CaMKII alpha Antibody, Clone 6G9

Calcium/calmodulin-dependent protein kinase II (CaMKII) is a pivotal serine/threonine kinase that plays a critical role in synaptic plasticity, memory formation, and neurodegenerative disease mechanisms. Highly enriched in forebrain neurons, CaMKII is localized to both the soma and dendrites, where it orchestrates calcium signaling in response to synaptic activity. The neuronal isoforms—comprising 52 kDa (α subunit) and 60 kDa (β subunit) —assemble into multimeric holoenzymes that integrate calcium dynamics with downstream signaling. CaMKII activation is initiated by Ca²⁺/calmodulin binding, which relieves autoinhibition and triggers autophosphorylation at threonine 286 (Thr286) . This phosphorylation event confers autonomous kinase activity, even after calcium levels subside, and enhances CaMKII’s affinity for NMDA receptors at postsynaptic densities—an essential mechanism for long-term potentiation (LTP) . The phosphorylation state of Thr286 is tightly regulated: protein phosphatase 1 (PP1) dephosphorylates it, while protein kinase A (PKA) counteracts this dephosphorylation, sustaining CaMKII activity. Dysregulation of CaMKII signaling has been implicated in multiple neurodegenerative disorders, including Alzheimer’s disease, where aberrant phosphorylation and synaptic dysfunction are hallmark features. As a master regulator of synaptic strength and plasticity, CaMKII remains a high-value target in neuroscience research and therapeutic development for cognitive and neurodegenerative disorders.

CaMKII, CaM kinase II, CaM KII, CaMK-II, CamK-II, CAMKII, CaMKii, CamKII, Camkii, camKII, camkII, camkii, CAMKIIalpha, CamKIIalpha, CAMKIId, CDPK1, dCAMKII, dCaMKII, DCK, CAMK2A, CAMK2B, CAMK2D, CAMK2G, CAMKA

0.1 µg/ml was sufficient for detection of CamKII in 20 µg rat brain tissue extract by colorimetric immunoblot analysis using Goat Anti-Mouse IgG:AP as the secondary.

1. Hughes K. et al. (2001) J. Biol. Chem. 276: 36008–36013. 2. Barria A. et al. (1997) Science 276: 2042–2045. 3. Bennet M.K. and Kennedy M.B. (1987) Proc. Natl. Acad. Sci. U.S.A. 84: 1794-1798. 4. Broke L., Srinivasan M. and Schulman H. (1995) J. Neurosci. 15: 6797-6808. 5. Nghiem P., Saati S. M., Martens C. L., Gardner P. and Schulman H. (1993) J. Biol. Chem. 268: 5471-5479. 6. Edman C.F. and Schulman H. (1994) Biochem. Biophys. Acta 1221: 90-102. 7. Tombes R.M. and Krystal G.W., (1997) Biochem. Biophys. Acta 13555: 281-292. 8. Means A.R. (2000) Mol. Endocrinol. 14: 4–12. 9. Makhinson M. et al. (1999) J. Neurosci. 19: 2500–2510. 10. Strack S. and Colbran R.J. (1998) J. Biol. Chem. 273: 20689-20692. 11. Leonard S.A., Lim I.A., Hemsworth D.E., Horne M.C. and Hell J.W. (1999) Proc. Natl. Acad. Sci. U.S.A. 96: 3239-3244. 12. Shen K. and Meyer Y. (1999) Science 284: 162-167.

1. Hughes K. et al. (2001) J. Biol. Chem. 276: 36008–36013. 2. Barria A. et al. (1997) Science 276: 2042–2045. 3. Bennet M.K. and Kennedy M.B. (1987) Proc. Natl. Acad. Sci. U.S.A. 84: 1794-1798. 4. Broke L., Srinivasan M. and Schulman H. (1995) J. Neurosci. 15: 6797-6808. 5. Nghiem P., Saati S. M., Martens C. L., Gardner P. and Schulman H. (1993) J. Biol. Chem. 268: 5471-5479. 6. Edman C.F. and Schulman H. (1994) Biochem. Biophys. Acta 1221: 90-102. 7. Tombes R.M. and Krystal G.W., (1997) Biochem. Biophys. Acta 13555: 281-292. 8. Means A.R. (2000) Mol. Endocrinol. 14: 4–12. 9. Makhinson M. et al. (1999) J. Neurosci. 19: 2500–2510. 10. Strack S. and Colbran R.J. (1998) J. Biol. Chem. 273: 20689-20692. 11. Leonard S.A., Lim I.A., Hemsworth D.E., Horne M.C. and Hell J.W. (1999) Proc. Natl. Acad. Sci. U.S.A. 96: 3239-3244. 12. Shen K. and Meyer Y. (1999) Science 284: 162-167.