Calcium/calmodulin-Dependent Protein Kinase II alpha (CAMK2A) (pThr286) antibody

Details for Product No. ABIN361458
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Antigen
Synonyms camk2, camk2b, zgc:112538, zgc:123320, CAMKA, CaMKII, R74975, mKIAA0968, PK2CDD, PKCCD
Epitope
pThr286
(23), (17), (7), (7), (5), (5), (5), (3), (3), (3), (2), (2), (1), (1), (1), (1), (1), (1), (1), (1)
Reactivity
Rat (Rattus)
(75), (62), (41), (9), (6), (6), (5), (5), (4), (4), (2), (2), (2), (1), (1), (1), (1), (1)
Host
Rabbit
(74), (44), (7)
Clonality
Polyclonal
Conjugate
Un-conjugated
(3), (3), (3), (3), (2), (2), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1)
Application
Western Blotting (WB)
(119), (64), (36), (36), (27), (24), (23), (5), (4), (3), (2), (2)
Pubmed 5 references available
Quantity 100 μL
Options
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Catalog No. ABIN361458
379.50 $
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Specificity Specific for the ~50k a-CaM Kinase II and the ~60k ß-CaM Kinase II proteins phosphorylated at Thr286. Immunolabeling is blocked by the (-phosphatase treatment.
Purification Affinity-purified
Alternative Name CaM Kinase II
Background 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). Anti-Phospho Thr286 CaM Kinase II Western blot of rat brain lysate showing specific immunolabeling of the ~50k (- and the ~60k (-CaM Kinase II phosphorylated at Thr286 (Control). The phosphospecificity of this labeling is shown in the second lane (lambda-phosphatase: (-Ptase). The blot is identical to the control except that it was incubated in (-Ptase (1200 units for 30 min) before being exposed to the Anti-Thr286 CaM Kinase II. The immunolabeling is completely eliminated by treatment with (-Ptase.
Application Notes Recommended Dilution: WB: 1:1000 Quality Control: Western blots performed on each lot.
Restrictions For Research Use only
Format Liquid
Storage -20 °C
Supplier Images
anti-Calcium/calmodulin-Dependent Protein Kinase II alpha (CAMK2A) (pThr286) antibody Western blots of rat brain lysate showing specific immunolabeling of the ~50k (- and the ~60k (-CaM Kinase II phosphorylated at Thr286 (Control). The phosphospecificity of this labeling is shown in the second lane (lambda-phosphatase: (-Ptase). The blot is identical to the control except that it was incubated in (-Ptase (1200 units for 30 min) before being exposed to the Anti-Thr286 CaM Kinase II. The immunolabeling is completely eliminated by treatment with (-Ptase.
Product cited in: Kothmann, Trexler, Whitaker et al.: "Nonsynaptic NMDA receptors mediate activity-dependent plasticity of gap junctional coupling in the AII amacrine cell network." in: The Journal of neuroscience : the official journal of the Society for Neuroscience, Vol. 32, Issue 20, pp. 6747-59, 2012 (PubMed).

Coultrap, Barcomb, Bayer: "A significant but rather mild contribution of T286 autophosphorylation to Ca2+/CaM-stimulated CaMKII activity." in: PLoS ONE, Vol. 7, Issue 5, pp. e37176, 2012 (PubMed). Method employed by authors: Western Blotting (WB)

Boguslavsky, Chiu, Foley et al.: "Myo1c binding to submembrane actin mediates insulin-induced tethering of GLUT4 vesicles." in: Molecular biology of the cell, Vol. 23, Issue 20, pp. 4065-78, 2012 (PubMed).

General Ahmed, Gardiner: "Preserving protein profiles in tissue samples: differing outcomes with and without heat stabilization." in: Journal of neuroscience methods, Vol. 196, Issue 1, pp. 99-106, 2011 (PubMed).

Ferrario, Loweth, Milovanovic et al.: "Alterations in AMPA receptor subunits and TARPs in the rat nucleus accumbens related to the formation of Ca(2+)-permeable AMPA receptors during the incubation of cocaine craving." in: Neuropharmacology, 2011 (PubMed).

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