Detection of GRIN2B/NMDAR2B by Western Blot. Western blot of rat hippocampal lysate showing specific immunolabeling of the approximately 180 kDa NR2B subunit of the NMDA Receptor.
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NMDA (N-Methyl D-Aspartate) receptors are members of the glutamate receptor family of ligand-gated ion channels. The functional NMDA receptor (NMDAR) is a 650-850 kDa heteromultimer of at least two NR2 (NMDAR2) subunits and two NR1 subunits. NR2 subunits determine overall NMDAR characteristics such as conductance and Mg++ sensitivity. In addition, NR2 subunits mediate NMDAR clustering and synaptic localization through cytoplasmic interaction with PSD-95/SAP90 family members. Upon glutamate binding to NR2, and glycine binding to NR1, the NMDA channel is opened, allowing calcium and sodium influx into the cell. There are four genes that code for NR2 subunits (NR2A-D). The two (or three) NR2 subunits making up the NMDAR may be homodimers or heterodimers. The 2B form generates a high conductance NMDAR. Human NR2B (also NR3 and GRIN2B) is a 180 kDa, 1458 amino acid (aa), three transmembrane (TM) glycoprotein that contains a 531 aa N-terminal extracellular domain (ECD) and a 646 aa cytoplasmic region. The loop connecting TM segments 2 and 3, plus the N-terminal ECD constitute the glutamate binding site. Human NR2B is more than 98% aa identical to NR2B in mouse, rat, and dog.
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