
New Monoclonal Antibodies Target C5a Receptor Phosphorylation

Scientists at the Georg-August-University Göttingen produced different monoclonal antibodies directed against phosphorylation sites of C5aR. Using these antibodies the activation state of C5aR can be directly measured in tissue or cultured cells.
Since the relevant epitope is known to be phosphorylated by Protein Kinase C (PKC), this principle can also be used to measure PKC activity or to screen for new PKC inhibitors. CD88 is expressed by peripherial blood granulocytes and monocytes. Binding of C5a (fragment of the complement factor C5) to CD88 leads to cellular activation, including chemotaxis.
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