Human CD2 is also referred as LFA-2 (leukocyte function-associated antigen-2), which belongs to the immunoglobulin supergene family. CD2 is a monomeric transmembrane glycoprotein with a weight of 45–50 kDa and binds CD58, CD48, or CD59. It consists of two extracellular Ig-like domains (one V-like and one C-like) and a proline-rich cytoplasmic tail. CD2 is commonly expressed on most mature peripheral T cells, NK-cells, and a subset of thymic B-cells during human thymocyte development. CD2 is crucial in T-cell activation, T- or NK-mediated cytolysis, apoptosis in activated peripheral T-cells, and the production of cytokines by T-cells. CD2 is an excellent pan-T-cell marker. The low expression level of CD2 is thought to associated with some of the T-lymphoid malignancies, particularly peripheral T-cell lymphomas. MUC1 (Mucin 1, cell surface associated), also referred to tumor-associated epithelial membrane antigen, EMA, MCD or CD227, is a 122 kDa single-pass type I transmembrane protein mapping at the chromosome 1q22. It is generally expressed on glandular or luminal epithelial cells of the mammary gland, stomach, esophagus, duodenum, pancreas, prostate, uterus, and lungs, and lesser in hematopoietic cells, but absent in the skin epithelium and mesenchymal cells. MUC1 gene coding for a membrane-bound protein, a member of the mucin family, is an O-glycosylated protein that functions in forming protective mucous barriers on epithelial cell surfaces. And they also play a part in intracellular signaling. Abnormally glycosylated MUC1 is overexpressed in most human epithelial cancer cells and has been regarded as an oncogenic molecule.