Recombinant Mouse TEM8/ANTXR1 Fc Chimera Protein, CF Summary
Accession # Q9CZ52
CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.
In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.
|Formulation||Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose.|
|Reconstitution||Reconstitute at 500 μg/mL in PBS.|
|Shipping||The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below.|
|Stability & Storage:||Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
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.
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.
- Bradley, KA. et al. (2001) Nature 414:225.
- Hotchkiss, K. et al. (2004). Experimental Cell Research. 305:133.
- Whittaker, CA. and Hynes, R. (2002). Mol Biol Cell. 13:3369.
- Fu, S. et al. (2010) PLOS One. 5:e11203.
- Carson-Walter, EB. et al. (2001). Cancer Res. 18:6649.
- Verma, K. et al. (2011) PLOS One. 6:e22334.
- Miles, L. et al. (2017). J Clin Invest. 8:2957.
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