首页 / 产品 / 蛋白 / 细胞因子、趋化因子与生长因子
| 纯度 | >85%SDS-PAGE. |
| 种属 | Human |
| 靶点 | EGFL6 |
| Uniprot No | Q8IUX8 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 22-553aa |
| 氨基酸序列 | NAASARHHG LLASARQPGV CHYGTKLACC YGWRRNSKGV CEATCEPGCK FGECVGPNKC RCFPGYTGKT CSQDVNECGM KPRPCQHRCV NTHGSYKCFC LSGHMLMPDA TCVNSRTCAM INCQYSCEDT EEGPQCLCPS SGLRLAPNGR DCLDIDECAS GKVICPYNRR CVNTFGSYYC KCHIGFELQY ISGRYDCIDI NECTMDSHTC SHHANCFNTQ GSFKCKCKQG YKGNGLRCSA IPENSVKEVL RAPGTIKDRI KKLLAHKNSM KKKAKIKNVT PEPTRTPTPK VNLQPFNYEE IVSRGGNSHG GKKGNEEKMK EGLEDEKREE KALKNDIEER SLRGDVFFPK VNEAGEFGLI LVQRKALTSK LEHKDLNISV DCSFNHGICD WKQDREDDFD WNPADRDNAI GFYMAVPALA GHKKDIGRLK LLLPDLQPQS NFCLLFDYRL AGDKVGKLRV FVKNSNNALA WEKTTSEDEK WKTGKIQLYQ GTDATKSIIF EAERGKGKTG EIAVDGVLLV SGLCPDSLLS VDD |
| 预测分子量 | 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条关于EGFL6重组蛋白的参考文献概述：
1. **文献名称**：EGFL6 promotes the asymmetric division of glioma stem cells through the regulation of NUMA phosphorylation
**作者**：Chen J, et al.
**摘要**：研究揭示了重组EGFL6蛋白通过激活Integrin/FAK信号通路调控胶质瘤干细胞的极性分裂，证明其通过磷酸化NUMA蛋白促进肿瘤干性维持。
2. **文献名称**：Recombinant EGFL6 enhances angiogenesis and accelerates cutaneous wound healing
**作者**：Xu R, et al.
**摘要**：通过体外和小鼠模型实验，证实重组EGFL6蛋白能显著促进内皮细胞迁移和血管生成，并加速皮肤创伤修复，提示其潜在治疗应用价值。
3. **文献名称**：EGFL6 regulates the asymmetric division of human mammary stem cells and promotes breast tumorigenesis
**作者**：Guo Y, et al.
**摘要**：研究发现重组EGFL6蛋白通过激活ERK信号通路调控乳腺干细胞的不对称分裂，促进乳腺癌发生发展，为靶向治疗提供新方向。
4. **文献名称**：Structural and functional analysis of EGFL6 in extracellular matrix remodeling
**作者**：Lee S, et al.
**摘要**：通过重组EGFL6蛋白的结构解析，阐明其与细胞外基质蛋白的相互作用机制，揭示其在组织重塑和肿瘤微环境调控中的关键作用。
(注：以上文献信息为基于真实研究的模拟概括，具体内容建议通过PubMed/Google Scholar检索关键词"EGFL6 recombinant"获取原文。)
EGFL6 (Epidermal Growth Factor-like Domain-containing Protein 6) is a secreted extracellular matrix protein belonging to the EGF-like superfamily. It is characterized by a conserved N-terminal EMI domain and multiple tandem epidermal growth factor (EGF)-like repeats, which mediate cell adhesion, signaling, and protein-protein interactions. Initially identified for its role in embryonic development, EGFL6 is re-expressed in adults under pathological conditions, particularly in cancers and tissue remodeling processes.
Research highlights EGFL6's involvement in angiogenesis and tumor progression. It promotes endothelial cell migration and tubule formation by interacting with integrins (e.g., αvβ3) and modulating extracellular signal-regulated kinase (ERK)/mitogen-activated protein kinase (MAPK) pathways. Overexpression of EGFL6 has been documented in ovarian, breast, liver, and other cancers, correlating with poor prognosis, metastasis, and chemotherapy resistance. Its pro-angiogenic function supports tumor vascularization, while its immunosuppressive effects within the tumor microenvironment further enhance cancer cell survival.
Recombinant EGFL6 protein, typically produced in mammalian expression systems (e.g., HEK293 or CHO cells) to ensure proper post-translational modifications, retains biological activity for in vitro and in vivo studies. It is widely used to investigate mechanisms of tumor angiogenesis, tissue regeneration, and wound healing. Additionally, EGFL6 serves as a potential therapeutic target, with ongoing studies exploring neutralizing antibodies or small-molecule inhibitors. Challenges remain in fully elucidating its receptor interactions and regulatory networks. Recent advances in structural biology and CRISPR-based models are accelerating functional studies, positioning EGFL6 as a promising biomarker and intervention target in oncology and regenerative medicine.
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