|Calculated MW||143101 Da|
|Homology||Mouse, human- 14/15 amino acid residues identical.|
|Other Names||Glutamate receptor ionotropic, NMDA 2D, GluN2D, Glutamate [NMDA] receptor subunit epsilon-4, N-methyl D-aspartate receptor subtype 2D, NMDAR2D, NR2D, Grin2d, GluN2D|
|Related products for control experiments||Control peptide antigen (supplied with the antibody free of charge).|
|Target/Specificity||Peptide CRTQNRTHRGESLHR, corresponding to amino acid residues 345-359 of rat NMDAR2D (Accession Q62645). Extracellular, N-terminus.|
|Peptide Confirmation||Confirmed by amino acid analysis.|
|Format||Affinity purified antibody, lyophilized powder|
|Reconstitution||25 µl, 50 µl or 0.2 ml deionized water, depending on the sample size.|
|Antibody Concentration After Reconstitution||0.8 mg/ml.|
|Buffer After Reconstitution||Phosphate buffered saline (PBS), pH 7.4, 1% BSA, 0.025% NaN3.|
|Storage Before Reconstitution||Lyophilized powder can be stored intact at room temperature for several weeks. For longer periods, it should be stored at -20°C.|
|Storage After Reconstitution||The reconstituted solution can be stored at 4ºC for up to 2 weeks. For longer periods, small aliquots should be stored at -20ºC or below. Avoid multiple freezing and thawing. The further dilutions should be made using a carrier protein such as BSA (1%). Centrifuge all antibody preparations before use (10000 × g 5 min).|
|Control Antigen Storage Before Reconstitution||Lyophilized powder can be stored intact at room temperature for several weeks. For longer periods, it should be stored at -20°C.|
|Control Antigen Reconstitution||100 µl water.|
|Control Antigen Storage After Reconstitution||-20ºC.|
|Preadsorption Control||1 µg peptide per 1 µg antibody.|
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Provided below are standard protocols that you may find useful for product applications.
The NMDA receptors (NMDARs) are members of the glutamate receptor family of ion channels that also include the AMPA and Kainate receptors. The NMDA receptors are encoded by seven genes: one NMDAR1 (or NR1) subunit, four NR2 (NR2A-NR2D) and two NR3 (NR3A-NR3B) subunits. The functional NMDA receptor appears to be a heterotetramer composed of two NMDAR1 and two NMDAR2 subunits. Whereas the NMDAR2 subunits that assemble with the NMDAR1 subunit can be either of the same kind (i.e. two NMDAR2A subunits) or different (one NMDAR2A with one NMDAR2B). NMDAR3 subunits can substitute the NMDAR2 subunits in their complex with the NMDAR1 subunit. The NMDAR is unique among ligand-gated ion channels in that it requires the simultaneous binding of two obligatory agonists: glycine and glutamate that bind to the NMDAR1 and NMDAR2 binding sites respectively. Another unique characteristic of the NMDA receptors is their dependence on membrane potential. At resting membrane potentials the channels are blocked by extracellular Mg2+. Neuronal depolarization relieves the Mg2+ blockage and allows ion influx into the cells. NMDA receptors are strongly selective for Ca2+ influx differing from the other glutamate receptor ion channels that are non-selective cation channels. Ca2+ entry through the NMDAR regulates numerous downstream signaling pathways including long term potentiation (a molecular model of memory) and synaptic plasticity that may underlie learning. In addition, the NMDA receptors have been implicated in a variety of neurological disorders including epilepsy, ischemic brain damage, Parkinson’s and Alzheimer’s disease. The expression and function of NMDA receptors are modulated by a variety of factors including receptor trafficking to the synapses and internalization as well as phosphorylation and interaction with other intracellular proteins. Abgent is pleased to offer a highly specific antibody directed against an epitope located at the extracellular N-terminal domain of rat NMDA Receptor 2D (NMDAR2D). Anti-NMDA Receptor 2D (GluN2D) (extracellular) antibody (#AG1428) can be used in western blot analysis and has been designed to recognize NR2D from rat, mouse and human samples.
References 1. Dingledine, R. et al. (1999) Pharmacol. Rev. 51, 7. 2. Mayer, M.L. and Armstrong, N. (2004) Annu. Rev. Physiol. 66, 161. 3. Prybylowski, K. and Wenthold, R.J. (2004) J. Biol. Chem. 279, 9673. 4. Mayer, M.L. (2006) Nature 440, 456.
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