Phospho-CaMKII (Tyr231) Antibody detects endogenous levels of CaMKII only when phosphorylated at Tyr231.
Source / Purification
Polyclonal antibodies are produced by immunizing animals with a synthetic phosphopeptide corresponding to residues surrounding Tyr231 of human CaMKII. Antibodies are purified by protein A and peptide affinity chromatography.
Background
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through its inhibitory effect on PP1 (4).Phospho-CaMKII (Tyr231) Antibody is directed against a previously unpublished CaMKII tyrosine phosphorylation site at Tyr231 that was identified at Cell Signaling Technology (CST) using PhosphoScan®, CST's MS/MS platform for phosphorylation site discovery. Phosphorylation of CamKII at Tyr231 was observed in extracts isolated from ischemic rat brain.