Recombinant Human Glutamate receptor 3 | MyBioSource MBS951465 product information

product summary

company name :

MyBioSource

product type :

protein

product name :

Recombinant Human Glutamate receptor 3

catalog :

MBS951465

quantity :

0.05 mg (E-Coli)

price :

190 USD

more info or order :

MyBioSource product webpage

product information

catalog number :

MBS951465

products type :

Recombinant Protein

products full name :

Recombinant Human Glutamate receptor 3

products short name :

Glutamate receptor 3

products name syn :

AMPA-selective glutamate receptor 3; GluR-C; GluR-K3; Glutamate receptor ionotropic, AMPA 3; GluA3

other names :

glutamate receptor 3 isoform 2; Glutamate receptor 3; glutamate receptor 3; glutamate ionotropic receptor AMPA type subunit 3; AMPA-selective glutamate receptor 3; GluR-C; GluR-K3; Glutamate receptor ionotropic, AMPA 3; GluA3

products gene name :

GRIA3

other gene names :

GRIA3; GRIA3; GLUR3; GLURC; GluA3; MRX94; GLUR-C; GLUR-K3; GLUR3; GLURC; GluR-3; GluA3

uniprot entry name :

GRIA3_HUMAN

host :

E Coli or Yeast or Baculovirus or Mammalian Cell

sequence positions :

151-250

sequence length :

894

sequence :

SLLGHYKWEKFVYLYDTERGFSILQAIMEAAVQNNWQVT
ARSVGNIKDVQEFRRIIEEMDRRQEKRYLIDCEVERINT
ILEQVVILGKHSRGYHYMLANL

purity :

Greater than 90% as determined by SDS-PAGE.

form :

Liquid containing glycerol; lyophilization may be available upon request.

storage stability :

Store at -20 degree C, for extended storage, conserve at -20 degree C or -80 degree C.

products categories :

Neuroscience

products description :

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.

products 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 gi num :

163659858

ncbi acc num :

NP_000819.3

ncbi gb acc num :

NM_000828.4

uniprot acc num :

P42263

ncbi mol weight :

27.97kD

ncbi pathways :

Activation Of AMPA Receptors Pathway (1268797); Activation Of NMDA Receptor Upon Glutamate Binding And Postsynaptic Events Pathway (1268798); Amphetamine Addiction Pathway (547607); Amphetamine Addiction Pathway (550546); BDNF Signaling Pathway (712093); Circadian Entrainment Pathway (698773); Circadian Entrainment Pathway (699872); Dopaminergic Synapse Pathway (469199); Dopaminergic Synapse Pathway (469185); Glutamate Binding, Activation Of AMPA Receptors And Synaptic Plasticity Pathway (1268794)

ncbi summary :

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- 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 summary :

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

size1 :

0.05 mg (E-Coli)

price1 :

190 USD

size2 :

0.05 mg (Yeast)

price2 :

190

size3 :

0.2 mg (E-Coli)

price3 :

460

size4 :

0.2 mg (Yeast)

price4 :

460

size5 :

0.5 mg (E-Coli)

price5 :

750

more info or order :

MyBioSource product webpage