Phospho-CaMKII (Thr286) Antibody detects autogenous levels of CaMKII alone if phosphorylated at Thr286.
Polyclonal antibodies are produced by immunizing animals with a constructed phosphopeptide agnate to residues surrounding Thr286 of animal CaMKII. Antibodies are antiseptic by protein A and peptide affection chromatography.
CaMKII is an important member of the calcium/calmodulin-activated protein kinase family, functioning in neural synaptic stimulation and T-cell receptor signaling (1,2). CaMKII has catalytic and regulatory domains. The binding of Ca2+/calmodulin to its regulatory domain releases its autoinhibitory effect and activates the kinase (3). The activated CaMKII further autophosphorylates at Thr286 to render the kinase constitutively active (3). The threonine phosphorylation state of CaMKII can be regulated through PP1/PKA. PP1 (protein phosphatase 1) dephosphorylates phospho-CaMKII at Thr286. PKA (protein kinase A) prevents this dephosphorylation through its inhibitory effect on PP1 (4).
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