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Rat CD155 Recombinant


accession:  Q5U334
   Size A     20ug   $ 160
   Size B      100ug  $480
   Size C      500ug  $ 1650
Domain  :  Ig-like C2
Gene  :  CD155
Catalog no. :  RKQ5U334

Optimized DNA sequence  encoding  extracellular domain of rat PVR (CD155) including a C-terminal 6His tag was expressed in HEK293 cells.

Molecular weight:

Recombinant rat PVR (CD155) is a monomer protein consisting of 329 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

Biological Activity:
The biological activity of rat PVR was measured by the binding ability of immobilized recombinant rat CD155 (20 μg/ml ,100 μl/well ) to mouse CD226 (linear ranger of 6 - 200 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 rat CD155 is supplied as a 0.2 μm filtered PBS solution,  pH7.2 .

Recombinant rat PVR (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 unknown, the protein binds specifically to the extracellular matrix component vitronectin (Lange et al., 2001). Transcriptional regulation of the CD155 gene is tightly controlled.

Related Publications:
dnam-1/CD155 interactions promote cytokine and nk cell-mediated suppression of poorly immunogenic melanoma metastases
J. Immunol., Jan 2010; 184: 902 - 911.
primary human tumor cells expressing CD155 impair tumor targeting by down-regulating dnam-1 on nk cells
J. Immunol., Oct 2009; 183: 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., Jan 2009; 284: 2235 - 2244.
crystal structure of CD155 and electron microscopic studies of its complexes with polioviruses
PNAS, Nov 2008; 105: 18284 - 18289.
characterization of the new world monkey homologues of human poliovirus receptor CD155
J. Virol., Jul 2008; 82: 7167 - 7179.

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Purified Polyclonal
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