛选近期高质量论文。
DMBT1 (Deleted in Malignant Brain Tumors 1) is a secreted glycoprotein encoded by the DMBT1 gene located on human chromosome 10q26.13. Initially identified as a potential tumor suppressor in brain and epithelial cancers, DMBT1 has since been recognized for its multifunctional roles in innate immunity, mucosal protection, and tissue homeostasis. Structurally, it belongs to the scavenger receptor cysteine-rich (SRCR) superfamily, characterized by conserved SRCR domains interspersed with CUB (C1r/C1s-Uegf-Bmp1) and ZP (zona pellucida) domains. These domains enable DMBT1 to interact with pathogens (e.g., bacteria, viruses), extracellular matrix components, and immune mediators, functioning as a pattern recognition molecule.
In mucosal surfaces (e.g., lungs, gastrointestinal tract), DMBT1 binds to microbial ligands, promoting pathogen aggregation and clearance while modulating inflammatory responses. It also facilitates epithelial cell migration and differentiation, contributing to tissue repair. Dysregulation of DMBT1 is linked to chronic inflammatory diseases, infections, and cancer progression. For instance, reduced expression correlates with poor prognosis in glioblastoma and colorectal cancer, while elevated levels are observed in cystic fibrosis and COPD, reflecting its context-dependent roles.
Recombinant DMBT1 proteins are engineered to study its biological mechanisms or therapeutic potential. Produced via mammalian, bacterial, or insect cell systems, these proteins retain key functional domains but may lack native glycosylation patterns critical for certain interactions. Research applications include elucidating DMBT1’s role in pathogen neutralization, immune regulation, and epithelial regeneration. Therapeutic exploration focuses on leveraging its anti-inflammatory or antimicrobial properties for mucosal diseases, regenerative medicine, or as a biomarker for cancer and inflammation. Challenges remain in optimizing recombinant forms to mimic endogenous protein behavior, particularly post-translational modifications, to advance translational studies.
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