CaM Kinase II Antibody (Phospho-Thr286) (OAPC00145)

Catalog No: OAPC00145 (Formerly GWB-7F8E7E)

Size:100 ul

Western blot of rat brain lysate showing specific immunolabeling of the ~50k alpha - and the ~60k beta -CaM Kinase II phosphorylated at Thr286 (Control). The phosphospecificity of this labeling is shown in the second lane (lambda-phosphatase: lambda -Ptase). The blot is identical to the control except that it was incubated in lambda -Ptase (1200 units for 30 min) before being exposed to the Anti-Thr286 CaM Kinase II. The immunolabeling is completely eliminated by treatment with lambda -Ptase.

Product Info

• Predicted Species Reactivity: Rat
• Product Format: Liquid. 100 ul in 10 mM HEPES (pH 7.5), 150 mM NaCl, 100 ug per ml BSA and 50% glycerol. Adequate amount of material to conduct 10-mini Western Blots.
• Clonality: Polyclonal
• Host: Rabbit
• Application: WB
• Additional Information: Packaging :
  100 ul in 10 mM HEPES (pH 7.5), 150 mM NaCl, 100 ug per ml BSA and 50% glycerol. Adequate amount of material to conduct 10-mini Western Blots.
• Reconstitution and Storage: For long term storage -20C is recommended. Stable at -20C for at least 1 year.
• Immunogen: Phosphopeptide corresponding to amino acid residues surrounding the phospho-Thr286 found in rat brain CaM Kinase II.
• Purification: Prepared from rabbit serum by affinity purification via sequential chromatography on phospho- and dephosphopeptide affinity columns.
• Predicted Homology Based on Immunogen Sequence: Rat
• Specificity: Specific for the ~50k alpha -CaM Kinase II and the ~60k beta -CaM Kinase II proteins phosphorylated at Thr286. Immunolabeling is blocked by the lambda -phosphatase treatment.
• Application Info: The antibody has been directly tested for reactivity in Western blots with rat tissue. It is anticipated that the antibody will react with human, mouse and Xenopus based on the fact that these species have 100% homology with the amino acid sequence used as antigen.
  Western blot of rat brain lysate showing specific immunolabeling of the ~50k alpha - and the ~60k beta -CaM Kinase II phosphorylated at Thr286 (Control). The phosphospecificity of this labeling is shown in the second lane (lambda-phosphatase: lambda -Ptase). The blot is identical to the control except that it was incubated in lambda -Ptase (1200 units for 30 min) before being exposed to the Anti-Thr286 CaM Kinase II. The immunolabeling is completely eliminated by treatment with lambda -Ptase.
  
• Reference: 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.
  Sun X, Milovanovic M, Zhao Y, Wolf ME. (2008) Acute and chronic dopamine receptor stimulation modulates AMPA receptor trafficking in nucleus accumbens neurons cocultured with prefrontal cortex neurons. J Neurosci. Apr 16;28(16):4216-30.
  Rebekah S. Vest, Heather O'Leary, Steven J. Coultrap, Mark S. Kindy, and K. Ulrich Bayer (2010) Effective Post-insult Neuroprotection by a Novel Ca2+/ Calmodulin-dependent Protein Kinase II (CaMKII) InhibitorJ. Biol. Chem., 285: 20675 - 20682.
  Kurtis D. Davies, Susan M. Goebel-Goody, Steven J. Coultrap, and Michael D. Browning (2008) Long Term Synaptic Depression That Is Associated with GluR1 Dephosphorylation but Not alpha -Amino-3-hydroxy-5-methyl-4-isoxazolepropionic Acid (AMPA) Receptor Internalization J. Biol. Chem., 283: 33138 - 33146.
  Xiu Sun, Michael Milovanovic, Yun Zhao, and Marina E. Wolf (2008) Acute and Chronic Dopamine Receptor Stimulation Modulates AMPA Receptor Trafficking in Nucleus Accumbens Neurons Cocultured with Prefrontal Cortex Neurons. J. Neurosci., 28: 4216 - 4230
  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 beta Inhibits Specific Signal Transduction Cascades Common to the Insulin Receptor Pathway. J. Biol. Chem., 282: 33305 - 33312

Target Info

• Gene Symbol: CAMK2A/B
• Alias Symbols: PKCCD, PK2CDD
• NCBI Gene Id: 25400
• Protein Name: Calcium/calmodulin-dependent protein kinase type II subunit alpha
• Description of Target: 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 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).
• Uniprot ID: P11275
• Protein Accession #: NP_037052.1
• Molecular Weight: ~50kDa Alpha & ~60kDa Beta