| 纯度 | >95%SDS-PAGE. |
| 种属 | Human |
| 靶点 | TEM8 |
| 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TEM8(ANTXR1)重组蛋白的3篇参考文献示例，涵盖其功能及应用研究：
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1. **文献名称**：*"Recombinant Expression and Functional Characterization of TEM8/ANTXR1 in Tumor Angiogenesis"*
**作者**：Smith J, et al.
**摘要**：该研究通过基因克隆技术在大肠杆菌中表达了可溶性TEM8重组蛋白，并验证其与配体(如胶原VI)的结合能力。实验表明，重组TEM8能促进内皮细胞迁移，提示其在肿瘤血管生成中的潜在作用。
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2. **文献名称**：*"Structural Insights into TEM8 Extracellular Domain Interaction with Protective Antigen of Bacillus anthracis"*
**作者**：Lee H, et al.
**摘要**：作者解析了TEM8重组胞外域与炭疽杆菌保护性抗原(PA)的复合物晶体结构，揭示了关键结合位点，为设计靶向TEM8的抑制剂提供了结构基础。
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3. **文献名称**：*"TEM8 Recombinant Protein as a Therapeutic Target in Colorectal Cancer Metastasis"*
**作者**：Zhang Y, et al.
**摘要**：研究利用哺乳动物细胞表达系统制备了TEM8-Fc融合蛋白，发现其能抑制肿瘤细胞侵袭并减少转移灶形成，提示靶向TEM8在癌症治疗中的潜力。
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注：以上文献为示例，实际引用时请核对真实来源及发表详情。如需进一步文献检索协助，可提供更具体的研究方向或关键词。
TEM8 (tumor endothelial marker 8), also known as anthrax toxin receptor 1 (ANTXR1), is a cell surface protein first identified in 2001 due to its selective overexpression in tumor-associated endothelial cells. It belongs to the ANTXR family, which includes ANTXR2 (CMG2), both sharing structural homology but differing in ligand-binding specificity. TEM8 is a type I transmembrane protein characterized by a conserved extracellular von Willebrand factor A (vWA) domain, a single-pass transmembrane region, and a short cytoplasmic tail. Its extracellular domain interacts with the protective antigen (PA) component of anthrax toxin, facilitating toxin internalization. However, its physiological role extends beyond pathogen entry.
Functionally, TEM8 is implicated in cell adhesion, migration, and signaling. It binds extracellular matrix components like collagen α1 and α2 chains through its vWA domain, suggesting involvement in tissue remodeling and angiogenesis. In cancer biology, TEM8 is upregulated in tumor vasculature and certain malignant cells, correlating with poor prognosis. Studies propose it promotes tumor angiogenesis by regulating endothelial cell proliferation and vascular patterning, possibly via integrin-like signaling pathways. Additionally, TEM8 may influence tumor cell invasiveness through matrix metalloproteinase regulation.
Beyond oncology, TEM8’s role in anthrax infection highlights its significance in infectious disease. Its dual relevance in pathology and homeostasis—such as collagen organization during development—underscores functional versatility. Recent research explores TEM8-targeted therapies, including antibody-drug conjugates and anti-angiogenic agents, capitalizing on its tumor-specific expression. However, its precise signaling mechanisms and interactions with endogenous ligands remain areas of active investigation, offering potential insights into both cancer biology and infectious disease pathways.
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