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The rat anti-mouse CD51 (clone RMV-7) antibody reacts with the 140kDa 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). It has been reported to be expressed on activated T lymphocytes, polymorphonuclear granulocytes, blastocysts, and osteoclasts. CD51 has reportedly been found to be undetectable on mouse platelets using either antibody clones H9.2B8 or RMV-7. CD51 also forms heterodimers with CD29 (integrin β1), integrins β5, β6, and β8 chains. αV integrins have diverse functions in development and homeostasis. The rat anti-mouse (clone RMV-7) mAb has been reported to block LAK-cell binding to vitronectin, fibronectin, fibrinogen, and CD31. Furthermore, the RMV-7 clone reportedly inhibits LAK-cell cytoxicity against certain target cells by interfering with the binding of LAK cells to their target cells. This antibody has been tested by LAL assay for endotoxin level and is routinely tested by flow cytometric analysis. Other applications were tested at BD Biosciences Pharmingen during antibody development only or reported in the literature.
