Anti-GluA1-GluR1 Antibody (56547)

Fusion protein corresponding to aa 1-389 (extracellular N-terminus) of rat GluA1/GluR1 (accession no. P19490).

PBS, pH 7.4; 50% glycerol, 0.09% sodium azide.

Liquid

Purified by Protein G affinity chromatography

This antibody is stable for at least one (1) year at -20°C. Avoid repeated freezing and thawing.

For in vitro investigational use only. Not for use in therapeutic or diagnostic procedures.

Next Day 2-8°C

This antibody recognizes mouse and rat GluA1/GluR1. It does not cross-react with GluR2.

Regulation of alpha-amino-3-hydroxy-5- methyl-4-isoxazole propionic acid receptors (AMPARs) plays a key role in altering excitatory synaptic transmission in the CNS. Interestingly, the regulatory mechanisms differ between distinct subunits of AMPAR, which range from glutamate receptor 1 (GluR1) to GluR4 (also referred to as GluA1–4). For example, subunits with a long intracellular carboxy terminus (i.e., GluR1, GluR2L, and GluR4) are involved in activity- dependent synaptic targeting of AMPAR, whereas those with a shorter carboxy terminus (i.e., GluR2, GluR3, and GluR4s) seem to maintain basal synaptic transmission. GluR1 has several phosphorylation sites on the intracellular carboxy terminus. Many of these sites have been demonstrated to play a role in synaptic AMPAR regulation and synaptic plasticity.

Ionotropic glutamate receptor. 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. {PubMed:16793768, PubMed:19265014}.