Enzyme was purified from cell extracts by CaM-sepharose.

CaMKII is autophosphorylated.

Interaction in vitro; enzyme derived from transfected COS cell extract.

CaMKII was purified from cell extracts by CaM-sepharose. Purified protein was subjected to gel filtration and its fractionation was monitored via its enzyme activity.

CaMKII exists as oligomers with a molecular mass of about 390-460 kDa.

Interaction in vitro; protein derived from transfected COS cell extract.

CaMKII was purified from cell extracts by CaM-sepharose. Purified protein was subjected to gel filtration and its fractionation was monitored via its enzyme activity.

CaMKII exists as oligomers with a sedimentation coefficient of about 19.0-20.2S

Interaction in vitro; protein derived from transfected COS cell extract.

Enzyme was purified from cell extracts by CaM-sepharose.

CaMKII is autophosphorylated.

Interaction in vitro; enzyme derived from transfected COS cell extract.

The kinase reaction when performed with CaMKII bound to immobilized eag does not require Ca2+ however, the presence of Ca2+ enhances measured kinase activity.

Interaction in vitro; enzyme produced as a recombinant fusion protein in baculovirus and Sf21 cell system.