The Recombinant Human TEM8/ANTXR1 Protein is a biologically active recombinant protein that plays a significant role in various cellular processes and signaling pathways in human biology. This protein is widely employed in immunological research, cell biology studies, protein-protein interaction analyses, and therapeutic development, providing researchers with a reliable tool for investigating TEM8/ANTXR1 function and its implications in health and disease.
This product (SKU: RPCB1267) is produced using HEK293 cells and features a C-His tag for convenient detection and purification. The protein exhibits a calculated molecular weight of 19.65 kDa with an observed molecular weight of 40-50 kDa under denaturing conditions, achieving ≥ 95 % as determined by SDS-PAGE., ensuring exceptional quality and consistency for research applications.
High quality, high purity and low endotoxin recombinant Recombinant Human TEM8/ANTXR1 Protein (RPCB1267), tested reactivity in HEK293 cells and has been validated in SDS-PAGE.100% guaranteed.
Endotoxin:
< 0.01 EU/μg of the protein by LAL method
Purity:
≥ 95 % as determined by SDS-PAGE.
Formulation:
Lyophilized from 0.22 μm filtered solution in PBS (pH 7.4). Normally 8% trehalose is added as protectant before lyophilization.
Reconstitution:
Centrifuge the vial before opening. Reconstitute to a concentration of 0.1-0.5 mg/mL in sterile distilled water. Avoid vortex or vigorously pipetting the protein. For long term storage, it is recommended to add a carrier protein or stablizer (e.g. 0.1% BSA, 5% HSA, 10% FBS or 5% Trehalose), and aliquot the reconstituted protein solution to minimize free-thaw cycles.
Storage:
Store at -20℃.Store the lyophilized protein at -20℃ to -80 ℃ up to 1 year from the date of receipt. After reconstitution, the protein solution is stable at -20℃ for 3 months, at 2-8℃ for up to 1 week.
Anthrax toxin receptor 1 (ANTXR1), also known as Tumor endothelial marker 8 (TEM8), is a glycoprotein of the Anthrax Toxin Receptor family that is expressed by endothelial cells. Anthrax toxin receptor 1 contains a 289 amino acid (aa) extracellular domain, a 21 aa transmembrane domain, and a 222 aa cytoplasmic domain. Type I transmembrane isoforms of 564 aa (80‑85 kDa) and 368 aa (60 kDa) and potentially secreted isoforms of 330 aa and 297 aa (45 kDa) are differentially expressed. All diverge at the C-terminal end but share the N-terminal extracellular domain. The extracellular domain shares structural similarity with von Willebrand factor type (vWFA) domains, which are characterized by their interactions with ECM components. The extracellular domain is involved in reorganization of cell actin cytoskeleton. Anthrax Receptor 1 binds Anthrax Protective Antigen with lesser affinity that Anthrax Receptor 2 and induces toxin internalization. Anthrax toxin receptor 1 has been implicated in tumor angiogenesis, as its expression has been shown to up-regulate in tumor blood vessels and is characterized as a tumor endothelial marker. ANTXR-1 was reported to be an amplifier of Wnt signaling in tumor microenvironment. Additionally, Anthrax toxin receptor 1 serves as the receptor for Seneca Valley virus, an oncolytic picornavirus affecting neuroendocrine cancers. Human ANTXR1 shares 99% aa identity with mouse and rat and 92% identity with dog and chick ANTXR1 within the extracellular domain.
Recombinant Human TEM8/ANTXR1 Protein was determined by SDS-PAGE under reducing conditions with Coomassie Blue.
