CaMKII

Detects ~50-60kDa protein corresponding to the apparent molecular mass of CaMKII & alpha; - subunit on SDS-PAGE immunblots. Both the phosphorylated and nonphosphorylated forms are recognized.

1. 0mg/mL; 0. 1ug/ml of SMC124 was needed for detection of CaMKII in 20 ug of rat brain tissue. 0. 1ug/ml was needed for detection of CaMKII in 20 ug of rat brain tissue extract by colorimetric immunoblot analysis using goat anti-mouse IgG:AP as the secondary antibody. Storage and stability: -20& deg; C; 1 year+ CaMKII is an important member of calcium/calmodulinactivated protein kinase family functioning in neural synaptic stimulation and T-cell receptor signaling. CaMKII is expressed in many different tissues but is specifically found in the neurons of the forebrain and its mRNA is found within the dendrites and the soma of the neuron. The CaMKII that is found in the neurons consist of two subunits of 52 (termed alpha genes) and 60 kDa (beta genes). CaMKII has catalytic and regulatory domains as well as an ATP-binding domain and a consensus phosphorylation site . The binding of Ca 2+ /calmodulin to its regulatory domain releases its auto inhibitory effect and activates the kinase. This kinase activation results in autophosphorylation at threonine 286. The threonine phosphorylation state of CaMKII can be regulated through PP1/PKA. Whereas PP1 (protein phosphatase 1) dephosphorylates phospho-CaMKII at Thr286 PKA (protein kinase A) prevents this dephosphorylation. Autophosphorylation also enables CaMKII to attain an enhanced affinity for NMDA receptors in postsynaptic densities .