CD11b is a heterodimeric integral membrane protein belonging to major surface antigen family on human leukocytes. It not only promotes several adhesive interactions of granulocytes, macrophages and monocytes, to each other and to stimulated endothelial cell monolayers, but also helps in the phagocytosis of complement coated particles. CD11b is known to act as a marker to discriminate between naive and memory CD8+ T cells in virus infection. It plays a role in inflammation in neointimal thickening, leukocyte recruitment to mechanically injured arteries, and osteoclast differentiation. Reports suggest that along with CD14 and Toll-like receptor (TLR) 4, CD11b may help in LPS recognition and thus may act as signaling receptors in murine macrophages. Susceptibility to systemic lupus erythematosus (SLE), a chronic, inflammatory and often febrile multisystemic disorder of connective tissue, is due to genetic aberrations in CD11b. The ICRF44 monoclonal antibody specifically reacts with the 165 kDa human adhesion glycoprotein CD11b, which forms, together with the 95 kDa CD18 (integrin β2) a complex known as Mac-1. CD11b is expressed on the surface of activated lymphocytes, a subset of natural killer cells, granulocytes, and monocytes. It functions as a receptor in cell-cell and cell-matrix interactions.
In 50% Glycerol/PBS with 1% BSA and 0.09% sodium azide