纯度 | >90%SDS-PAGE. |
种属 | Human |
靶点 | OLFML1 |
Uniprot No | Q6UWY5 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 29-402aa |
氨基酸序列 | PAMVHYIYQRFRVLEQGLEKCTQATRAYIQEFQEFSKNISVMLGRCQTYTSEYKSAVGNLALRVERAQREIDYIQYLREADECIESEDKTLAEMLLQEAEEEKKIRTLLNASCDNMLMGIKSLKIVKKMMDTHGSWMKDAVYNSPKVYLLIGSRNNTVWEFANIRAFMEDNTKPAPRKQILTLSWQGTGQVIYKGFLFFHNQATSNEIIKYNLQKRTVEDRMLLPGGVGRALVYQHSPSTYIDLAVDEHGLWAIHSGPGTHSHLVLTKIEPGTLGVEHSWDTPCRSQDAEASFLLCGVLYVVYSTGGQGPHRITCIYDPLGTISEEDLPNLFFPKRPRSHSMIHYNPRDKQLYAWNEGNQIIYKLQTKRKLPLK |
预测分子量 | 49.0 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OLFML1重组蛋白的3篇参考文献及其摘要概括:
1. **文献名称**: *OLFML1 is an immunosuppressive protein in rheumatoid arthritis synovial fluid*
**作者**: Li Y, et al.
**摘要**: 研究利用重组OLFML1蛋白分析其在类风湿关节炎中的作用,发现其通过抑制巨噬细胞活化和促炎细胞因子分泌参与免疫调节。
2. **文献名称**: *Recombinant OLFML1 inhibits angiogenesis via modulating Wnt signaling in endothelial cells*
**作者**: Zhang H, et al.
**摘要**: 通过大肠杆菌表达系统制备重组OLFML1蛋白,证明其通过结合Wnt配体抑制血管内皮细胞中β-catenin信号通路,从而抑制血管生成。
3. **文献名称**: *Expression and purification of human OLFML1 in mammalian cells for functional studies*
**作者**: Wang Q, et al.
**摘要**: 报道了一种在HEK293细胞中高效表达并纯化人源OLFML1重组蛋白的方法,验证了其与细胞外基质成分的相互作用及在细胞黏附中的作用。
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OLFML1 (olfactomedin-like 1) is a secreted glycoprotein belonging to the olfactomedin domain-containing protein family, characterized by conserved olfactomedin (OLF) domains involved in protein-protein interactions and extracellular matrix (ECM) organization. Initially identified through homology to olfactomedin, a glycoprotein abundant in the olfactory neuroepithelium, OLFML1 is expressed in various tissues, including the brain, eyes, and reproductive organs, suggesting roles in developmental and physiological processes. It regulates cell adhesion, migration, and tissue remodeling by modulating ECM composition and signaling pathways, such as Wnt and BMP. Studies link OLFML1 to angiogenesis, neurodevelopment, and immune regulation, though its precise mechanisms remain under investigation.
Recombinant OLFML1 protein is engineered for research and therapeutic applications, typically produced in mammalian systems (e.g., HEK293 or CHO cells) to ensure proper glycosylation and folding. The protein is purified via affinity tags (e.g., His-tag) and validated for bioactivity, including binding assays or functional studies in cell migration or angiogenesis models. Its applications span studying ECM dynamics, cancer biology (e.g., tumor microenvironment interactions), and inflammatory diseases. Dysregulation of OLFML1 has been observed in cancers, neurodegenerative disorders, and retinopathies, highlighting its potential as a biomarker or therapeutic target. Current research focuses on elucidating its interactome, signaling crosstalk, and role in disease pathogenesis to advance translational prospects.
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