CD68 is a Type I transmembrane glycoprotein with a heavily glycosylated extracellular domain . The primary sequence of human CD68 consists of 354 amino acids, with a predicted molecular weight of 37.4 kD if it were not glycosylated . The extracellular domain contains 9 potential N-linked glycosylation sites and numerous potential O-linked glycosylation sites . This domain is divided into two distinct regions separated by an extended proline hinge: a distal mucin-like domain and a proximal domain with significant sequence homology to a family of lysosomal/plasma membrane shuttling proteins .
CD68 is a member of the LAMP (lysosome-associated membrane glycoprotein) family, which includes other proteins such as LAMP1 . It is also functionally and evolutionarily related to other hematopoietic mucin-like molecules, including leukosialin/CD43 and stem cell antigen CD34 .
CD68 is primarily localized to lysosomes and endosomes, with a smaller fraction circulating to the cell surface . It is highly expressed by human monocytes and tissue macrophages . The protein plays a crucial role in the clearance of cellular debris, promotion of phagocytosis, and recruitment and activation of macrophages .
CD68 is widely used as a marker for various cells of the macrophage lineage, including monocytes, histiocytes, giant cells, Kupffer cells, and osteoclasts . Immunohistochemistry can identify the presence of CD68 in the cytoplasmic granules of a range of different blood cells and myocytes . This makes it particularly useful in distinguishing diseases of otherwise similar appearance, such as the monocyte/macrophage and lymphoid forms of leukemia .