Recombinant Mouse TEM8/ANTXR1 Fc Chimera Protein, CF

When Anthrax Protective Antigen is immobilized at 1.5 μg/mL, 100 μL/well, Recombinant Mouse TEM8/ANTXR1 Fc Chimera (Catalog # 10202-AR) binds with an ED50 of 5-30 ng/mL.

2 μg/lane of Recombinant Mouse TEM8/ANTXR1 Fc Chimera (Catalog # 10202-AR) was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Blue staining, showing bands at 62-81 kDa and 125-160 kDa, respectively.

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

Recombinant Mouse TEM8/ANTXR1 Fc Chimera Protein, CF Summary

• Details of Functionality: Measured by its binding ability in a functional ELISA. When Anthrax Protective Antigen is immobilized at 1.5 μg/mL (100 μL/well), the concentration of Recombinant Mouse TEM8/ANTXR1 Fc Chimera (Catalog # 10202-AR) that produces 50% of the optimal binding response is 5-30 ng/mL.
• Source: Mouse myeloma cell line, NS0-derived mouse TEM8/ANTXR1 protein
  

  Mouse TEM8/ANTXR1 (Glu31-Ser319) Accession # Q9CZ52	IEGRMDP	Mouse IgG2a (Glu98-Lys330)
  N-terminus		C-terminus

• Accession #: Q9CZ52
• N-terminal Sequence: Glu31
• Structure / Form: Disulfide-linked homodimer
• 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: 60 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: 62-81 kDa, under 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 to -70 °C under sterile conditions after reconstitution.
• Buffer: Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose.
• 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 Mouse TEM8/ANTXR1 Fc Chimera 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. TEM8/ANTXR1 contains a 289 amino acid (aa) extracellular domain, a 21 aa transmembrane domain, and a 222 aa cytoplasmic domain. Isoforms diverging at the C-termiuns include 564 aa (80‑85 kDa), 368 aa (60 kDa), and potentially secreted isoforms of 330 aa and 297 aa (45 kDa) (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). TEM8/ANTXR1 binds Anthrax Protective Antigen with lesser affinity that Anthrax Receptor 2 and induces toxin internalization (4). TEM8/ANTXR1 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). TEM8/ANTXR1 was reported to be an amplifier of Wnt signaling in tumor microenvironment (6). Additionally, TEM8/ANTXR1 serves as the receptor for Seneca Valley virus, an oncolytic picornavirus affecting neuroendocrine cancers (7). Mouse TEM8/ANTXR1 shares 99% and 100% aa identity with human and rat TEM8/ANTXR1, respectively, within the extracellular domain.

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

Bioinformatics

• Uniprot:
  • Q9CZ52()