Western blot analysis of rat cortex lysate showing specific immunolabeling of the ~50 kDa alpha-subunit and ~60 kDa beta-subunit of CaM Kinase II phosphorylated at Thr286 (Lane 1). The phosphospecificty of this labeling is shown in Lane 2 (lambda-phosphatase). The blot is identical to the control except that it was incubated in lambda-Ptase (1200 unit for 30 min.) before being exposed to the Phospho-Thr286 CaM Kinase II antibody. The immunolabeling of the CaM Kinase II is completely eliminated by the lambda-phosphatase.
|Tested species reactivity||Rat|
|Published species reactivity||Not Applicable|
|Host / Isotype||Rabbit / IgG|
|Immunogen||Synthetic phospho-peptide corresponding to amino acid residues surrounding Thr286 of rat CAMK2A/B conjugated to KLH|
|Storage buffer||0.01M HEPES, pH 7.5, with 0.15M NaCl, 100µg/ml BSA, 50% glycerol|
|Storage Conditions||-20° C, Avoid Freeze/Thaw Cycles|
|Tested Applications||Dilution *|
|Dot blot (DB)||1:1000|
|Western Blot (WB)||1:1000|
* Suggested working dilutions are given as a guide only. It is recommended that the user titrate the product for use in their own experiment using appropriate negative and positive controls.
|Western Blot (WB)||See 1 publications below|
This antibody is predicted to react with human, mouse and Xenopus based on 100% sequence homology.
This antibody is specific for the ~50 kDa alpha-CaM Kinase II subunit and the ~60 kDa beta-CaM Kinase II subunit phosphorylated at Thr286 in Western blots of rat brain lysates. Immunolabeling is blocked by the phosphopeptide used as the antigen but not by the corresponding dephosphopeptide.
Ca2+/Calmodulin-Dependent Protein Kinase II (CaM Kinase II) is a multi-functional calcium and calmodulin-dependent protein kinase that mediates cellular response 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 reduces LTP and learning (Elgersma et al., 2002).
For Research Use Only. Not for use in diagnostic procedures. Not for resale without express authorization.
Time-dependent activation of MAPK/Erk1/2 and Akt/GSK3 cascades: modulation by agomelatine.
PA1-4614 was used in western blot to study modulation of agomelatine by time dependent activation of Akt/GSK3 and MAPK/Erk1/2 cascades
|Musazzi L,Seguini M,Mallei A,Treccani G,Pelizzari M,Tornese P,Racagni G,Tardito D||BMC neuroscience (15:null)||2014|