Glutamate Receptor, Ionotropic, N-Methyl D-Aspartate 2a (GRIN2A) (2nd Cytoplasmic Domain) antibody

Antigen: Glutamate Receptor, Ionotropic, N-Methyl D-Aspartate 2a (GRIN2A)

Synonyms: GRIN2A, NMDAR2A, NR2A, nr2a

Binding Site: 2nd Cytoplasmic Domain

Clonality: Polyclonal

Host: Rabbit

Reactivity: Please enquire

Conjugate: Un-conjugated

Application: Immunohistochemistry (IHC), Western Blotting (WB)

Catalog no.: ABIN350518

Additional Information

Alternative name: NMDAR2A (GRIN2A)

UniProt: Q12879

Immunogen: A synthetic peptide from the 2d cytoplasmic domain of human NMDAR2A (GRIN2A) conjugated to an immunogenic carrier protein was used as the immunogen.

Format: Lyophilized

Isotype: IgG

Description: FUNCTION: NMDA receptor subtype of glutamate-gated ion channels possesses high calcium permeability and voltage-dependent sensitivity to magnesium. Activation requires binding of agonist to both types of subunits. Subcellular location: Cell membrane; Multi-pass membrane protein. Cell junction › synapse › postsynaptic cell membrane; Multi-pass membrane protein. Also known as: GRIN2A, Glutamate receptor subunit epsilon-1, Glutamate [NMDA] receptor subunit epsilon-1, N-methyl D-aspartate receptor subtype 2A, NMDE1, NR2A.

Specificity: Appears to be specific for NMDAR2A.

Application Details

Application Notes: IHC, WB. A concentration of 10-50 µg/ml is recommended. The optimal concentration should be determined by the end user. Not yet tested in other applications.

Purity: IgG

Purification: The antibody is affinity-purified from rabbit antiserum by affinity chromatography using epitope-specific phosphopeptide. The antibody against non-phosphopeptide is removed by chromatography using non-phosphopeptide corresponding to the phosphorylation site.

Storage: Maintain the lyophilised/reconstituted antibodies frozen at -20°C for long term storage and refrigerated at 2-8°C for a shorter term. When reconstituting, glycerol (1:1) may be added for an additional stability. Avoid freeze and thaw cycles.

Restrictions: For Research Use only

Publications

Foldes, Adams, Fantaske et al.: "Human N-methyl-D-aspartate receptor modulatory subunit hNR2A: cloning and sequencing of the cDNA and primary structure of the protein." in: Biochimica et biophysica acta, Vol. 1223, Issue 1, pp. 155-9, 1994 (PubMed).

Hess, Daggett, Crona et al.: "Cloning and functional characterization of human heteromeric N-methyl-D-aspartate receptors." in: The Journal of pharmacology and experimental therapeutics, Vol. 278, Issue 2, pp. 808-16, 1996 (PubMed).

Olsen, Blagoev, Gnad et al.: "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." in: Cell, Vol. 127, Issue 3, pp. 635-48, 2006 (PubMed).

Munton, Tweedie-Cullen, Livingstone-Zatchej et al.: "Qualitative and quantitative analyses of protein phosphorylation in naive and stimulated mouse synaptosomal preparations." in: Molecular & cellular proteomics : MCP, Vol. 6, Issue 2, pp. 283-93, 2007 (PubMed).

Molina, Horn, Tang et al.: "Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry." in: Proceedings of the National Academy of Sciences of the United States of America, Vol. 104, Issue 7, pp. 2199-204, 2007 (PubMed).