Detection of Phospho-GRIN2B/NMDAR2B (Y1472) by Western Blot
Western blot of rat hippocampal lysate showing specific immunolabeling of the ~180 kDa NR2B subunit of the NMDAR (Control). The phosphospecificty of this labeling is demonstrated by treatment with 1200 U of lambda Phosphatase ( lambda -PPase) for 30 minutes before being exposed to the Anti-Phospho-NMDA NR2B subunit (Y1472). The immunolabeling is completely eliminated by treatment with lambda -PPase.
Preparation and Storage
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Stability & Storage
For long-term storage, ≤ -20° C is recommended. Product is stable at ≤ -20° C for at least 1 year.
Rat NMDA receptor subunit 2B (NR2B) is a 1456 amino acid, 180 kDa, 3-transmembrane member of the glutamate-gated ion channel family. NMDA are heteromultimers of at least two NR1 subunits and two NR2 or two (presumably) NR3 subunits. Upon ligand binding, NMDA receptors open and allow cation transit. The NR1 subunits bind glycine and are essential for the physical formation of the ion channel. NR2 subunits apparently bind glutamate and impart pharmacological properties to the receptor complex. Fully functional receptors require the presence of both glycine and glutamate. The NR1-NR2B complex has the highest affinity for glutamate. Both NR1 and NR2B subunits can be phosphorylated by PKC. On NR1, PKC phosphorylates on serine at 890; on NR2B, PKC phosphorylates on tyrosine at 1472. Phosphorylation is considered to promote ion transit and impact NR2B interaction with downstream signaling molecules.
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Liu, Y. and J. Zhang (2000) Chin. Med. J. 113:948.
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