Cd111CD103

Cd111CD103, also known as Integrin alphaX beta2, is a cell surface glycoprotein that plays a role in immune cell adhesion and signaling. It is a member of the integrin family, which are heterodimeric transmembrane receptors composed of alpha and beta subunits. Cd111CD103 specifically is formed by the alphaX (CD11c) and beta2 (CD18) subunits.

This integrin is primarily expressed on myeloid cells, including monocytes, macrophages, dendritic cells, and granulocytes. Its expression levels can vary depending on the cell type and activation state. Cd111CD103 is involved in mediating interactions between immune cells and other cells, as well as the extracellular matrix.

One of the key ligands for Cd111CD103 is complement receptor 3 (CR3)-binding protein, and it also binds to ICAMs (Intercellular Adhesion Molecules). This interaction is important for various immune functions such as leukocyte recruitment to sites of inflammation, phagocytosis of complement-opsonized particles, and cell-cell adhesion. Research has indicated its involvement in processes like immune surveillance, antigen presentation, and T cell activation. Dysregulation of Cd111CD103 expression or function has been implicated in certain inflammatory and autoimmune diseases, highlighting its significance in immune homeostasis.