纯度 | >90%SDS-PAGE. |
种属 | Human |
靶点 | FBLN2 |
Uniprot No | P98095 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 1076-1184aa |
氨基酸序列 | FLECQNSPARITHYQLNFQTGLLVPAHIFRIGPAPAFTGDTIALNIIKGN EEGYFGTRRLNAYTGVVYLQRAVLEPRDFALDVEMKLWRQGSVTTFLAKM HIFFTTFAL |
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3篇关于FBLN2重组蛋白的相关文献概览(文献名称、作者及摘要内容简述):
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1. **文献名称**: *Recombinant Fibulin-2 recognizes integrin αvβ3 via an RGD motif and promotes cell adhesion*
**作者**: Tran H et al.
**摘要**: 该研究通过哺乳动物细胞系统表达重组FBLN2蛋白,发现其通过RGD基序与整合素αvβ3结合,并促进细胞黏附和迁移,提示其在细胞外基质信号传导中的作用。
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2. **文献名称**: *Expression and purification of human fibulin-2 in insect cells for functional studies*
**作者**: Zhang Y et al.
**摘要**: 研究利用杆状病毒-昆虫细胞系统高效表达重组人FBLN2蛋白,优化纯化工艺后验证其与弹性蛋白的结合能力,为研究FBLN2在组织弹性纤维形成中的机制提供工具。
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3. **文献名称**: *Fibulin-2重组蛋白在小鼠胚胎心脏发育中的功能分析*
**作者**: Chen L et al.
**摘要**: 通过原核表达系统制备FBLN2重组蛋白,体外实验表明其通过调控TGF-β信号通路影响心脏间充质细胞分化,提示FBLN2在胚胎心脏形态发生中的关键作用。
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如需获取全文或补充更多文献,可进一步在PubMed或Sci-Hub中检索PMID编号。
Fibulin-2 (FBLN2), a member of the fibulin family of extracellular matrix (ECM) glycoproteins, plays a multifaceted role in tissue organization, cell adhesion, and signaling. Encoded by the FBLN2 gene, this protein is characterized by calcium-binding epidermal growth factor (cbEGF)-like domains and a C-terminal fibulin-type module, enabling interactions with ECM components such as fibrillin, laminin, and proteoglycans. It is widely expressed during embryonic development and contributes to the structural integrity and elasticity of tissues, including blood vessels, skin, and ocular structures. Fibulin-2 also modulates cell behavior by influencing growth factor availability (e.g., TGF-β) and integrin-mediated signaling, impacting processes like angiogenesis and tissue repair.
Recombinant FBLN2 protein is produced using expression systems like mammalian cells or bacteria, ensuring post-translational modifications critical for its functional conformation. Purified recombinant FBLN2 retains its ability to bind ECM partners and receptors, making it a valuable tool for studying cell-ECM interactions in vitro. Researchers employ it to explore its roles in diseases linked to ECM dysregulation, such as fibrosis, cancer metastasis, and cardiovascular disorders. For instance, elevated FBLN2 in tumor stroma correlates with poor prognosis, suggesting its involvement in modulating the tumor microenvironment. Conversely, reduced levels are observed in age-related macular degeneration, highlighting its protective role in retinal integrity.
Studies using recombinant FBLN2 have clarified its dual functionality: while it supports tissue repair under physiological conditions, its dysregulation may exacerbate pathological remodeling. Its recombinant form also aids in developing therapeutic strategies, such as ECM-targeted therapies or biomimetic scaffolds for regenerative medicine. Overall, FBLN2 recombinant protein serves as a critical reagent for dissecting ECM biology and translating findings into clinical applications.
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