|Reactivity||Human, Mouse, Rat|
|Calculated MW||112125 Da|
|Homology||Human, mouse - identical.|
|Other Names||Glutamate receptor ionotropic, delta-1, GluD1, GluR delta-1 subunit, Grid1|
|Related products for control experiments||Control peptide antigen (supplied with the antibody free of charge).|
|Target/Specificity||Peptide (C)KDMRKLATWDSEK, corresponding to amino acid residues 407-419 of rat GluD1 (Accession Q62640). Extracellular, N-terminus.|
|Peptide Confirmation||Confirmed by mass-spectrography and amino acid analysis.|
|Format||Affinity purified antibody, lyophilized powder|
|Reconstitution||50 µl or 0.2 ml deionized water, depending on the sample size.|
|Antibody Concentration After Reconstitution||0.8 mg/ml.|
|Storage Before Reconstitution||Lyophilized powder can be stored intact at room temperature for several weeks. For longer periods, it should be stored at -20°C.|
|Storage After Reconstitution||The reconstituted solution can be stored at 4ºC for up to 2 weeks. For longer periods, small aliquots should be stored at -20ºC or below. Avoid multiple freezing and thawing. The further dilutions should be made using a carrier protein such as BSA (1%). Centrifuge all antibody preparations before use (10000 × g 5 min).|
|Control Antigen Storage Before Reconstitution||Lyophilized powder can be stored intact at room temperature for several weeks. For longer periods, it should be stored at -20°C.|
|Control Antigen Reconstitution||100 µl DDW.|
|Control Antigen Storage After Reconstitution||-20ºC.|
|Preadsorption Control||1 µg peptide per 1 µg antibody.|
|Formulation||Lyophilized powder. Reconstituted antibody contains phosphate buffered saline (PBS), pH 7.4, 1% BSA, 0.05% NaN3.|
Thousands of laboratories across the world have published research that depended on the performance of antibodies from Abgent to advance their research. Check out links to articles that cite our products in major peer-reviewed journals, organized by research category.
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Provided below are standard protocols that you may find useful for product applications.
Excitatory neurotransmission in the vertebrate central nervous system is mainly mediated by ionotropic glutamate receptors (iGluRs). Molecular cloning identified 18 mammalian iGluR subunits, of which only 16 sort into the traditional pharmacological subfamilies of AMPA, kainate (KA), and N-methyl-D-aspartate (NMDA) receptors. The 2 remaining subunits were termed “orphan” receptors, “glutamate-like” receptors, “nonionotropic” receptors, or, most commonly, delta receptors1. Ionotropic glutamate receptors are integral membrane proteins composed of four large subunits that form a central ion channel pore. Sequence similarity among all known glutamate receptor subunits, including the δ receptors, suggests they share a similar architecture. Glutamate receptor subunits are modular structures that contain four discrete semiautonomous domains: the extracellular amino-terminal domain (ATD), the extracellular ligand-binding domain (LBD), the transmembrane domain (TMD), and an intracellular carboxyl-terminal domain (CTD)2. The delta family of ionotropic glutamate receptors (iGluRs) consists of the glutamate δ1 (GluD1) and glutamate δ2 (GluD2) receptors3. GluD1 is highly expressed in the inner hair cells of the organ of Corti4, diffusely expressed throughout the forebrain during development with high levels in the hippocampus during adulthood3. Deletion of GluD1 leads to a deficit in high frequency hearing in mice5. Genetic association studies have established the GRID1 gene, which codes for GluD1, is a strong candidate gene for schizophrenia, bipolar disorder, and major depressive disorder6. Copy number variation studies have also implicated GRID1 in autism spectrum disorder (ASD)7. In addition, GRID1 gene is localized to the 10q22–q23 genomic region which is a site for recurrent deletions associated with cognitive and behavioral abnormalities8.
References 1. Schmid, S. M. et al. (2009) Proc. Natl. Acad. Sci. U.S.A. 106, 10320. 2. Traynelis, S.F. et al. (2010) Pharmacol. Rev. 62, 405. 3. Lomeli, H. et al. (1993) FEBS Lett. 315, 318. 4. Safieddine, S. and Wenthold, R.J. (1997) J. Neurosci. 17, 7523. 5. Gao, J. et al. (2007) Mol. Cell Biol. 27, 4500. 6. Treutlein, J. et al. (2009) Schizophr. Res. 111, 123. 7. Smith, M. et al. (2009) Ann N Y Acad Sci 1151, 102. 8. Balciuniene, J. et al. (2007) Am. J. Hum. Genet. 80, 938.
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