Recombinant Cynomolgus CD155/PVR Fc Chimera Protein, CF Summary
Details of Functionality |
Measured by its binding ability in a functional ELISA. When Recombinant Cynomolgus Monkey CD155/PVR Fc Chimera
is coated at 5 μg/mL (100 μL/well), the concentration of Recombinant Human CD96v2 Fc Chimera (Catalog # 9556-CD)
that produces 50% optimal binding response is 0.25-1.25 μg/mL.
|
Source |
Human embryonic kidney cell, HEK293-derived cynomolgus monkey CD155/PVR protein Cynomolgus Monkey CD155/PVR (Asp28-Asn343) Unique Sequence | IEGRMD | Human IgG1 (Pro100-Lys330) | N-terminus | | C-terminus | |
|
Accession # |
|
N-terminal Sequence |
Asp28 |
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 |
|
Theoretical MW |
85 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 |
68-77 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 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 Cynomolgus CD155/PVR Fc Chimera Protein, CF
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 may play a role
in cancer cell invasion and migration, and binds other molecules including
Vitronectin, Nectin-3, DNAM-1/CD226, CD96, and TIGIT but does not bind homophilicly
(3, 4). The mature human CD155 consists of a 323 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 50 aa cytoplasmic tail.
The
sequence of the cynomolgus
CD155/PVR was
isolated from a cynomolgus monkey cDNA library and aligns with the sequence for
Macaca nemestrina (XP_011734201.1 aa24-339,
T77M, V93T, G223S, R328G). 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, 5-8). It is
preferentially expressed on Th17 cells compared to Th2 cells (9), and its
activation promotes the development of Th1 responses (10). On migrating cells, CD155
is concentrated at the leading edge, where it binds basement membrane
Vitronectin, recruits Nectin-3-expressing cells, and cooperates with PDGF and
Integrin alpha v beta 3 to promote cell migration
(1, 3, 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, 6, 12). Binding of monocyte DNAM‑1 to endothelial cell CD155
promotes transendothelial migration (7).
- 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.
- 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.
- Mueller, S. and E. Wimmer (2003) J. Biol. Chem. 278:31251.
- Chan, C.J. et al. (2010) J. Immunol. 184:902.
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