Human CellExp CD155, human recombinant protein
PVR, FLJ25946, PVS, CD155, TAGE4, HVED, NECL5, cluster of differentiation 155.
|Calculated MW||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.|
|Other Names||PVR, FLJ25946, PVS, CD155, TAGE4, HVED, NECL5, cluster of differentiation 155.|
|Results||Measured by its ability to bind with recombinant human DNAM1 / CD226 in a functional ELISA assay|
|Application Notes||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.|
|Storage||-20°C; Lyophilized from 0.22 µm filtered solution in PBS, pH 7.4. Normally Mannitol or Trehalose is added as protectants before lyophilization.|
firstname.lastname@example.org, and receive a free "I Love Antibodies" mug.
Provided below are standard protocols that you may find useful for product applications.
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 TM 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 while a high resolution structures of the ectodomain D1 and D2 of CD155 were solved by x-ray crystallography.
Mendelsohn C.L.,et al.Cell 56:855-865(1989).
Racaniello V.R.,et al.Submitted (JUL-1995) to the EMBL/GenBank/DDBJ databases.
Koike S.,et al.EMBO J. 9:3217-3224(1990).
Ota T.,et al.Nat. Genet. 36:40-45(2004).
Grimwood J.,et al.Nature 428:529-535(2004).
If you have any additional inquiries please email technical services at email@example.com.