Specific for ~180k NMDAR NR2B subunit protein phosphorylated at Tyr1336. Immunolabeling of the NMDAR NR2B subunit band is blocked by (-phosphatase treatment.
Kreuzreaktivität
Maus, Ratte (Rattus)
Homologie
human, non-human primate
Aufreinigung
Antigen Affinity Purified from Pooled Serum
Immunogen
Synthetic phospho-peptide corresponding to amino acid residues surrounding Tyr1336 conjugated to KLH
Recommended Dilution: WB: 1:1000 IHC: 1:400 Quality Control: Western blots performed on each lot.
Beschränkungen
Nur für Forschungszwecke einsetzbar
Format
Liquid
Buffer
100 μL in 10 mM HEPES ( pH 7.5), 150 mM NaCl, 100 μg per ml BSA and 50 % glycerol.
Lagerung
-20 °C
Jiang, Knox, Pathipati, Ferriero: "Developmental localization of NMDA receptors, Src and MAP kinases in mouse brain." in: Neuroscience letters, Vol. 503, Issue 3, pp. 215-9, (2011) (PubMed).
Hicklin, Wu, Radcliffe, Freund, Goebel-Goody, Correa, Proctor, Lombroso, Browning: "Alcohol inhibition of the NMDA receptor function, long-term potentiation, and fear learning requires striatal-enriched protein tyrosine phosphatase." in: Proceedings of the National Academy of Sciences of the United States of America, Vol. 108, Issue 16, pp. 6650-5, (2011) (PubMed).
Chernova, Steinert, Guerin, Nicotera, Forsythe, Smith: "Neurite degeneration induced by heme deficiency mediated via inhibition of NMDA receptor-dependent extracellular signal-regulated kinase 1/2 activation." in: The Journal of neuroscience : the official journal of the Society for Neuroscience, Vol. 27, Issue 32, pp. 8475-85, (2007) (PubMed).
The 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 Tyr1336 is thought to potentiate NMDA receptor-dependent influx of calcium (Takasu et al., 2002) and ischemia may also increase the phosphorylation of this site (Takagi et al., 2003). Anti-Phospho-Tyr1336 NMDA Receptor NR2B Subunit Western blot of rat hippocampal lysate showing specific immunolabeling of the ~180k NR2B subunit of the NMDAR phosphorylated at Tyr1336 (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-Tyr1336 NMDA NR2B antibody. The immunolabeling is completely eliminated by treatment with (-Ptase.