The antibody has been directly tested for reactivity in Western blots with rat tissue. It is anticipated that the antibody will react with human, mouse and non-human primate based on the fact that these species have 100% homology with the amino acid sequence used as antigen. Specific for the ~100k GluR1 protein phosphorylated at Ser845 in Western blots of rat brain extracts. Immunolabeling is blocked by the phosphopeptide used as antigen but not by the corresponding dephosphopeptide. Immunolabeling is completely eliminated by treatment with λ-Ptase.
Réactivité croisée
Souris, Rat (Rattus)
Homologie
human, non-human primates
Purification
Antigen Affinity Purified from Pooled Serum
Immunogène
Synthetic phospho-peptide corresponding to amino acid residues surrounding Ser845 conjugated to KLH
100 μL in 10 mM HEPES ( pH 7.5), 150 mM NaCl, 100 μg per ml BSA and 50 % glycerol.
Stock
-20 °C
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Affinity purified rabbit polyclonal antibody. Biological Significance: The ion channels activated by glutamate are typically divided into two classes. Those that are sensitive to N-methyl-D-aspartate (NMDA) are designated NMDA receptors (NMDAR) while those activated by α-amino-3-hydroxy-5-methyl-4-isoxalone propionic acid (AMPA) are known as AMPA receptors (AMPAR). The AMPAR are comprised of four distinct glutamate receptor subunits designated (GluR1-4) and they play key roles in virtually all excitatory neurotransmission in the brain (Keinänen et al., 1990; Hollmann and Heinemann, 1994). The GluR1 subunit is widely expressed throughout the nervous system. Phosphorylation of Ser845 on GluR1 is thought to be mediated by PKA and phosphorylation of this site increases the conductance of the AMPAR (Roche et al., 1996; Banke et al., 2000). In addition, phosphorylation of this site has been linked to synaptic plasticity as well as arning and memory (Lee at al., 2003; Esteban at al., 2003).