Clone REA1195 recognizes the human CD112 antigen, a Single-pass type I membrane protein which is also known as Nectin-2, Herpesvirus entry mediator B (HveB) or Poliovirus receptor-related protein 2 (PRR2). Nectins are Ca2+-independent cell adhesion molecules that consist of 4 members: CD111 (Nectin-1), CD112 (Nectin-2), CD113 (Nectin-3), and Nectin-4. CD112 is one of the plasma membrane components of adherens junctions and is widely expressed in human tissues, including hematopoietic cells. It is also over-expressed in various cancers, e.g. breast and ovarian cancers. It has been reported to regulate cell adhesion between epithelial cells through the formation of trans-dimers between adjacent cells. CD112-mediated cell adhesion induces the formation of E-cadherin-based adherens junctions followed by the formation of claudin-based tight junctions. In addition to its function as a cell adhesion molecule, previous studies have suggested that CD112 acts as an organizer of Sertoli cell-spermatid junctions in the testis and of synapse formation by neurons and as an entry receptor for viruses. CD112 is also known to be one of the ligands of CD226 (DNAM-1) and TIGIT.
Additional information: Clone REA1195 displays negligible binding to Fc receptors.