Transglutaminase (TG) is a thiolase that induces intermolecular cross-linking of proteins, by catalysing the formation of isopeptide bonds between the γ-carboxamide group of glutamine residues and the primary ε-amine group of other compounds.

(Trp63,Trp64)?-?C3a(63-77) is a C3a synthetic analogue peptide, which exhibits Ca2+ stimulating efficacy in human neutrophils and hC3aR or mC3aR expressing RBL-2H3 cells with EC50 of 9.5, 2.0 and 0.8 nM, respectively.

A cell-permeable synthetic peptide NEMO-binding domain peptide (NBD peptide) corresponding to the NEMO amino-terminal alpha-helical region is shown to block TNF-alpha-induced NF-kB activation. The interaction of IKγNEMO with the IKK complex is vital for the activation of the IKK complex and the subsequent activation of NF-kB.