Recombinant Human Glutamate Receptor 2 (GRIA2) Protein (His&Myc)

Name: Recombinant Human Glutamate Receptor 2 (GRIA2) Protein (His&Myc)
Brand: Beta LifeScience
SKU: BLC-01211P
Availability: InStock

Greater than 85% as determined by SDS-PAGE.

Collections: High-quality recombinant proteins, Other recombinant proteins

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Product Overview

Description	Recombinant Human Glutamate Receptor 2 (GRIA2) Protein (His&Myc) is produced by our E.coli expression system. This is a protein fragment.
Purity	Greater than 85% as determined by SDS-PAGE.
Uniprotkb	P42262
Target Symbol	GRIA2
Synonyms	(GluR-2)(AMPA-selective glutamate receptor 2)(GluR-B)(GluR-K2)(Glutamate receptor ionotropic, AMPA 2)(GluA2)
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-10His&C-Myc
Target Protein Sequence	NSIQIGGLFPRGADQEYSAFRVGMVQFSTSEFRLTPHIDNLEVANSFAVTNAFCSQFSRGVYAIFGFYDKKSVNTITSFCGTLHVSFITPSFPTDGTHPFVIQMRPDLKGALLSLIEYYQWDKFAYLYDSDRGLSTLQAVLDSAAEKKWQVTAINVGNINNDKKDEMYRSLFQDLELKKERRVILDCERDKVNDIVDQVITIGKHVKGYHYIIANLGFTDGDLLKIQFGGANVSGFQIVDYDDSLVSKFIERWSTLEEKEYPGAHTTTIKYTSALTYDAVQVMTEAFRNLRKQRIEISRRGNAGDCLANPAVPWGQGVEIERALKQVQVEGLSGNIKFDQNGKRINYTINIMELKTNGPRKIGYWSEVDKMVVTLTELPSGNDTSGLENKTVVVTTILESPYVMMKKNHEMLEGNERYEGYCVDLAAEIAKHCGFKYKLTIVGDGKYGARDADTKIWNGMVGELVYGKADIAIAPLTITLVREEVIDFSKPFMSLGISIMIKKPQKSKPGVFSFLDPLA
Expression Range	25-543aa
Protein Length	Partial
Mol. Weight	63.3 kDa
Research Area	Neuroscience
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target Function	Receptor for glutamate that functions as ligand-gated ion channel in the central nervous system. It 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 chemical 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. Through complex formation with NSG1, GRIP1 and STX12 controls the intracellular fate of AMPAR and the endosomal sorting of the GRIA2 subunit toward recycling and membrane targeting.
Subcellular Location	Cell membrane; Multi-pass membrane protein. Endoplasmic reticulum membrane; Multi-pass membrane protein. Cell junction, synapse, postsynaptic cell membrane; Multi-pass membrane protein. Cell junction, synapse, postsynaptic density membrane; Multi-pass membrane protein.
Protein Families	Glutamate-gated ion channel (TC 1.A.10.1) family, GRIA2 subfamily
Database References	HGNC: 4572 OMIM: 138247 KEGG: hsa:2891 STRING: 9606.ENSP00000264426 UniGene: PMID: 28608743 Measured the expression of GRIA2 and GABRA1 in patients with methamphetamine-use disorder. Also examined whether miR-181a down-regulates GRIA2 and GABRA1 in a cell-based assay. We further examined the effects of chronic methamphetamine exposure on the expression of miR-181a, GRIA2 and GABRA1. The results demonstrated that serum GRIA2 is higher in patients with methamphetamine-use disorder than in healthy controls. PMID: 27767084 This study demonstrated that a significant decrease in the protein level of GluN2A in major depression disorder. PMID: 27661418 both the intracellular C-terminal domain (CTD) and the loop region between the M1 and M2 helices move during activation and the CTD is detached from the membrane PMID: 27313205 The results of this study suggest that neurons in hypothalamic hamartoma may bear Ca(2+) -permeable AMPA receptors(GluA2 ) due to dislocation of ADAR2 PMID: 28195308 A transient positive feedback mechanism between AMPAR and stargazin has implications for information processing in the brain, because it should allow activity-dependent facilitation of excitatory synaptic transmission through a postsynaptic mechanism. PMID: 26744192 The GluR2 subunit of the AMPA receptor is involved in cell migration and calcium signaling. PMID: 26311781 RAB39B selectively regulates GluA2 trafficking to determine synaptic AMPAR composition PMID: 25784538 GRIA2CCC polymorphism is genetic risk marker for paranoid schizophrenia in Russians.Low risk genetic markers of paranoid schizophrenia were revealed: in Tatars-GRIA2T/T (rs43025506) of GRIA2 gene and GRIA2*CCT in Russians. PMID: 25842862 GRIA2 is