Specific for ~180k NMDAR NR2B subunit protein phosphorylated at Ser1480. Immunolabeling of the NMDA NR2B subunit band is blocked by the phosphopeptide used as the antigen but not by the corresponding dephosphopeptide. Immunolabeling is also blocked by (-phosphatase treatment.
The NMDA receptor (NMDAR) plays an essential role in memory, neuronal development and it has also been implicated in several disorders of the central nervous system including Alzheimer’s, epilepsy and ischemic neuronal cell death (Grosshans et al., 2002, Wenthold et al., 2003, Carroll and Zukin, 2002). The rat NMDAR1 (NR1) was the first subunit of the NMDAR to be cloned. The NR1 protein can form NMDA activated channels when expressed in Xenopus oocytes but the currents in such channels are much smaller than those seen in situ. Channels with more physiological characteristics are produced when the NR1 subunit is combined with one or more of the NMDAR2 (NR2 A-D) subunits (Ishii et al., 1993). It has been shown that phosphorylation of Ser1480 disrupts the interaction of NR2B with the PDZ domains of PSD-95 and SAP102 and decreases surface NR2B expression in neurons (Chung et al., 2004). Anti-Phospho-Ser1480 NMDA Receptor NR2B Subunit Western blot of rat hippocampal lysate showing specific immunolabeling of the ~180k NR2B subunit of the NMDAR phosphorylated at Ser1480 (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 phospho-Ser1480 NMDA NR2B subunit antibody. The immunolabeling is completely eliminated by treatment with (-Ptase.