Specific for the ~100k GluR1 protein phosphorylated at Ser831. Immunolabeling is blocked by the phosphopeptide used as antigen but not by the corresponding dephosphopeptide. Immunolabeling is completely eliminated by lambda-phosphatase treatment.
Réactivité croisée (Details)
Species reactivity (expected):Human, Canine, Chicken and Mouse. Species reactivity (tested):Rat.
Purification
Sequential Chromatography on phospho- and dephosphopeptide affinity columns.
Immunogène
Phosphopeptide corresponding to amino acid residues surrounding the phospho-Ser831 of GluR1.
GLUR1
Reactivité: Rat
WB, IHC, IF, ICC
Hôte: Souris
Monoclonal
S355-1
PE
Indications d'application
Western blot: 1/1000. Other applications not tested. Optimal dilutions are dependent on conditions and should be determined by the user.
Restrictions
For Research Use only
Format
Liquid
Buffer
10 mM HEPES ( pH 7.5), 150 mM NaCl, 100 μg/mL BSA and 50 % Glycerol.
Conseil sur la manipulation
Avoid repeated freezing and thawing.
Stock
-20 °C
Stockage commentaire
Store the antibody undiluted (in aliquots) at-20 °C.
Barcomb, Coultrap, Bayer: "Enzymatic activity of CaMKII is not required for its interaction with the glutamate receptor subunit GluN2B." dans: Molecular pharmacology, Vol. 84, Issue 6, pp. 834-43, (2013) (PubMed).
Jiao, Jalan-Sakrikar, Robison, Baucum, Bass, Colbran: "Characterization of a central Ca2+/calmodulin-dependent protein kinase IIalpha/beta binding domain in densin that selectively modulates glutamate receptor subunit phosphorylation." dans: The Journal of biological chemistry, Vol. 286, Issue 28, pp. 24806-18, (2011) (PubMed).
Sears, Liu, Narayanan, Sharf, Yeckel, Laubach, Aghajanian, DiLeone: "Regulation of nucleus accumbens activity by the hypothalamic neuropeptide melanin-concentrating hormone." dans: The Journal of neuroscience : the official journal of the Society for Neuroscience, Vol. 30, Issue 24, pp. 8263-73, (2010) (PubMed).
Coultrap, Buard, Kulbe, DellAcqua, Bayer: "CaMKII autonomy is substrate-dependent and further stimulated by Ca2+/calmodulin." dans: The Journal of biological chemistry, Vol. 285, Issue 23, pp. 17930-7, (2010) (PubMed).
Davies, Goebel-Goody, Coultrap, Browning: "Long term synaptic depression that is associated with GluR1 dephosphorylation but not alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid (AMPA) receptor internalization." dans: The Journal of biological chemistry, Vol. 283, Issue 48, pp. 33138-46, (2008) (PubMed).
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 alpha-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. GluR1 is potentiated by phosphorylation at Ser831 which has been shown to be mediated by either PKC or CaM kinase II (McGlade-McCulloh et al., 1993, Mammen et al., 1999, Roche et al., 1996). In addition, phosphorylation of this site has been linked to synaptic plasticity as well and learning and memory (Soderling and Derkach, 2000).Synonyms: AMPA-selective glutamate receptor 1, AMPA1, GLUH1, GRIA1, GluR-1, GluR-A, GluR-K1, Glutamate receptor ionotropic