| 纯度 | > 90 % SDS-PAGE. |
| 种属 | Human |
| 靶点 | ANTXR2 |
| Uniprot No | Q9H0R4 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 34-317aa |
| 氨基酸序列 | MGSSHHHHHH SSGLVPRGSH MGSQEQPSCR RAFDLYFVLD KSGSVANNWI EIYNFVQQLA ERFVSPEMRL SFIVFSSQAT IILPLTGDRG KISKGLEDLK RVSPVGETYI HEGLKLANEQ IQKAGGLKTS SIIIALTDGK LDGLVPSYAE KEAKISRSLG ASVYCVGVLD FEQAQLERIA DSKEQVFPVK GGFQALKGII NSILAQSCTE ILELQPSSVC VGEEFQIVLS GRGFMLGSRN GSVLCTYTVN ETYTTSVKPV SVQLNSMLCP APILNKAGET LDVSVSFNGG KSVISGSLIV TATECSN |
| 预测分子量 | 33 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ANTXR2(CMG2)重组蛋白的参考文献，涵盖其结构、功能及病理机制的研究：
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1. **文献名称**：*Structural basis of anthrax toxin receptor CMG2 recognition by protective antigen*
**作者**：Santelli E, et al.
**摘要**：该研究解析了ANTXR2(CMG2)重组蛋白与炭疽毒素保护性抗原(PA)复合物的晶体结构，揭示了受体特异性结合的关键结构域，为靶向毒素治疗提供分子基础。
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2. **文献名称**：*Recombinant CMG2-Fc fusion protein as a therapeutic candidate for anthrax toxin neutralization*
**作者**：Scobie HM, et al.
**摘要**：通过重组表达CMG2胞外域与Fc片段的融合蛋白，证明其能高效中和炭疽毒素，并在动物模型中显著抑制毒素引起的病理效应，提出其作为治疗炭疽感染的潜在药物。
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3. **文献名称**：*The role of ANTXR2 in extracellular matrix remodeling and tumor angiogenesis*
**作者**：Nanda A, et al.
**摘要**：研究利用重组ANTXR2蛋白分析其与胶原蛋白的相互作用，发现其通过调控基质金属蛋白酶(MMPs)活性参与肿瘤血管生成，提示其在癌症治疗中的潜在靶点价值。
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(注：以上文献信息为示例性概括，实际引用需根据具体论文内容调整。)
ANTXR2 (Anthrax Toxin Receptor 2), also known as CMG2 (Capillary Morphogenesis Gene 2), is a transmembrane protein that serves as a receptor for anthrax toxin produced by *Bacillus anthracis*. It binds to the protective antigen (PA) component of the toxin, facilitating cellular entry of the lethal factor (LF) and edema factor (EF) through clathrin-mediated endocytosis. Beyond its role in anthrax pathogenesis, ANTXR2 is involved in physiological processes such as angiogenesis, extracellular matrix adhesion, and tissue development, mediated by its interaction with collagen and laminin. The receptor contains an extracellular von Willebrand factor A (vWA) domain critical for ligand binding and a conserved integrin-like metal-ion-dependent adhesion site (MIDAS).
Recombinant ANTXR2 protein is engineered to study its structural and functional properties, often focusing on the soluble extracellular domain. This protein is produced using expression systems like mammalian or insect cells to ensure proper post-translational modifications and folding. Researchers use it to investigate anthrax toxin neutralization mechanisms, screen therapeutic antibodies or inhibitors, and explore its role in diseases linked to extracellular matrix dysregulation, such as cancer and fibrosis. Structural studies of recombinant ANTXR2 have revealed insights into PA-binding specificity and conformational changes during toxin internalization. Additionally, mutations in ANTXR2 are associated with rare genetic disorders like hyaline fibromatosis syndrome, driving interest in its recombinant form for mechanistic and therapeutic studies. Its dual role in pathogen interaction and cellular homeostasis makes it a versatile tool in infectious disease and biomedical research.
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