When Recombinant Mouse CD96 (Catalog # 5690-CD) is coated at 1 μg/mL, 100 μL/well, Recombinant Mouse CD155/PVR Fc Chimera (Catalog # 9670-CD) binds with an ED50 of 6‑36 ng/mL.
Recombinant Mouse CD155/PVR Fc Chimera Protein, CF Summary
Details of Functionality
Measured by its binding ability in a functional ELISA. When Recombinant Mouse CD96 (Catalog # 5690-CD) is coated at 1 μg/mL (100 μL/well),
the concentration of Recombinant Mouse CD155/PVR Fc Chimera that produces 50% optimal binding response
is 6-36 ng/mL.
Source
Mouse myeloma cell line, NS0-derived mouse CD155/PVR protein
>90%, 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
62 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
92-108 kDa, reducing conditions
Publications
Read Publications using 9670-CD in the following applications:
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.
Purity
>90%, 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 CD155/PVR Fc Chimera Protein, CF
CD155 antigen
CD155
HVED
NECL5
Necl-5
nectin-like 5
Nectin-like protein 5
poliovirus receptor
PVR
PVS
PVSFLJ25946
Tage4
Background
CD155,
also known as PVR (poliovirus receptor), Necl-5 (nectin-like molecule-5) and,
in rodents, TAGE4 (tumor-associated glycoprotein E4), is a 70-kDa type I
transmembrane glycoprotein in the nectin-related family of adhesion proteins
within the immunoglobulin superfamily (1, 2). CD155, which may play a role in cancer cell
invasion and migration, binds other molecules including Vitronectin, Nectin-3,
DNAM-1/CD226, CD96, and TIGIT but does not bind homotypically (3, 4). Mature
mouse CD155 consists of a 318 amino acid (aa) extracellular domain (ECD) with
one N-terminal V-type and two C2-type Ig-like domains, a 24 aa transmembrane
segment, and a 38 aa cytoplasmic tail. Within the ECD, mouse CD155 shares 46%,
73%, and 44% aa sequence identity with human CD155, rat CD155, and mouse
Nectin-2, respectively. The V-type domain of CD155 mediates all binding,
including to polio virus (1), and alternative splicing within this domain in
humans can modulate ligand binding (5). CD155 is up-regulated on endothelial
cells by IFN-gamma and is highly expressed on immature thymocytes, lymph node
dendritic cells, and tumor cells of epithelial and neuronal origin (1, 2, 6-9).
It is preferentially expressed on Th17 cells compared to Th2 cells (10), and
its activation promotes the development of Th1 responses (11). Enhanced CD155
expression in tumor cells contributes to loss of contact inhibition and
increased migration but also allows tumor cell recognition and killing by
DNAM-1 or CD96 expressing NK cells (1, 7, 12). Binding of monocyte DNAM-1 to
endothelial cell CD155 promotes transendothelial migration (8). The expression
of CD155 on mouse CD8+ thymocytes prevents their premature exit from the thymus
(13). Within intestinal Peyer's patches, follicular dendritic cell CD155
activates follicular helper T cells via DNAM-1 or CD96 binding (7-9, 14). CD155
also binds the inhibitory ligand TIGIT on NK and some mature T cells, antagonizing
DNAM-1 effects (7, 14, 15).
Mandai, K. et al. (2015) Curr. Top. Dev. Biol. 112:197.
Ravens, I. et al. (2003) Biochem. Biophys. Res. Commun. 312:1364.
Sloan, K. et al. (2004) BMC Cancer. 4: 73.
Sato, T. et al. (2004) Genes to Cells 9:791.
Meyer, D. et al. (2009) J. Biol. Chem. 284:2235.
Escalante, N.K. et al. (2011) Arterioscler. Thromb. Vasc. Biol. 31:1177.
Xu, Z. and B. Jin (2010) Cell. Mol. Immunol. 7:11.
Reymond, N. et al. (2004) J. Exp. Med. 199:1331.
Maier, M.K. et al. (2007) Eur. J. Immunol. 37 :2214.
Lozano, E. et al. (2013) J. Immunol. 191:3673.
Yamashita-Kanemaru, Y. et al. (2015) J. Immunol. 194:5644.
Chan, C.J. et al. (2010) J. Immunol. 184:902.
Qui, Q. et al. (2010) J. Immunol. 184:1681.
Seth, S. et al. (2009) Eur. J. Immunol. 39:3160.
Stanietsky, N. et al. (2009) Proc. Natl. Acad. Sci. USA 106:17858.
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