Recombinant Human TEM8/ANTXR1 His-tag Protein, CF

When anthrax protective antigen (PA) is coated at 1.5 μg/mL, 100 μL/well, Recombinant Human TEM8/ANTXR1 (Catalog # 3886-AR) binds with an ED50 of 0.6-3.6 μg/mL.

2 μg/lane of Recombinant Human TEM8/ANTXR1 was resolved with SDS-PAGE underreducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Bluestaining, showing bands at 38 - 46 kDa and 36 - 43 kDa, respectively.

• Reactivity: Hu
• Applications: Bioactivity
• Format: Carrier-Free

Recombinant Human TEM8/ANTXR1 His-tag Protein, CF Summary

• Details of Functionality: Measured by its binding ability in a functional ELISA. When Anthrax Protective Antigen is coated at 1.5 μg/mL (100 μL/well), the concentration of Recombinant Human TEM8/ANTXR1 that produces 50% optimal binding response is 0.6-3.6 μg/mL.
• Source: Human embryonic kidney cell, HEK293-derived human TEM8/ANTXR1 protein
  Glu33-Ser321, with a C-terminal 6-His tag
• Accession #: Q9H6X2
• N-terminal Sequence: No results obtained. Gln28 inferred from enzymatic pyroglutamate treatment revealing Gly29
• Structure / Form: Monomer
• Protein/Peptide Type: Recombinant Proteins
• Purity: >95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
• Endotoxin Note: <0.10 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

• Dilutions:
  • Bioactivity
• Theoretical MW: 34 kDa.
  Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.
• SDS-PAGE: 38-46 kDa, reducing conditions

Packaging, Storage & Formulations

• Storage: Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
  • 12 months from date of receipt, -20 to -70 °C as supplied.
  • 1 month, 2 to 8 °C under sterile conditions after reconstitution.
  • 3 months, ≤ -20 °C under sterile conditions after reconstitution.
• Buffer: Lyophilized from a 0.2 μm filtered solution in PBS.
• Purity: >95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
• Reconstitution Instructions: Reconstitute at 500 μg/mL in PBS.

Notes

This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.

Alternate Names for Recombinant Human TEM8/ANTXR1 His-tag Protein, CF

• anthrax toxin receptor 1
• ANTXR1
• ATR2310008J16Rik
• FLJ10601
• FLJ11298
• FLJ21776
• TEM8
• TEM82810405N18Rik
• Tumor endothelial marker 8

Background

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 (1). The extracellular domain shares structural similarity with von Willebrand factor type (vWFA) domains, which are characterized by their interactions with ECM components (2, 3). The extracellular domain is involved in reorganization of cell actin cytoskeleton (2, 3). Anthrax Receptor 1 binds Anthrax Protective Antigen with lesser affinity that Anthrax Receptor 2 and induces toxin internalization (4). 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 (5). ANTXR-1 was reported to be an amplifier of Wnt signaling in tumor microenvironment (6). Additionally, Anthrax toxin receptor 1 serves as the receptor for Seneca Valley virus, an oncolytic picornavirus affecting neuroendocrine cancers (7). Human ANTXR1 shares 99% aa identity with mouse and rat and 92% identity with dog and chick ANTXR1 within the extracellular domain.

1. Bradley, Kenneth A, et al. (2001) Nature 414:225.
2. Hotchkiss, K. et al. (2004). Experimental Cell Research. 305:133.
3. Whittaker, C. and Hynes, R. (2002). Mol Biol Cell. 13:3369.
4. Sheng, Fu. et al. (2010) PLOS One. 5(6): e11203.
5. Carson-Walter, EB. et al. (2001). Cancer Res. 18:6649.
6. Verma, K. et al. (2011) PLOS One. 6(8):e22334.
7. Miles, L. et al. (2017). J Clin Invest. 8:2957.

Bioinformatics

• Uniprot:
  • Q9H6X2()