Anti-GluR1-Subunit (Ser831) Antibody
Our Anti-GluR1-Subunit (Ser831) rabbit polyclonal phosphospecific primary antibody from PhosphoSolutions is produced in-house. It detects human, mouse, and rat GluR1-Subunit (Ser831) and is antigen affinity purified from pooled serum. It is great for use in WB.
Western blot of rat hippocampal lysate showing specific immunolabeling of the ~100 kDa GluR1 protein phosphorylated at Ser831 in the first lane (-). Phosphospecificity is shown in the second lane (+) where immunolabeling is completely eliminated by blot treatment with lambda phosphatase (λ-Ptase, 1200 units for 30 min).
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SKU: p1160-831
Ships: 1-2 business days
Product Details
GluR1-Subunit (Ser831)
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. GluR1 is potentiated by phosphorylation at Ser-831 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 as learning and memory (Soderling and Derkach, 2000).
Antigen Affinity Purified from Pooled Serum
Polyclonal
IgG
ELISA, WB
Rabbit
GRIA1
100 kDa
Synthetic phospho-peptide corresponding to amino acid residues surrounding Ser831 of rat GluR1 conjugated to keyhole limpet hemocyanin (KLH).
Rat
Mouse, Rat
Canine, Chicken
AB_2492127
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.
Liquid
Prepared from pooled rabbit serum by affinity purification via sequential chromatography on phospho and non-phosphopeptide affinity columns.
10 mM HEPES (pH 7.5), 150 mM NaCl, 100 µg per ml BSA and 50% glycerol.
WB: 1:1000
WB Brain: 1:1000
WB Brain: 1:1000
Unconjugated
Specific for endogenous levels of the ~100 kDa GluR1 protein phosphorylated at Ser831. Immunolabeling is completely eliminated by treatment with λ-phosphatase.
Phosphorylated
Ser831
Western blots performed on each lot.
For research use only. Not intended for therapeutic or diagnostic use. Use of all products is subject to our terms and conditions, which can be viewed on our website.
After date of receipt, stable for at least 1 year at -20°C.
GLUR 1; GLUR A; AMPA 1; AMPA selective glutamate receptor 1; AMPA-selective glutamate receptor 1; GluA1; GLUH1; GluR K1; GluR-1; GluR-A; GluR-K1; GLUR1; GLURA; GluRK1; Glutamate receptor 1; Glutamate receptor ionotropic AMPA 1; Glutamate receptor ionotropic; Glutamate receptor; ionotropic; Gria1; GRIA1_HUMAN; HBGR1; MGC133252; OTTHUMP00000160643; OTTHUMP00000165781; THUMP00000224241; OTTHUMP00000224242; OTTHUMP00000224243
P19490
UniProt Summary: Ionotropic glutamate receptor that functions as a ligand-gated cation channel, gated by L-glutamate and glutamatergic agonists such as alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid (AMPA), quisqualic acid, and kainic acid (PubMed:1311100, PubMed:20805473, PubMed:21172611, PubMed:28628100, PubMed:35675825). 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 upon entry of monovalent and divalent cations such as sodium and calcium. The receptor then desensitizes rapidly and enters in a transient inactive state, characterized by the presence of bound agonist (By similarity). In the presence of CACNG2 or CACNG4 or CACNG7 or CACNG8, shows resensitization which is characterized by a delayed accumulation of current flux upon continued application of L-glutamate (PubMed:21172611). Resensitization is blocked by CNIH2 through interaction with CACNG8 in the CACNG8-containing AMPA receptors complex (PubMed:21172611). Calcium (Ca(2+)) permeability depends on subunits composition and, heteromeric channels containing edited GRIA2 subunit are calcium-impermeable. Also permeable to other divalents cations such as strontium(2+) and magnesium(2+) and monovalent cations such as potassium(1+) and lithium(1+) (By similarity). {ECO:0000250|UniProtKB:P19490, ECO:0000269|PubMed:1311100, ECO:0000269|PubMed:20805473, ECO:0000269|PubMed:21172611, ECO:0000269|PubMed:28628100, ECO:0000269|PubMed:35675825}.
UniProt Summary: Ionotropic glutamate receptor that functions as a ligand-gated cation channel, gated by L-glutamate and glutamatergic agonists such as alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid (AMPA), quisqualic acid, and kainic acid (PubMed:1311100, PubMed:20805473, PubMed:21172611, PubMed:28628100, PubMed:35675825). 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 upon entry of monovalent and divalent cations such as sodium and calcium. The receptor then desensitizes rapidly and enters in a transient inactive state, characterized by the presence of bound agonist (By similarity). In the presence of CACNG2 or CACNG4 or CACNG7 or CACNG8, shows resensitization which is characterized by a delayed accumulation of current flux upon continued application of L-glutamate (PubMed:21172611). Resensitization is blocked by CNIH2 through interaction with CACNG8 in the CACNG8-containing AMPA receptors complex (PubMed:21172611). Calcium (Ca(2+)) permeability depends on subunits composition and, heteromeric channels containing edited GRIA2 subunit are calcium-impermeable. Also permeable to other divalents cations such as strontium(2+) and magnesium(2+) and monovalent cations such as potassium(1+) and lithium(1+) (By similarity). {ECO:0000250|UniProtKB:P19490, ECO:0000269|PubMed:1311100, ECO:0000269|PubMed:20805473, ECO:0000269|PubMed:21172611, ECO:0000269|PubMed:28628100, ECO:0000269|PubMed:35675825}.
50592
Blue Ice
- Western Blot Protocol: Download

