Overview |
bs-70125r-100ul |
GluR2-subunit (Ser880) Antibody |
WB |
Specific for endogenous levels of the ~100 kDa GluR2 protein phosphorylated at Ser880. Immunolabeling is blocked by preadsorption with the phosphopeptide used as antigen, but not by the corresponding non-phosphopeptide. |
Rat |
Human, Mouse, Chicken, Zebrafish, Non-Human Primate |
Specifications |
Unconjugated |
Rabbit |
Synthetic phospho-peptide corresponding to amino acid residues surrounding Ser880 conjugated to keyhole limpet hemocyanin (KLH). |
Ser880 |
Polyclonal |
IgG |
Lot Dependent |
Antigen Affinity purification from Pooled whole antiserum |
10 mM HEPES (pH 7.5), 150 mM NaCl, 100 µg per ml BSA and 50% glycerol. |
Storage at -20°C is recommended, as aliquots may be taken without freeze/thawing due to presence of 50% glycerol. Stable for at least 1 year at -20°C. |
Target |
29627 |
P19491 |
AMPA 2 antibody, AMPA selective glutamate receptor 2 antibody, AMPA-selective glutamate receptor 2 antibody, AMPA2 antibody, GluA2 antibody, GLUR 2 antibody, GLUR B antibody, GluR K2 antibody, GluR-2 antibody, GluR-B antibody, GluR-K2 antibody, GLUR2 antibody, GLURB antibody, Glutamate receptor 2 antibody, Glutamate receptor ionotropic AMPA 2 antibody, Glutamate receptor ionotropic antibody, Gria2 antibody, GRIA2_HUMAN antibody, HBGR2 antibody |
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 number of GluR2 subunits in the AMPA receptor complex affects the Ca2+ permeability, rectification and single-channel conductance of AMPA receptors. Ser-880 has been identified as the PKC phosphorylation site within the C-terminal region of GluR2 and has been shown to differentially regulate the interaction of the PDZ domain-containing proteins GRIP1 and PICK 1 (Matsuda et al., 1999) |
Application Dilution |
WB |
1:300-5000 |