Human PVRIG Antibody Summary
Thr 41 & Glu43-Leu172
Accession # Q6DK17
Please Note: Optimal dilutions should be determined by each laboratory for each application. General Protocols are available in the Technical Information section on our website.
Detection of PVRIG in HEK293 Human Cell Line Transfected with Human PVRIG and eGFP by Flow Cytometry. HEK293 human embryonic kidney cell line transfected with either (A) human PVRIG or (B) irrelevant protein and eGFP was stained with Rabbit Anti-Human PVRIG Monoclonal Antibody (Catalog # MAB93651) followed by APC-conjugated Goat anti-Rabbit IgG Secondary Antibody (Catalog # F0111). Quadrant markers were set based on Rabbit IgG control antibody staining (Catalog # MAB1050, data not shown). View our protocol for Staining Membrane-associated Proteins.
Preparation and Storage
- 12 months from date of receipt, -20 to -70 °C as supplied.
- 1 month, 2 to 8 °C under sterile conditions after reconstitution.
- 6 months, -20 to -70 °C under sterile conditions after reconstitution.
Human PVRIG (poliovirus receptor related immunoglobulin domain-containing protein), also known as CD112 receptor (CD112R), is an approximately 34 kDa single transmembrane protein in the poliovirus receptor-like protein (PVR) family (1). It is composed of a single extracellular IgV domain, one transmembrane domain, and a long intracellular domain. The intracellular domain contains two tyrosine residues, one within an ITIM-like motif that is a potential docking site for phosphatases (1). The extracellular domain sequence of human and mouse PVRIG have approximately 65% similarity. The human PVRIG gene is preferentially expressed in lymphocytes, such as T cells and NK cells, but not in monocyte derived dendritic cells (1). PVRIG functions as a cell surface receptor for Nectin-2/CD112, a cell surface protein that is widely expressed on antigen-presenting cells and tumor cells. Disrupting the PVRIG/Nectin-2 interaction enhances human T cell response, suggesting PVRIG is a novel checkpoint for human T cells (1).
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