Anti-Ionotropic Glutamate receptor 2/GRIA2 Antibody Picoband® Fluoro647 Conjugated

Glutamate receptor 2, also known as GLUR2, is a protein that in humans is encoded by the GRIA2 gene. This gene product belongs to a family of glutamate receptors that are sensitive to alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionate (AMPA), and function as ligand-activated cation channels. GLUR2's cytogenetic location is 4q32.1. The crystal structures of the GLUR2 ligand-binding core in the apo state and in the presence of the antagonist DNQX, the partial agonist kainate, and the full agonists AMPA and glutamate.GLUR2 plays a major role in depression at synapses in which glutamate remains in the synaptic cleft for prolonged periods of time during normal operation of the synapse. The overexpression of GLUR2 increases dendritic spine size and density in hippocampal neurons, and more remarkably, induces spine formation in GABA-releasing interneurons that normally lack spines.

E.coli-derived human GRIA2 recombinant protein (Position: N25-I360) . Human GRIA2 shares 99% amino acid (aa) sequence identity with both mouse and rat GRIA2.

Receptor for glutamate that functions as ligand-gated ion channel in the central nervous system and plays an important role in excitatory synaptic transmission. L-glutamate acts as an excitatory neurotransmitter at many synapses in the central nervous system. Binding of the excitatory neurotransmitter L- glutamate induces a conformation change, leading to the opening of the cation channel, and thereby converts the chemical signal to an electrical impulse. The receptor then desensitizes rapidly and enters a transient inactive state, characterized by the presence of bound agonist. In the presence of CACNG4 or CACNG7 or CACNG8, shows resensitization which is characterized by a delayed accumulation of current flux upon continued application of glutamate. .

1. Armstrong, N., Gouaux, E. Mechanisms for activation and antagonism of an AMPA-sensitive glutamate receptor: crystal structures of the GluR2 ligand binding core. Neuron 28: 165-181, 2000. 2. Biou, V., Bhattacharyya, S., Malenka, R. C. Endocytosis and recycling of AMPA receptors lacking GluR2/3. Proc. Nat. Acad. Sci. 105: 1038-1043, 2008. 3. Mameli, M., Balland, B., Lujan, R., Luscher, C. Rapid synthesis and synaptic insertion of GluR2 for mGluR-LTD in the ventral tegmental area. Science 317: 530-533, 2007.

Cell membrane ; Multi-pass membrane protein . Endoplasmic reticulum membrane ; Multi-pass membrane protein . Cell junction, synapse, postsynaptic cell membrane ; Multi-pass membrane protein . Interaction with CACNG2, CNIH2 and CNIH3 promotes cell surface expression. .