CD155 Recombinant Protein Cat. No.: 96-840

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psi-iconSpecifications
SPECIES:Human
SOURCE SPECIES:HEK293 cells
SEQUENCE:Trp 21 - Asn 343
FUSION TAG:Fc Tag
TESTED APPLICATIONS:ELISA, WB
APPLICATIONS:This recombinant protein can be used for E, WB. For research use only.
BIOLOGICAL ACTIVITY: Measured by its binding ability in a functional ELISA. Immobilized Human CD155, Fc Tag at 10 ug/mL (100 uL/well) can bind Biotinylated Human TIGIT, His Tag with a linear range of 0.08-0.31 ug/mL (QC tested).
psi-iconProperties
PURITY:>95% as determined by SDS-PAGE.

Endotoxin level is less than 1.0 EU per ug by the LAL method.
PREDICTED MOLECULAR WEIGHT:61.7 kDa
PHYSICAL STATE:Lyophilized
BUFFER:Tris with Glycine, Arginine and NaCl, pH7.5
STORAGE CONDITIONS:Lyophilized Protein should be stored at -20˚C or lower for long term storage. Upon reconstitution, working aliquots should be stored at -20˚C or -70˚C. Avoid repeated freeze-thaw cycles.
psi-iconAdditional Info
ALTERNATE NAMES:PVR,FLJ25946,PVS,CD155,TAGE4,HVED,NECL5
ACCESSION NO.:AAH15542
OFFICIAL SYMBOL:CD155
GENE ID:5817
psi-iconBackground and References
BACKGROUND: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 fulllength (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 TM segment and a 50 aa cytoplasmic tail. The extracellular region contains one N terminal V type and two C2 type Ig like domains. CD155 is a transmembrane protein with 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 while a high resolution structures of theectodomain D1 and D2 of CD155 were solved by x-ray crystallography.
REFERENCES:1) Mendelsohn CL, Wimmer E, Racaniello VR, 1989, Cell 56 (5): 855–65 .
2) Maier MK, Seth S, Czeloth N, et al., 2007, European Journal of Immunology 37 (8): 2214.
3) Koike, H. et al., 1990, EMBO J. 9:3217.
4) Zhang P, Mueller S, Morais MC. Proc. Natl. Acad. Sci. U.S.A. 105 (47): 18284–9.

FOR RESEARCH USE ONLY.

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