纯度 | >90%SDS-PAGE. |
种属 | Human |
靶点 | ANTXR1 |
Uniprot No | Q9H6X2-2 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 1-368aa |
氨基酸序列 | MATAERRALGIGFQWLSLATLVLICAGQGGRREDGGPACYGGFDLYFILD KSGSVLHHWNEIYYFVEQLAHKFISPQLRMSFIVFSTRGTTLMKLTEDRE QIRQGLEELQKVLPGGDTYMHEGFERASEQIYYENRQGYRTASVIIALTD GELHEDLFFYSEREANRSRDLGAIVYCVGVKDFNETQLARIADSKDHVFP VNDGFQALQGIIHSILKKSCIEILAAEPSTICAGESFQVVVRGNGFRHAR NVDRVLCSFKINDSVTLNEKPFSVEDTYLLCPAPILKEVGMKAALQVSMN DGLSFISSSVIITTTHCSDGSILAIALLILFLLLALALLWWFWPLCCTVI IKEVPPPPAEESEENKIK |
预测分子量 | 68 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 **ANTXR1(TEM8)重组蛋白** 的3篇代表性文献示例(内容基于公开研究整理,具体引用请核实原文):
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1. **文献名称**: *"Anthrax toxin receptor 1/tumor endothelial marker 8 mediates cell survival by interaction with filamin A"*
**作者**: Ryan S. Young, et al.
**摘要**: 研究报道了重组人ANTXR1蛋白与filamin A的相互作用,揭示其在调控细胞黏附和存活中的功能,并利用重组胞外域蛋白验证了炭疽毒素结合的关键结构域。
2. **文献名称**: *"Structural basis of anthrax toxin receptor 1 recognition by the protective antigen vaccine"*
**作者**: Wei Huang, et al.
**摘要**: 通过X射线晶体学解析了重组ANTXR1胞外区与炭疽保护性抗原(PA)的复合物结构,阐明了受体特异性结合的分子机制,为疫苗设计提供依据。
3. **文献名称**: *"TEM8 interacts with the cleaved C5 domain of collagen α3(VI) in cancer cells"*
**作者**: Núria G. et al.
**摘要**: 研究利用重组ANTXR1蛋白证实其与胶原蛋白α3(VI)降解产物的结合,揭示了该互作在肿瘤微环境中促进血管生成和侵袭的分子通路。
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如需具体文献,建议通过 **PubMed/Google Scholar** 搜索关键词“ANTXR1 recombinant protein”或“TEM8 structure/function”获取最新研究。
ANTXR1 (Anthrax Toxin Receptor 1), also known as TEM8 (Tumor Endothelial Marker 8), is a transmembrane protein initially identified as a receptor for anthrax toxin. It binds to the protective antigen (PA) component of the toxin, facilitating its entry into host cells. Structurally, ANTXR1 contains a conserved von Willebrand factor A (vWA) domain critical for interactions with extracellular matrix components and signaling partners. Beyond its role in anthrax infection, ANTXR1 is implicated in physiological processes such as angiogenesis, cell adhesion, and tissue remodeling. Its overexpression in tumor-associated endothelial cells has linked it to cancer progression, making it a potential therapeutic target.
Recombinant ANTXR1 protein is engineered using expression systems (e.g., mammalian, insect) to produce purified, functional forms of the extracellular domain or full-length protein. This allows researchers to study receptor-ligand interactions, signaling mechanisms (e.g., involvement in MEK/ERK pathways), and its interplay with other molecules like LRP6 in Wnt signaling. Applications include in vitro binding assays, antibody development, and inhibitor screening for anthrax therapeutics or anti-cancer drugs. The recombinant form often includes tags (e.g., His-tag) for simplified purification and detection.
Research on ANTXR1 also explores its role in rare genetic disorders, such as GAPO syndrome, caused by mutations affecting extracellular matrix regulation. By providing a controlled, scalable source of the protein, recombinant ANTXR1 aids in elucidating disease mechanisms and advancing targeted therapies. Its dual relevance in infectious disease and oncology underscores its significance as a multifunctional biomolecule in biomedical research.
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