Western blot of rat hippocampal lysate showing specific immunolabeling of the ~180 kDa NR2B subunit of the NMDAR (Lane 1). The phosphospecificty of this labeling is shown in Lane 2 (lambda phosphatase). The blot is identical to the control except that it was incubated in lambda-Ptase (1200 units for 30 min) before being exposed to the Anti Phospho Tyr1336 NMDA NR2B subunit. The immunolabeling of NR2B is completely eliminated by treatment with lambda-Ptase.
|Tested species reactivity||Rat|
|Published species reactivity||Rat|
|Host / Isotype||Rabbit / IgG|
|Immunogen||Synthetic phospho-peptide corresponding to amino acid residues surrounding Tyr1336 of rat GRIN2B conjugated to KLH|
|Storage buffer||0.01M HEPES, pH 7.5, with 0.15M NaCl, 100µg/ml BSA, 50% glycerol|
|Storage Conditions||-20° C, Avoid Freeze/Thaw Cycles|
|Tested Applications||Dilution *|
|Western Blot (WB)||1:1000|
* Suggested working dilutions are given as a guide only. It is recommended that the user titrate the product for use in their own experiment using appropriate negative and positive controls.
|Western Blot (WB)||See 1 publications below|
This antibody is predicted to react with human, mouse and non-human primate based on 100% sequence homology.
This antibody is specific for ~180 kDa NMDAR NR2B subunit protein phosphorylated at Tyr1336. Immunolabeling can be blocked by lambda-phosphatase treatment.
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 and quote;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).
For Research Use Only. Not for use in diagnostic procedures. Not for resale without express authorization.
Estradiol potentiation of NR2B-dependent EPSCs is not due to changes in NR2B protein expression or phosphorylation.
PA1-4633 was used in western blot to investigate the mechanism for the synaptic regulation by estradiol
|Snyder MA,Cooke BM,Woolley CS||Hippocampus (21:398)||2011|