Clone REA434 recognizes the human proto-oncogene tyrosine-protein kinase Src phosphorylated at tyrosine 418 (pY418). Src is a non-receptor protein tyrosine kinase which is activated following engagement of many different classes of cellular receptors including immune response receptors, integrins, and other adhesion receptors, receptor protein tyrosine kinases, G protein-coupled receptors, as well as cytokine receptors. It participates in signaling pathways that control a diverse spectrum of biological activities including gene transcription, immune response, cell adhesion, cell cycle progression, apoptosis, migration, and transformation. Src appears to be one of the primary kinases activated following engagement of receptors and plays a role in the activation of other protein tyrosine kinase families. Receptor clustering or dimerization leads to recruitment of SRC to the receptor complexes where it phosphorylates the tyrosine residues within the receptor cytoplasmic domains. Src activity is regulated by phosphorylation at key sites, including the autophosphorylation site pY418 and the inhibitory site pY529.

Additional information: Clone REA434 displays negligible binding to Fc receptors.