Glutamate receptor 3 (GRIA3) Recombinant Protein | GRIA3 recombinant protein

Recombinant Human Glutamate receptor 3 (GRIA3), partial

Cat. Num. AAA951465

• Gene Names: GRIA3; GLUR3; GLURC; GluA3; MRX94; GLUR-C; GLUR-K3
• Purity: Greater or equal to 85% purity as determined by SDS-PAGE.
• Synonyms: Glutamate receptor 3 (GRIA3); Recombinant Human Glutamate receptor 3 (GRIA3); partial; AMPA-selective glutamate receptor 3; GluR-C; GluR-K3; Glutamate receptor ionotropic; AMPA 3; GluA3; GRIA3 recombinant protein

• Host: E Coli or Yeast or Baculovirus or Mammalian Cell
• Purity/Purification: Greater or equal to 85% purity as determined by SDS-PAGE.
• Form/Format: Lyophilized or liquid (Format to be determined during the manufacturing process)
• Sequence Positions: 151-250aa; Partial
• Sequence: SLLGHYKWEKFVYLYDTERGFSILQAIMEAAVQNNWQVTARSVGNIKDVQEFRRIIEEMDRRQEKRYLIDCEVERINTILEQVVILGKHSRGYHYMLANL

• Preparation and Storage: Store at -20 degree C, for extended storage, conserve at -20 degree C or -80 degree C.

SDS-PAGE

Related Product Information for GRIA3 recombinant protein

Receptor for glutamate that functions as ligand-gated ion channel in the central nervous system and plays an important role in excitatory synaptic transmission. 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 chical signal to an electrical impulse. The receptor then desensitizes rapidly and enters a transient inactive state, characterized by the presence of bound agonist. In the presence of CACNG4 or CACNG7 or CACNG8, shows resensitization which is characterized by a delayed accumulation of current flux upon continued application of glutamate.

Product Categories/Family for GRIA3 recombinant protein

Neuroscience

References

Human glutamate receptor hGluR3 flip and flop isoforms cloning and sequencing of the cDNAs and primary structure of the proteins.Rampersad V., Elliott C.E., Nutt S.L., Foldes R.L., Kamboj R.K.Biochim. Biophys. Acta 1219:563-566(1994) McLaughlin D.P., Kerwin R.W. Characterization of the human glutamate receptor subunit 3 gene (GRIA3) , a candidate for bipolar disorder and nonspecific X-linked mental retardation.Gecz J., Barnett S., Liu J., Hollway G., Donnelly A., Eyre H., Eshkevari H.S., Baltazar R., Grunn A., Nagaraja R., Gilliam C., Peltonen L., Sutherland G.R., Baron M., Mulley J.C.Genomics 62:356-368(1999) Candidate gene analysis in Rett syndrome and the identification of 21 SNPs in Xq.Amir R., Dahle E.J., Toriolo D., Zoghbi H.Y.3.3.CO;2-N>Am. J. Med. Genet. 90:69-71(2000) The DNA sequence of the human X chromosome.Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C., Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.Nature 434:325-337(2005)

NCBI and Uniprot Product Information

• NCBI GI #: 163659858
• NCBI GeneID: 2892
• NCBI Accession #: NP_000819.3
• NCBI GenBank Nucleotide #: NM_000828.4
• UniProt Accession #: P42263; Q4VXD5; Q4VXD6; Q9HDA0; Q9HDA1; Q9HDA2; Q9P0H1; D3DTF1
• Molecular Weight: 14 kDa
• NCBI Official Full Name: glutamate receptor 3 isoform 2
• NCBI Official Synonym Full Names: glutamate ionotropic receptor AMPA type subunit 3
• NCBI Official Symbol: GRIA3
• NCBI Official Synonym Symbols: GLUR3; GLURC; GluA3; MRX94; GLUR-C; GLUR-K3
• NCBI Protein Information: glutamate receptor 3
• UniProt Protein Name: Glutamate receptor 3
• Protein Family: Glutamate receptor
• UniProt Gene Name: GRIA3
• UniProt Synonym Gene Names: GLUR3; GLURC; GluR-3; GluA3
• UniProt Entry Name: GRIA3_HUMAN

NCBI Description

Glutamate receptors are the predominant excitatory neurotransmitter receptors in the mammalian brain and are activated in a variety of normal neurophysiologic processes. These receptors are heteromeric protein complexes composed of multiple subunits, arranged to form ligand-gated ion channels. The classification of glutamate receptors is based on their activation by different pharmacologic agonists. The subunit encoded by this gene belongs to a family of AMPA (alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionate)-sensitive glutamate receptors, and is subject to RNA editing (AGA->GGA; R->G). Alternative splicing at this locus results in different isoforms, which may vary in their signal transduction properties. [provided by RefSeq, Jul 2008]

Uniprot Description

GluR3: an integral membrane protein belonging to the glutamate-gated ion channel family. L-glutamate (Glu) acts as an excitatory neurotransmitter at many synapses in the central nervous system. Glutamate receptors are heteromeric protein complexes with multiple subunits, each possessing transmembrane regions, and all arranged to form a ligand-gated ion channel. The postsynaptic actions of Glu are mediated by a variety of receptors that are named according to their selective agonists. Interacts with protein kinase C-alpha binding protein. Each of the four GluR proteins (GRIA1-4) include flip and flop isoforms generated by alternative RNA splicing.

Protein type: Membrane protein, multi-pass; Channel, ligand-gated; Membrane protein, integral

Chromosomal Location of Human Ortholog: Xq25

Cellular Component: asymmetric synapse; cell junction; dendritic shaft; dendritic spine; nucleoplasm; perikaryon; plasma membrane; postsynaptic density; postsynaptic membrane; terminal button

Molecular Function: alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionate selective glutamate receptor activity; extracellular-glutamate-gated ion channel activity

Biological Process: glutamate signaling pathway; ionotropic glutamate receptor signaling pathway; synaptic transmission; transport

Disease: Mental Retardation, X-linked, Syndromic, Wu Type