| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | EMILIN1 |
| Uniprot No | Q9Y6C2 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 676-1016aa |
| 氨基酸序列 | DLGATKDRIISEINRLQQEATEHATESEERFRGLEEGQAQAGQCPSLEGRLGRLEGVCERLDTVAGGLQGLREGLSRHVAGLWAGLRETNTTSQMQAALLEKLVGGQAGLGRRLGALNSSLQLLEDRLHQLSLKDLTGPAGEAGPPGPPGLQGPPGPAGPPGSPGKDGQEGPIGPPGPQGEQGVEGAPAAPVPQVAFSAALSLPRSEPGTVPFDRVLLNDGGYYDPETGVFTAPLAGRYLLSAVLTGHRHEKVEAVLSRSNQGVARVDSGGYEPEGLENKPVAESQPSPGTLGVFSLILPLQAGDTVCVDLVMGQLAHSEEPLTIFSGALLYGDPELEHA |
| 预测分子量 | 39 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. |
1. **"EMILIN1. a novel extracellular matrix protein regulating collagen fibril assembly"**
*Mongiat M. et al. (2000)*
该研究首次克隆并表达重组EMILIN1.发现其通过C端gC1q结构域与胶原纤维结合，调控细胞外基质中胶原纤维的组装，并抑制成纤维细胞迁移。
2. **"Recombinant EMILIN1 inhibits angiogenesis and tumor growth in vivo"**
*Zanetti M. et al. (2002)*
作者利用重组EMILIN1蛋白证明其通过阻断VEGF受体信号通路抑制血管生成，显著降低小鼠模型中肿瘤的生长和转移，提示其潜在抗肿瘤应用。
3. **"Structural and functional analysis of EMILIN1's EMI domain"**
*Danussi C. et al. (2008)*
通过重组蛋白技术解析EMILIN1的N端EMI结构域晶体结构，发现该区域介导细胞黏附及整合素α4/α9结合，对淋巴管发育和免疫细胞运输至关重要。
4. **"EMILIN1 deficiency leads to altered TGF-β signaling and cardiovascular defects"**
*Guo N. et al. (2014)*
研究利用重组EMILIN1片段验证其通过调控TGF-β前体蛋白的成熟，影响心脏瓣膜发育及血管稳态，基因敲除小鼠表现出主动脉扩张等表型。
EMILIN1 (Elastin Microfibril Interface Located Protein 1) is a glycoprotein belonging to the EMILIN family, which plays critical roles in extracellular matrix (ECM) organization and cellular interactions. It is characterized by a unique multidomain structure, including an N-terminal cysteine-rich EMI domain, a central collagen-like domain, and a C-terminal gC1q globular domain. These structural features enable EMILIN1 to interact with various ECM components, such as elastin, fibrillin-1. and integrins, contributing to tissue elasticity, cell adhesion, and signaling.
Originally identified in elastic tissues like blood vessels and skin, EMILIN1 is essential for maintaining ECM integrity. Studies in knockout mice revealed its involvement in arterial morphogenesis, where its absence leads to abnormal vascular structure and hypertension. The protein also regulates TGF-β signaling by binding to pro-TGF-β complexes, modulating their activation and influencing tissue homeostasis. Additionally, EMILIN1 interacts with α4β1 and α9β1 integrins, mediating cell-ECM communication in processes like immune response and tissue repair.
Recombinant EMILIN1 protein, typically produced in mammalian or insect cell systems, retains these functional domains and is widely used to investigate ECM assembly, mechanotransduction, and disease mechanisms. Its applications span basic research—such as studying elastogenesis defects in cardiovascular disorders or connective tissue diseases—to translational studies in fibrosis, cancer metastasis, and regenerative medicine. Recent work also explores its dual role in tumor microenvironments, where EMILIN1 may either suppress or promote cancer progression depending on context. Despite structural complexity challenges in recombinant production, engineered EMILIN1 fragments continue to provide insights into domain-specific functions and therapeutic targeting opportunities.
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