Rabbit polyclonal antibody
- Affinity Purified from Pooled Serum
- Rat, Mouse, Human, Xenopus, Bovine, Chicken, Zebra fish, Canine
- WB 1:1000
- Gene Name:
- Molecular Reference:
- ~50 kDa and ~60 kDa
- Cite This Antibody:
- PhosphoSolutions Cat# p1005-306, RRID:AB_2560940
The antigen is a phosphopeptide corresponding to amino acid residues surrounding the phospho-Thr306 found in rat brain CaM Kinase II.
The antibody is prepared from pooled rabbit serum by affinity purification via sequential chromatography on phospho- and dephospho-peptide affinity columns.
Ca 2+/Calmodulin-Dependent Protein Kinase II (CaM Kinase II) is a multifunctional 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). CaMKIIα autophosphorylation at Thr286 and Thr305/Thr306 has recently been shown to regulate kinase activity and modulate subcellular targeting and is critical for normal synaptic plasticity and learning and memory (Baucum et al., 2015).
100 µl in 10 mM HEPES (pH 7.5), 150 mM NaCl, 100 µg per ml BSA and 50% glycerol. Adequate amount of material to conduct 10-mini Western Blots.
For long term storage –20° C is recommended. Stable at –20° C for at least 1 year.
Baucum AJ , Shonesy BC, Rose KL, Colbran RJ (2015) Quantitative Proteomics Analysis of CaMKII Phosphorylation and the CaMKII Interactome in the Mouse Forebrain. ACS Chem Neurosci. 2015 Feb 24.
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 26:243-257.
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.