Specific for ~180k NMDAR NR2B subunit protein phosphorylated at Tyr1252. 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 antibody may also show some slight reactivity with Tyr1246 of NR2A.
Cross-Reactivity
Mouse (Murine), Rat (Rattus)
Predicted Reactivity
bovine, canine, chicken, human, non-human primate, zebra fish
Purification
Antigen Affinity Purified from Pooled Serum
Immunogen
Synthetic phospho-peptide corresponding to amino acid residues surrounding Tyr1252 conjugated to KLH
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). Phosphorylation of Tyr1252 is thought to potentiate NMDA receptor-dependent influx of calcium (Takasu et al., 2002). Anti-Phospho-Tyr1252 NMDA Receptor NR2B Subunit Western blot of rat hippocampal lysate showing specific immunolabeling of the ~180k NR2B subunit of the NMDAR phosphorylated at Tyr1252 (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-Tyr1252 NMDA NR2B subunit antibody. The immunolabeling is completely eliminated by treatment with (-Ptase.