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. CD2 is one of the earliest T-cell markers, being present on more than 95% of thymocytes. Due to its structural characteristics, CD2 is a member of the immunoglobulin superfamily; it possesses two immunoglobulin-like domains in its extracellular portion. The localization of CD2 to 1p13 is established by in situ hybridization. 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 is identified within the 3-prime flanking region of the human CD2 gene.

Optimal dilution of the anti-Cd2 antibody should be determined by the researcher.

Amino acids R23-S203 of the mouse protein were used as the immunogen for the anti-Cd2 antibody.

After reconstitution, the anti-Cd2 antibody can be stored for up to one month at 4oC. For long-term, aliquot and store at -20oC. Avoid repeated freezing and thawing.