Intracellular Calcium (Ca2+) acts as major secondary messenger that mediates signalling induced by hormones and neurotransmitters. Cellular responses to calcium are modulated by a family of Ca2+/Calmodulin dependent protein kinases. The members of this family include CaMK I, CAMK II and CAMK IV. These kinases mediate rapid, highly specific and reversible post-translational modification involving ATP. CaMK II is abundantly expressed in mammalian brain, with highest expression in neurons of hippocampus and cerebral cortex, and plays critical role in synaptic transmission, memory, learning and behaviour. CaMK II family has four members, CaMK IIα, CaMK IIβ, CaMK IIγ and CaMK IIδ. The CaMK IIα?and β?isoforms are predominantly expressed in the brain, localized mainly in the cytosol and postsynaptic densities (PSDs), whereas the CaMK IIγ and δ isoforms are expressed in all tissues. CaMK II is autophosphorylated at α-Thr286 residue in response to changes in the concentration of intracellular calcium. This may prolong physiological responses to temporary changes in Ca2+ concentrations. CaMK II regulates synaptic signalling by phosphorylating glutamate receptors in the neurons. A distinct CaMK II has also been implicated in the process of smooth muscle contraction by phosphorylation of myosin light chain kinase.
This product reacts with the recombinant and native rat phosphorylated CaMK II α subunit only (50 kDa). It does not cross-react with the non-phosphorylated α subunit or with the 60 kDa β subunit in either phosphorylation state.
