CD2 Antibody

Cluster of differentiation 2 is a cell adhesion molecule found on the surface of T cells and natural killer (NK) cells. It has also been called T-cell surface antigen T11/Leu-5, LFA-2, LFA-3 receptor, erythrocyte receptor and rosette receptor. Monoclonal antibodies directed against CD2 inhibit the formation of rosettes with sheep erythrocytes, indicating that the protein is the erythrocyte receptor or is closely associated with it. It is one of the earliest T-cell markers, being present on more than 95% of thymocytes; it is also found on some natural killer cells but not on B lymphocytes. Due to its structural characteristics, CD2 is a member of the immunoglobulin superfamily; it possesses two immunoglobulin-like domains in its extracellular portion. CD2 interacts with other adhesion molecules, such as lymphocyte function-associated antigen-3 (LFA-3/CD58) in humans, or CD48 in rodents, which are expressed on the surfaces of other cells. With the use of transgenic mice, such an LCR was identified within the 3-prime flanking region of the human gene.