|Predicted||Bovine, Chicken, Human, Mouse, Xenopus, Zebrafish|
|Calculated MW||50/60 KDa|
|Other Names||Calcium/calmodulin-dependent protein kinase type II subunit alpha, CaM kinase II subunit alpha, CaMK-II subunit alpha, Camk2a|
|Target/Specificity||Synthetic phospho-peptide corresponding to amino acid residues surrounding Thr305 conjugated to KLH.|
|Format||Unpurified neat serum.|
|Antibody Specificity||Specific for the ~50k α-CaM Kinase II and the ~60k β-CaM Kinase IIproteins phosphorylated at Thr305. Immunolabeling is blocked by the phosphopeptide used asantigen but not by the corresponding dephosphopeptide|
|Storage||Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.|
|Precautions||Phospho-Thr305 CaM Kinase II Antibody is for research use only and not for use in diagnostic or therapeutic procedures.|
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Provided below are standard protocols that you may find useful for product applications.
Ca2+/Calmodulin-Dependent Protein Kinase II (CaM Kinase II) is a multi-functional calcium and calmodulin-dependent protein kinase that mediates cellular responses to a wide variety of intercellular signals (Kennedy, 1998; Schulman and Hanson, 1993). CaM Kinase II has been shown to regulate diverse cellular functions including synaptic plasticity, neurotransmitter synthesis and release, gene expression, ion channel function, carbohydrate metabolism, cytoskeletal function, and Ca2+-homeostasis (Gleason et al., 2003; Soderling, 2000; Hudmon and Schulman, 2002). Phosphorylation of Thr286 on the kinase produces an autonomously active form of CaM Kinase II (Meng et al., 2003; Picciotto et al., 1993). Autophosphorylation of Thr305 inhibits the activity of CaM Kinase II. Phosphorylation at this site appears to reduce the association of CaM Kinase II with the PSD and reduce LTP and learning (Elgersma et al., 2002).
Elgersma Y, Fedorov NB, Ikonen S, Choi ES, Elgersma M, Carvalho OM, Giese KP, Silva AJ (2002) Inhibitory
autophosphorylation of CaMKII controls PSD association, plasticity, and learning. Neuron 36:493-505.
Gleason MR, Higashijima S, Dallman J, Liu K, Mandel G, Fetcho JR (2003) Translocation of CaM kinase II to
synaptic sites in vivo. Nature Neurosci 6:217-218.
Hudmon A, Schulman H (2002) Neuronal Ca2+/calmodulin-dependent protein kinase II: The role of structure and
autoregulation in cellular function. Annu Rev Biochem 71:473-510.
Kennedy MB (1998) Signal transduction molecules at the glutamatergic postsynaptic membrane. Brain Res Rev
Meng FJ, Guo J, Zhang QG, Song B, Zhang GY (2003) Autophosphorylated calcium/calmodulin-dependent protein
kinase IIa (CaMKIIa) reversibly targets to and phosphorylates N-methyl-D-aspartate receptor subunit 2B (NR2B)
in cerebral ischemia and reperfusion in hippocampus of rats. Brain Res 967:161-169.
Picciotto MR, Czernik AJ, Nairn AC (1993) Calcium/calmodulin-dependent protein kinase I. cDNA cloning and
identification of autophosphorylation site. J Biol Chem 268:26512-26521.
Schulman H, Hanson PI (1993) Multifunctional Ca2+/calmodulin-dependent protein kinase. Neurochem Res 18:65-77.
Soderling TR (2000) CaM-kinases: modulators of synaptic plasticity. Curr Opin Neurobiol 10:375-380.
Haiqin Lu, Hung-Tat Leung, Ning Wang, William L. Pak, and Bih-Hwa Shieh (2009) Role of Ca2+/Calmodulindependent
Protein Kinase II in Drosophila Photoreceptors J. Biol. Chem., 284: 11100 - 11109.
Rebekah S. Vest, Kurtis D. Davies, Heather O'Leary, J. David Port, and K. Ulrich Bayer (2007) Dual Mechanism of a
Natural CaMKII Inhibitor. Mol. Biol. Cell, 18: 5024 - 5033.
Matthew Townsend, Tapan Mehta, and Dennis J. Selkoe (2007) Soluble A Inhibits Specific Signal Transduction
Cascades Common to the Insulin Receptor Pathway. J. Biol. Chem., 282: 33305 - 33312
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