CD2 Human

CD2 is a single-pass type I membrane protein that contains one Ig-like C2-type (immunoglobulin-like) domain and one Ig-like V-type (immunoglobulin-like) domain . The extracellular domain of CD2 is responsible for its interactions with other cell surface molecules. The recombinant human CD2 protein is typically expressed in HEK293 cells and carries a polyhistidine tag at the C-terminus for purification purposes .

CD2 functions as an adhesion molecule and is involved in the activation and differentiation of T cells and NK cells. It interacts with other adhesion molecules such as lymphocyte function-associated antigen-3 (LFA-3/CD58) in humans, or CD48 in rodents . These interactions are critical for the formation of the immunological synapse, which is essential for effective immune responses.

Recombinant human CD2 proteins are produced using recombinant DNA technology. These proteins are used in various research applications, including studies on T cell activation, immune cell interactions, and the development of immunotherapies. The recombinant CD2 protein is often purified using affinity chromatography and is available in lyophilized form for long-term storage .

Recombinant CD2 proteins are valuable tools in immunological research. They are used in functional assays to study the binding interactions between CD2 and its ligands, such as CD58. These studies help in understanding the molecular mechanisms underlying T cell activation and immune responses. Additionally, recombinant CD2 proteins are used in the development of therapeutic antibodies and other immunotherapeutic agents .