Product Specification:
| Alternative Name: | Calcium/calmodulin-dependent protein kinase II |
| Clone: | 6G9 |
| Host: | Mouse |
| Isotype: | IgG1 |
| Immunogen: | Rat CaMKII (partially purified). |
| UniProt ID: | P15791 |
| GenBank ID: | J05072 |
| Species reactivity: | Mouse, Rat |
| Applications: | IHC, WBin vitro Assay |
| Recommended Dilutions/Conditions: | Western Blot (Colorimetric, 1:1,000)Suggested dilutions/conditions may not be available for all applications.Optimal conditions must be determined individually for each application. |
| Application Notes: | Detects a band of ~50-60kDa by Western blot. |
| Purity Detail: | Protein G affinity purified. |
| Formulation: | Liquid. In PBS containing 50% glycerol and 0.09% sodium azide. |
| Shipping: | Shipped on Blue Ice |
| Long Term Storage: | -20°C |
| Scientific Background: | CaMKIIa, the alpha subunit of Ca2+ calmodulin-dependent protein kinase II is part of a family of multifunctional protein kinases, which play a major role in Ca2+-mediated signal transduction. CaMKIIa is expressed in many different tissues but is specifically found in the neurons of the forebrain and its mRNA is found within the dendrites as well as the soma of the neuron. The neuronal CaMKII consists of two major subunits of 52 and 60 kDa which are encoded by a- and b-CaMKII genes, respectively. Additional isoforms are generated by alternative splicing of these as well as of the ubiquitious g- and d-CaMKII genes. Each subunit has an ATP-binding domain (arginine-X-X-serune/threonine), consensus phosphorylation site, catalytic domain, and a centrally located regulatory domain which has calmodulin binding activity. Activation and autophosphorylation of CaMKII may regulate numerous neuronal processes which includes two forms of synaptic plasticity, long term potentiation and long term depression. Neuronal CaMKII subunits assemble as large multimeric holoenzymes. The C-terminal association domains of 6-12 subunits assemble into a central globular structure from which the N-terminal catalytic/regulatory domains extend radially like petals of a flower. The subunit composition of the rat forebrain CaMKII holoenzyme consists of heteromers composed of a and β subunits at a ratio of 2:1 and homomers composed of only a subunits. The association of CaMKII subunits leads to the positioning of their catalytic/regulatory domains in close proximity and the neighboring calmodulin-bound subunits cooperate to rapidly phosphorylate each other. Autophosphorylation also enables CaMKII to attain an enhanced affinity for NMDA receptors in postsynaptic densities. |
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