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Human CellExp™ CD155, human recombinant

Establishes intercellular adherens junctions between epithelial cells
Catalog #: 7462
SKU-Size Size Price Qty
7462-10 10 μg
$180.00
7462-50 50 μg
$595.00
More Sizes Get Quote

Product Details

Alternate Name PVR, FLJ25946, PVS, CD155, TAGE4, HVED, NECL5, cluster of differentiation 155.
Gene Symbol PVR
Gene ID 5817
Accession # P15151
Source HEK293 cells
Appearance Lyophilized
Physical Form Description Lyophilized from 0.22 μm filtered solution in PBS, pH 7.4. Normally Mannitol or Trehalose is added as protectants before lyophilization.
Molecular Weight This protein is fused with a C-terminal 6×his tag and has a calculated MW of 28 kDa. The predicted N-terminus is Trp21. DTT-reduced protein migrates as 50-65 kDa polypeptide in SDS-PAGE resulting from glycosylation.
Purity by SDS-PAGE ≥95%
Endotoxin Level <1 EU/μg by LAL method
Biological Activity Measured by its ability to bind with recombinant human DNAM1 / CD226 in a functional ELISA assay
Reconstitution Instructions Centrifuge the vial prior to opening. Reconstitute in sterile PBS, pH 7.4 to a concentration of 50 µg/ml. Do not vortex. This solution can be stored at 2-8°C for up to 1 month. For extended storage, it is recommended to store at -20°C.
Handling Centrifuge the vial prior to opening.
Storage Conditions -20°C
Shipping Conditions Gel Pack
USAGE For Research Use Only! Not to be used in humans

Details

CD155 is a Type I transmembrane glycoprotein in the immunoglobulin superfamily. Commonly known as Poliovirus Receptor (PVR) due to its involvement in the cellular poliovirus infection in primates, CD155's normal cellular function is in the establishment of intercellular adherens junctions between epithelial cells. CD155/PVR was originally isolated based on its ability to mediate polio virus attachment to host cells. The full length (or CD155 alpha isoform) is synthesized as a 417 amino acid (aa) precursor that contains a 20 aa signal sequence, a 323 aa extracellular region, a 24 aa ™ segment and a 50 aa cytoplasmic tail. The extracellular region contains one N terminal V type and two C2 type Ig like domains. It has 3 extracellular immunoglobulin-like domains, D1-D3, where D1 is recognized by the virus. Low resolution structures of CD155 complexed with poliovirus have been obtained using electron microscopy[1] while a high resolution structures of the ectodomain D1 and D2 of CD155 were solved by x-ray crystallography.


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