|Reactivity||Human, Mouse, Rat|
|Calculated MW||54088 Da|
|Other Names||Calcium/calmodulin-dependent protein kinase type II subunit alpha, CaM kinase II subunit alpha, CaMK-II subunit alpha, CAMK2A, CAMKA, KIAA0968|
|Target/Specificity||A synthetic peptide corresponding to residues near the N-terminal of human CaMKII was used as an immunogen.|
|Format||50 mM Tris-Glycine (pH 7.4), 0.15 M NaCl, 40% Glycerol, 0.01% sodium azide and 0.05% BSA.|
|Precautions||CaMKII Antibody is for research use only and not for use in diagnostic or therapeutic procedures.|
|Function||CaM-kinase II (CAMK2) is a prominent kinase in the central nervous system that may function in long-term potentiation and neurotransmitter release. Member of the NMDAR signaling complex in excitatory synapses it may regulate NMDAR-dependent potentiation of the AMPAR and synaptic plasticity (By similarity). Phosphorylates transcription factor FOXO3 on 'Ser-298' (PubMed:23805378). Activates FOXO3 transcriptional activity (By similarity).|
|Cellular Location||Cell junction, synapse, presynaptic cell membrane. Cell junction, synapse Note=Postsynaptic lipid rafts.|
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Provided below are standard protocols that you may find useful for product applications.
Calcium/calmodulin-dependent protein kinase II (CaMKII) is a widely distributed protein kinase that regulates numerous physiological functions. It is a ubiquitous serine/threonine protein kinase which is abundant in brain as a major PSD constituent. This enzyme is composed of distinct but related subunits (alpha, beta, gamma, and delta) (1). The synapse contains densely localized and interacting proteins that enable it to adapt to changing inputs. A Ca2+-sensitive protein complex involved in the regulation of AMPA receptor synaptic plasticity. The complex is comprised of MUPPI, a multi-PDZ domain-containing protein; SynGAP, a synaptic GTPase-activating protein; and the Ca2+/calmodulin-dependent kinase CaMKII. In synapses of hippocampal neurons, SynGAP and CaMKII are brought together by direct physical interaction with the PDZ domains of MUPP1, and in this complex, SynGAP is phosphorylated. Ca2+CaM binding to CaMKII dissociates it from the MUPP1 complex, and Ca2+ entering via the NMDAR drives the dephosphorylation of SynGAP (2).
1. NCBI Reference Sequence (RefSeq) 2. Zhang J, et al. Biochem Biophys Res Commun 285(2): 229-34, 2001.
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