Cayman Pvrcd155 Extracellular Domain (Human, Recombinant), 100

Poliovirus receptor (PVR), also known as CD155, is a member of the nectin-like family of adhesion molecules encoded by the PVR gene in humans that regulates cell migration and proliferation and immune cell activation. It contains an N-terminal extracellular domain with three immunoglobulin-like (Ig-like) loops, C1-like and C2 domains that mediate dimerization, a transmembrane segment that acts as a ligand for receptors expressed by immune cells, and a C-terminal cytoplasmic tail that interacts with intracellular scaffold proteins.^, PVR is highly expressed by enterocytes and gastrointestinal lymphatic tissues. It localizes to the cell surface where it forms cis-homodimers that associate by trans-interactions with nectin-3 cis-homodimers expressed on adjacent cells, resulting in cell-cell adhesion. PVR internalization by endocytosis disrupts PDGFR and integrin αVβ3 signaling, inducing contact inhibition of cell movement and proliferation.^, PVR binds the co-stimulatory receptor CD226/DNAM-1 (Item Nos. | ), which is widely expressed by most immune cells, including T cells, B cells, natural killer (NK) cells, and monocytes, and the inhibitory receptors TIGIT (Item No. ) and CD96, which are expressed by NK cells and T cells, inducing activation or inhibition of immune cells in a receptor-specific manner. It is also the receptor for poliovirus attachment and entry into cells. In cancer cells, PVR expression is upregulated by FGF stimulation or expression of the oncogene Ras and downregulated by the unfolded protein response. Caymans PVR/CD155 Extracellular Domain (human, recombinant) protein can be used for binding assay applications. This protein is a disulfide-linked homodimer. The reduced monomer, comprised of PVR (amino acids 21-345) fused to human IgG1 Fc at its C-terminus, consists of 561 amino acids, has a calculated molecular weight of 61.8 kDa, and a predicted N-terminus of Trp21 after signal peptide cleavage. As a result of glycosylation, the monomer migrates at approximately 95 to 105 kDa by SDS-PAGE under reducing conditions.

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