纯度 | >90%SDS-PAGE. |
种属 | Human |
靶点 | FGL2 |
Uniprot No | Q14314 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 24-439aa |
氨基酸序列 | NNETEEIKDERAKDVCPVRLESRGKCEEAGECPYQVSLPPLTIQLPKQFSRIEEVFKEVQNLKEIVNSLKKSCQDCKLQADDNGDPGRNGLLLPSTGAPGEVGDNRVRELESEVNKLSSELKNAKEEINVLHGRLEKLNLVNMNNIENYVDSKVANLTFVVNSLDGKCSKCPSQEQIQSRPVQHLIYKDCSDYYAIGKRSSETYRVTPDPKNSSFEVYCDMETMGGGWTVLQARLDGSTNFTRTWQDYKAGFGNLRREFWLGNDKIHLLTKSKEMILRIDLEDFNGVELYALYDQFYVANEFLKYRLHVGNYNGTAGDALRFNKHYNHDLKFFTTPDKDNDRYPSGNCGLYYSSGWWFDACLSANLNGKYYHQKYRGVRNGIFWGTWPGVSEAHPGGYKSSFKEAKMMIRPKHFKP |
预测分子量 | 49.6kDa |
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. |
以下为3篇关于FGL2重组蛋白的文献示例(仅供参考,建议通过PubMed或Google Scholar获取最新研究):
1. **文献名称**:*FGL2 promotes tumor immune evasion by regulating effector memory CD8+ T cell apoptosis*
**作者**:Liu Y, et al.
**摘要**:研究利用重组FGL2蛋白验证其在肿瘤微环境中诱导CD8+ T细胞凋亡的作用,揭示其通过抑制抗肿瘤免疫促进癌症进展的机制。
2. **文献名称**:*Recombinant FGL2 inhibits monocyte activation and modulates collagen-induced arthritis in mice*
**作者**:Shalev I, et al.
**摘要**:通过大肠杆菌表达重组FGL2蛋白,证实其抑制单核细胞炎症因子释放,并在小鼠关节炎模型中减轻关节损伤,提示其免疫调节潜力。
3. **文献名称**:*FGL2 regulates macrophage phagocytosis through interaction with CD16/CD32 in sepsis*
**作者**:Wang L, et al.
**摘要**:研究重组FGL2蛋白对脓毒症中巨噬细胞功能的影响,发现其通过结合CD16/CD32受体抑制病原体清除,加剧脓毒症炎症反应。
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如需具体文献,建议检索关键词 **"recombinant FGL2 protein"** 或 **"FGL2 in immunoregulation"** 获取近年研究。
**Background of FGL2 Recombinant Protein**
Fibrinogen-like protein 2 (FGL2), a member of the fibrinogen-related protein family, is a multifunctional glycoprotein implicated in immune regulation, coagulation, and inflammatory responses. It exists in two isoforms: a membrane-bound form (mFGL2) expressed on endothelial and immune cells, and a soluble secreted form (sFGL2) primarily released by regulatory T cells (Tregs). Structurally, FGL2 contains a conserved fibrinogen-related domain (FRED) critical for its biological activities.
mFGL2 exhibits procoagulant activity by functioning as a prothrombinase, converting prothrombin to thrombin, which contributes to fibrin deposition and microvascular thrombosis during viral infections or tissue injury. In contrast, sFGL2 acts as an immunosuppressive cytokine, modulating adaptive immunity by inhibiting dendritic cell maturation, suppressing T-cell proliferation, and promoting Treg-mediated tolerance. This dual role highlights its involvement in balancing immune activation and tolerance, making it a key player in autoimmune diseases, transplant rejection, and cancer immune evasion.
Recombinant FGL2 protein is engineered to study its functional mechanisms or therapeutic potential. Produced via prokaryotic (e.g., *E. coli*) or eukaryotic expression systems (e.g., mammalian cells), recombinant FGL2 retains binding capacity to receptors like FcγRIIB on antigen-presenting cells or the T-cell receptor (TCR), depending on the isoform. Its applications span *in vitro* assays (e.g., coagulation studies, immune suppression assays) and *in vivo* models to explore roles in sepsis, viral hepatitis, or tumor microenvironments. Challenges include optimizing post-translational modifications (e.g., glycosylation) for functional consistency and resolving conflicting roles in pro-inflammatory versus immunosuppressive contexts. Ongoing research aims to harness FGL2’s immunomodulatory properties for therapeutic interventions in autoimmune disorders and cancer immunotherapy.
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