Optimized DNA sequence encoding extracellular domain of human CD155 including a C-terminal Fc tag was expressed in HEK293 cells.
Recombinant CD155 is a homodimer protein consisting of 561 amino acid residue subunits, due to glycosylation migrates as an approximately 55-60 kDa protein on SDS-PAGE.
>95%, as determined by SDS-PAGE and HPLC
The biological activity of Human PVR was measured by the binding ability of immobilized recombinant Human CD155 (2 μg/ml ,100 μl/well ) to human DNAM1 (linear range of 0.03 - 0.8 ng/ml) in a functional ELISA assay.
Endotoxin content was assayed using a LAL gel clot method.
Endotoxin level was found to be less than 0.1 ng/µg(1EU/µg).
Recombinant CD155 is supplied as a 0.2 μm filtered PBS solution, pH7.2 .
Recombinant CD155, as supplied, can be stored in working aliquots at 2° - 8° C for one month, or at -20°C to -70°C for twelve months.
Avoid repeated freeze/thaw cycles.
This product is for research purposes only. It may not be used for therapeutics or diagnostic purposes.
hPVR(CD155) is a member of
the immunoglobulin (Ig)
superfamily, with three
linked extracellular Ig-like
domains followed by a
membrane-spanning domain and
a cytoplasmic domain.
Although a physiological
function for CD155 is
the protein binds
specifically to the
matrix component vitronectin
(Lange et al., 2001).
of the CD155 gene is tightly
dnam-1/CD155 interactions promote cytokine and nk cell-mediated suppression of poorly immunogenic melanoma metastases
902 - 911.
primary human tumor cells expressing CD155 impair tumor targeting by down-regulating dnam-1 on nk cells
4921 - 4930.
cd96 interaction with CD155 via its first ig-like domain is modulated by alternative splicing or mutations in distal ig-like domains
J. Biol. Chem.,
2235 - 2244.
crystal structure of CD155 and electron microscopic studies of its complexes with polioviruses
18284 - 18289.
characterization of the new world monkey homologues of human poliovirus receptor CD155 J. Virol.,
7167 - 7179.