The RMV-7 monoclonal antibody specifically binds to CD51, the 140 kDa integrin αV chain. Heterodimers of CD51 with several integrin β chains function as receptors for extracellular matrix proteins. CD51/CD61 (αVβ3 integrin, vitronectin receptor) mediates adhesion to fibronectin, fibrinogen, vitronectin, thrombospondin, von Willebrand factor, and CD31 (PECAM-1). CD51 is expressed on activated T lymphocytes, polymorphonuclear granulocytes, blastocysts, and osteoclasts. CD51 is reportedly not detectable on mouse platelets using either H9.2B8 or RMV-7 antibody clones. CD51 also forms heterodimers with CD29 (integrin β1), integrins β5, β6, and β8 chains. αV integrins have diverse functions in development and homeostasis. The RMV-7 antibody reportedly blocks LAK-cell binding to vitronectin, fibronectin, fibrinogen, and CD31. Furthermore, the RMV-7 antibody reportedly inhibits LAK-cell cytoxicity against certain target cells by interfering with the binding of LAK cells to their target cells.