CD11b is a cell adhesion molecule that acts as a receptor for cell surface ligands such as intracellular adhesion molecules (ICAMs) or soluble ligands. Integrins are heterodimeric proteins that contain an alpha chain and beta chain. IntegrinαM combines with the Integrinβ2 to form a leukocyte-specific integrin referred to as macrophage receptor 1 (Mac-1), or inactivated-C3b (iC3b) receptor 3 (CR3). IntegrinαM/β2 is important in the adherence of neutrophils and monocytes to stimulated endothelium, and also in the phagocytosis of complement coated particles. The protein CD11b has been implicated in the various adhesion-related interactions of cells such as monocytes, macrophages, natural killer (NK) cells, and granulocytes. It is part of a heterodimer that consists of CD11b and CD18. It also modulates the uptake of complement-coated particles within the cell. It is commonly used as a microglial marker in tissues derived from the nervous system.Primary antib