CD2, also known as Cluster of Differentiation 2, is a cell adhesion molecule found on the surface of T cells and natural killer (NK) cells. It plays a crucial role in the immune response by facilitating cell-cell interactions and signaling. The recombinant form of CD2, tagged with Glutathione S-Transferase (GST), is widely used in research for various applications, including protein purification and interaction studies.
CD2 is a transmembrane glycoprotein that belongs to the immunoglobulin superfamily. It is primarily expressed on T cells, NK cells, and thymocytes. The molecule consists of an extracellular domain, a single transmembrane region, and a cytoplasmic tail. The extracellular domain of CD2 interacts with other adhesion molecules, such as CD58 (LFA-3) in humans, to mediate cell-cell adhesion .
In addition to its adhesive properties, CD2 acts as a co-stimulatory molecule, enhancing the activation and proliferation of T cells and NK cells. This co-stimulatory function is essential for the effective immune response against pathogens .
The GST tag is a widely used protein tag for the purification and detection of recombinant proteins. GST, or Glutathione S-Transferase, is an enzyme that binds to glutathione, a tripeptide. The GST tag is typically fused to the N-terminus of the protein of interest, promoting its expression and solubility .
The primary advantages of using a GST tag include:
The recombinant CD2 protein tagged with GST is utilized in several research areas: