Recombinant full-length human MYLK2 was expressed by baculovirus in Sf9 insect cells using an N-terminal His tag. MYLK2 is a member of the myosin light chain kinase family and is a calcium/calmodulin dependent enzyme that is exclusively expressed in adult skeletal muscle. MYLK2 has been proposed to participate in signaling pathways (calcium signaling pathway, focal adhesion, regulation of actin cytoskeleton) and cellular processes (neuromuscular synaptic transmission, protein/amino acid phosphorylation). MYLK2 is involved in multiple molecular functions as a result of various subdomains that participate in ATP binding, calmodulin binding, nucleotide binding, protein serine/threonine kinase activity and transferase activity). ADP-Glo Kinase Assay is a luminescent kinase assay that measures ADP formed from a kinase reaction; ADP is converted into ATP, which is a substrate in a reaction catalyzed by Ultra-Glo Luciferase that produces light. The luminescent signal positively correlates with ADP amount and kinase activity. The assay is well suited for measuring the effects chemical compounds have on the activity of a broad range of purified kinases, making it ideal for both primary screening as well as kinase selectivity profiling. The ADP-Glo Kinase Assay can be used to monitor the activity of virtually any ADP-generating enzyme (e.g., kinase or ATPase) using up to 1mM ATP.