Anti-human CD2 Monoclonal Antibody Unconjugated, Flow Validated

CD2 (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 CD2 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 portionThe localization of CD2 to 1p13 was established by in situ hybridization. By Southern blotting of DNA from a panel of somatic cell hybrids, Clayton et al. (1988) assigned the CD2 gene to human chromosome 1 and murine chromosome 3.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 CD2 gene.

CD2 interacts with lymphocyte function-associated antigen (LFA-3) and CD48/BCM1 to mediate adhesion between T-cells and other cell types. CD2 is implicated in the triggering of T- cells, the cytoplasmic domain is implicated in the signaling function.