CaM Kinase II α is a Ca2+/calmodulin-dependent kinase that belongs to the serine/threonine protein kinases family. It facilitates the regulation of NMDAR-dependent AMPA receptor trafficking to the synapses. Mouse anti-CaM kinase II α antibody reacts specifically with phosphorylated and non-phosphorylated forms of native and recombinant CaM (Ca2+/calmodulin-dependent) kinase II α subunit in rats. The product has shown no reactivity for phosphorylated or non-phosphorylated β subunit (60kD).
CaMKII is involved in many cellular functions in response to Ca2+ signaling, including synthesis and secretion of neurotransmitters, axonal transport, long term potentiation (LTP) and spatial learning, receptor function and regulation of gene expression. CaMKII plays a critical role in LTP, a cellular model of learning and memory. In the CNS, postsynaptic Ca2+ influx triggers rapid autophosphorylation and stable activation of CaMKII in a Ca2+/calmodulin dependent manner at a threonine residue in the autoinhibitory domain. Autophosphorylation of CaMKIIα at Thr286 has been shown to be required for LTP and learning.
