Our Anti-NMDA NR2B Subunit rabbit polyclonal primary antibody from PhosphoSolutions is produced in-house. It detects human, mouse, and rat NMDA NR2B Subunit and is antigen affinity purified from pooled serum. It is great for use in WB, IHC, IP.
Western blot of 10 µg of rat hippocampal lysate showing specific immunolabeling of the ~180 kDa NR2B subunit of the NMDA receptor.
The ion channels activated by glutamate that are sensitive to N-methyl-Daspartate (NMDA) are designated NMDA receptors (NMDAR). 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 NMDA receptor is also one of the principal molecular targets for alcohol in the CNS (Lovinger et al., 1989; Alvestad et al., 2003; Snell et al., 1996). The rat NMDAR1 (NR1) was the first subunit of the NMDAR to be cloned and it 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. Overexpression of the NR2B-subunit of the NMDA receptor has been associated with increases in learning and memory while aged, memory impaired animals have deficiencies in NR2B expression (Clayton et al., 2002a; Clayton et al., 2002b). The NMDAR is also potentiated by protein phosphorylation (Lu et al., 1999).
Antigen Affinity Purified from Pooled Serum
Polyclonal
IgG
IHC, IP, WB
Rabbit
GRIN2B
180 kDa
Fusion protein from the C-terminal region of the NR2B subunit of the rat NMDA receptor.
Human, Mouse, Rat
AB_2492176
Storage at -20°C is recommended, as aliquots may be taken without freeze/thawing due to presence of 50% glycerol. Stable for at least 1 year at -20°C.
Liquid
Prepared from pooled rabbit serum by affinity purification using a column to which the fusion protein immunogen was coupled.
10 mM HEPES (pH 7.5), 150 mM NaCl, 100 µg per ml BSA and 50% glycerol.
Specific for endogenous levels of the ~180 kDa NR2B subunit of the NMDA receptor. Immunolabeling is blocked by preadsorption of antibody with the fusion protein used to generate the antibody. No reactivity towards the NR2A and NR2C subunits.
Western blots performed on each lot.
For research use only. Not intended for therapeutic or diagnostic use. Use of all products is subject to our terms and conditions, which can be viewed on our website.
After date of receipt, stable for at least 1 year at -20°C.
Hinklin,T.R., et al. 2011. Alcohol inhibition of the NMDA receptor function, long-term potentiation, and fear learning requires striatal-enriched protein tyrosine phosphatase. PNAS, Apr 2011; 108: 6650 - 6655.
Cook, S.G., et al. 2019. Simultaneous Live Imaging of Multiple Endogenous Proteins Reveals a Mechanism for Alzheimer’s-Related Plasticity Impairment. Cell reports, 27(3), pp.658-665.
O’Leary, H., et al. 2016. Enhanced long term potentiation and decreased AMPA receptor desensitization in the acute period following a single kainate induced early life seizure. Neurobiology of disease, 87, 134-144.
Hinklin,T.R., et al. 2011. Alcohol inhibition of the NMDA receptor function, long-term potentiation, and fear learning requires striatal-enriched protein tyrosine phosphatase. PNAS, Apr 2011; 108: 6650 - 6655.
Davies, K.D., et al. 2008. Long Term Synaptic Depression That Is Associated with GluR1 Dephosphorylation but Not -Amino-3-hydroxy-5-methyl-4-isoxazolepropionic Acid (AMPA) Receptor Internalization. J. Biol. Chem., 283: 33138 - 33146.
Norris, E.H., et al. 2007. Modulation of NR2B-regulated contextual fear in the hippocampus by the tissue plasminogen activator system. PNAS, 104: 13473 – 1347.
Alvestead, R.M., et al. 2003. Tyrosine dephosphorylation and ethanol inhibition of N-methyl-D-aspartate receptor function. Journal of Biological Chemistry, 278(13), pp.11020-11025.