Recombinant Human TEM8/ANTXR1 His-tag Protein, CF Summary
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Analysis
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Carrier Free
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.
3886-AR
| Formulation | Lyophilized from a 0.2 μm filtered solution in PBS. |
| 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: | Store the unopened product at -20 to -70 °C. Use a manual defrost freezer and avoid repeated freeze-thaw cycles. Do not use past expiration date. |
Scientific Data
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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.
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2 μg/lane of Recombinant Human TEM8/ANTXR1 was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Blue staining, showing bands at 38 - 46 kDa and 36 - 43 kDa, respectively.
Reconstitution Calculator
Background: TEM8/ANTXR1
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.
- Bradley, Kenneth A, et al. (2001) Nature 414:225.
- Hotchkiss, K. et al. (2004). Experimental Cell Research. 305:133.
- Whittaker, C. and Hynes, R. (2002). Mol Biol Cell. 13:3369.
- Sheng, Fu. et al. (2010) PLOS One. 5(6): e11203.
- Carson-Walter, EB. et al. (2001). Cancer Res. 18:6649.
- Verma, K. et al. (2011) PLOS One. 6(8):e22334.
- Miles, L. et al. (2017). J Clin Invest. 8:2957.
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