Phospho-CaM Kinase II (T286) Antibody Summary
Applications
Please Note: Optimal dilutions should be determined by each laboratory for each application. General Protocols are available in the Technical Information section on our website.
Scientific Data
Detection of Phospho-CaM Kinase II (T286) by Western Blot. Western Blot of rat brain tissue lysate showing specific immunolabeling of the ~50 kDa alpha -CaMKII subunit phosphorylated at T286 and the ~60 kDa beta -CaMKII subunit phosphorylated at T287 (Control). The phosphospecificity of this labeling is demonstrated by treatment with 1200 U of lambda Phosphatase ( lambda -PPase) for 30 minutes before being exposed to the anti-phospho-CaMKII (T286). The immunolabeling is completely eliminated by treatment with lambda -PPase.
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Preparation and Storage
Background: CaM Kinase II
Calmodulin Kinase II (CaMKII) is a 500 kDa, 8-12 subunit multimer that belongs to the Ser/Thr protein kinase family. It is ubiquitously expressed and interacts with a very diverse group of substrates. In rat, there are four possible subunits/isozymes ( alpha, beta, gamma, δ) that vary from 480-540 amino acids in length. The alpha - and beta -isozymes predominate in the brain. Each subunit contains a catalytic, autoregulatory, and subunit-association domain. The enzyme complex is inactive, due to the association of an internal pseudosubstrate motif with each subunit’s catalytic domain. CaMKII is regulated by calmodulin (CaM), an intracellular receptor for calcium. Following an influx of calcium, two Ca++-CaM complexes interact with inactive CaMKII at the autoregulatory site of two adjacent CaMKII subunits. This dissociates the catalytic site from the pseudosubstrate motif, allowing for the auto(cross)-phosphorylation of T286 on one alpha -subunit (T287 on a beta -subunit) by the catalytic site on an adjacent subunit. The T286 phosphorylation event blocks a reassociation of the catalytic domain with the internal pseudosubstrate motif, resulting in prolonged activation. Once activated, an autoinhibitory program ensues. The dissociation of Ca++-CaM from CaMKII exposes a Thr at position 305. CaMKII autophosphorylation of Thr at this site downregulates existing CaMKII activity.
- Griffith, L.C. (2004) J. Neurosci. 24:8391.
- Hudmon, A. and H. Schulman (2002) Annu. Rev. Biochem. 71:473.
- Lin, C.R. et al. (1987) Proc. Natl. Acad. Sci. USA 84:5962.
- Thiel, G. et al. (1988) Proc. Natl. Acad. Sci. USA 85:6337.
- Elgersma, Y. et al. (2002) Neuron 36:493.
Product Datasheets
Citations for Phospho-CaM Kinase II (T286) Antibody
R&D Systems personnel manually curate a database that contains references using R&D Systems products. The data collected includes not only links to publications in PubMed, but also provides information about sample types, species, and experimental conditions.
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DAPK1 Promotes Extrasynaptic GluN2B Phosphorylation and Striatal Spine Instability in the YAC128 Mouse Model of Huntington Disease
Authors: ME Schmidt, NS Caron, AE Aly, FL Lemarié, L Dal Cengio, Y Ko, N Lazic, L Anderson, B Nguyen, LA Raymond, MR Hayden
Front Cell Neurosci, 2020-11-05;14(0):590569.
Species: Mouse
Sample Types: Tissue Homeogenates
Applications: Immunoprecipitation -
Ear2 deletion causes early memory and learning deficits in APP/PS1 mice.
Authors: Kummer M, Hammerschmidt T, Martinez A, Terwel D, Eichele G, Witten A, Figura S, Stoll M, Schwartz S, Pape H, Schultze J, Weinshenker D, Heneka M, Urban I
J Neurosci, 2014-06-25;34(26):8845-54.
Species: Mouse
Sample Types: Cell Lysates
Applications: Western Blot
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