Rat GRIN1 (Glutamate Receptor, Ionotropic, N-Methyl-D-Aspartate 1) ELISA Kit

The test principle applied in this kit is Sandwich enzyme immunoassay. The microtiter plate provided in this kit has been pre-coated with an antibody specific to Rat GRIN1. Standards or samples are added to the appropriate microtiter plate wells then with a biotin-conjugated antibody specific to Rat GRIN1. Next, Avidin conjugated to Horseradish Peroxidase (HRP) is added to each microplate well and incubated. After TMB substrate solution is added, only those wells that contain Rat GRIN1, biotin-conjugated antibody and enzyme-conjugated Avidin will exhibit a change in color. The enzyme-substrate reaction is terminated by the addition of sulphuric acid solution and the color change is measured spectrophotometrically at a wavelength of 450nm ± 10nm. The concentration of Rat GRIN1 in the samples is then determined by comparing the OD of the samples to the standard curve. Protein Function: Component of N-methyl-D-aspartate (NMDA) receptors (NMDARs) that function as heterotetrameric, ligand-gated cation channels with high calcium permeability and voltage-dependent block by Mg(2+) (PubMed:1350383, PubMed:1388270, PubMed:1834949, PubMed:8428958). NMDARs participate in synaptic plasticity for learning and memory formation by contributing to the long-term potentiation (LTP) (By similarity). Channel activation requires binding of the neurotransmitter L-glutamate to the GluN2 subunit, glycine or D-serine binding to the GluN1 subunit, plus membrane depolarization to eliminate channel inhibition by Mg(2+) (PubMed:11823786, PubMed:1350383, PubMed:1388270, PubMed:15996549, PubMed:18177891, PubMed:1834949, PubMed:24876489, PubMed:27135925, PubMed:27618671, PubMed:28384476, PubMed:28468946, PubMed:8428958). NMDARs mediate simultaneously the potasium efflux and the influx of calcium and sodium (By similarity). Each GluN2 or GluN3 subunit confers differential attributes to channel properties, including activation, deactivation and desensitization kinetics, pH sensitivity, Ca2(+) permeability, and binding to allosteric modulators (PubMed:10436042, PubMed:11160393, PubMed:11929923, PubMed:28384476, PubMed:9463421). Forms excitatory glycinergic receptor complexes with GluN3 alone which are activated by glycine binding to the GluN1 and GluN3 subunits (PubMed:11823786, PubMed:11929923, PubMed:12391275) [The Uniprot Consortium]