Myristoylated AIP CaMKII Inhibitor

Myristoylated AIP is a cell-associated form of the Autocamtide-2-Related Inhibitory Peptide, a potent substrate-competitive inhibitor of Ca2+/calmodulin-dependent protein kinase II (CaMKII). AIP is derived from Autocamtide-2 with the phosphorylation-site threonine replaced by alanine, converting the substrate motif into a nonphosphorylatable inhibitory sequence. N-terminal myristoylation increases hydrophobicity and is commonly used to enhance cellular association or uptake.

• CaMKII inhibition studies
• Ca2+/calmodulin signaling research
• phospholamban phosphorylation studies
• cell-associated kinase inhibition

This is an inhibitor, not a kinase substrate. Myristoylation materially changes solubility and membrane association; appropriate vehicle and scrambled or inactive controls are recommended for cellular experiments.

1. Targeted Inhibition of Ca2+/Calmodulin-dependent Protein Kinase II in Cardiac Longitudinal Sarcoplasmic Reticulum Results in Decreased Phospholamban Phosphorylation at Threonine 17
2. Stabilization of Calmodulin-dependent Protein Kinase II through the Autoinhibitory Domain