{"type":"root","children":[{"type":"paragraph","children":[{"type":"text","value":"CD57 antigen (HNK-1, LEU-7, or L2) is a 100-115 kDa terminally sulfated carbohydrate epitope that was originally reported as a marker of human natural killer cells. CD57 has been shown to be present on both CD4 and CD8 T-cells in the late stages of differentiation. CD57 was originally detected by immunoblot/immunohistochemical analysis of cell adhesion glycoproteins in the human nervous system, including the binding partners neural cell adhesion molecule, myelin-associated glycoprotein, 5′-nucleotidase, ICAM5, NCAM, integrins, cytotactin, TAG-1, MAG, PMP-22, contactin, L1, P0 and telencephalin, as well as on chondroitin sulfate proteoglycans and glycolipids such as sulfoglucuronylglycolipid-1 and sulfoglucuronylglycolipid-2. CD57 is now also known to act as a ligand for laminin, L-selectin, and P-selectin, as well as for the cerebellar adhesion protein amphoterin. These observations suggest that CD57 is associated with cell–cell and/or cell–matrix interactions."}]}]}