a useful marker for distinguishing solitary fibrous tumour from most mimics PMID: 24456377 a link between neurodegenerative processes and deficient RNA editing of the GluA2 Q/R site. PMID: 24679603 Statistical analysis showed no association between migraine and the GRIA2 and GRIA4 polymorphisms investigated. PMID: 24512576 analysis of changes in receptor kinetics with the R628E charge-inverting mutation in the "linker" region of alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid (AMPA) receptor PMID: 24550387 We show that excitatory cortical-patterned neurons derived from multiple human pluripotent stem cell lines exhibit native-like maturation changes in AMPAR composition such that there is an increase in the expression of GluA2(R) subunits. PMID: 24623784 The data potentially suggest a lack of epistatic interaction between GRIA2 and GRIA4 variants regarding clinical outcomes in patients with major depressive disorder. PMID: 23613500 The ionotrophic glutamate receptors AMPA2 and AMPA3 were decreased in hippocampus in patient with multiple sclerosis. PMID: 23595422 ADAR2 expression level reflects editing activity at the GluA2 Q/R site; although the edited GluA2 pre-mRNA is readily spliced, the unedited GluA2 pre-mRNA is also spliced and transported to the cytoplasm when ADAR2 expression is low. PMID: 22366356 Did not observed significant association between GRIA2 polymorphisms and clinical improvement in patients with Major depressive disorder.But rs4302506 and rs4403097 single nucleotide polymorphisms could be associated with age of onset of the disease. PMID: 22057216 We demonstrated that the expression of GRIA2 among the differentially expressed genes provides better prognosis of patients with advanced serous papillary ovarian adenocarcinoma. PMID: 22644307 The balance of expression of nerve growth factor (NGF) and that of its receptors shifts toward cell death mechanisms during the progression of Alzheimer disease. PMID: 21397006 the GluR2 gene is embedded into an open chromatin configuration in glioma cells and expression of GluR2 is controlled by REST and Sp1 PMID: 21948504 SNPs within GRIA2 may not be associated with the development and treatment outcomes in BD PMID: 22122651 significant association GRIA2 polymorphisms was found with the diagnosis of schizophrenia. PMID: 22094384 We conclude that polymorphisms in the GluR2 gene (GRIA2) are not a major contributory factor in the pathogenesis of ALS. PMID: 20409611 Data show that CALM influences the cell surface level of the AMPA receptor subunit GluR2. PMID: 21221849 Gain-of-function glutamate receptor interacting protein 1 variants alter GluA2 recycling and surface distribution in patients with autism PMID: 21383172 Transsynaptic signaling mediated by the extracellular domain of GluR2 regulates the stability of presynaptic terminals. PMID: 21173224 [review] The importance of mGlu2/3 glutamate receptors during normal central nervous system development is likely to play an important mechanistic role in the neurodevelopmental hypothesis of schizophrenia. PMID: 19933774 Post-transcriptional editing of this subunit at the Q/R/N site controls calcium permeability PMID: 11860506 role of interaction with N-ethylmaleimide-sensitive factor in regulation of AMPA receptors by brain-derived neurotrophic factor PMID: 12130635 Low levels of GluR2 mRNA in motoneurons of ALS did not differ from the control group, implying that selective reduction of the GluR2 subunit cannot be a mechanism of AMPA receptor-mediated neurotoxicity in ALS PMID: 12694394 the Q/R site of GluRs editing is regulated in a regional manner and the GluR2 Q/R site editing is critically regulated by ADAR2 in human brain PMID: 12859334 GluR2, a subunit of a ligand-gated cation channel, is up-regulated in leiomyomata relative to myometrium by 15- to 30-fold at the protein and mRNA level and is localized in endothelial cells PMID: 14630051 There is a defect in the editing of the mRNA encoding the GluR2 subunit of glutamate AMPA receptors in the spinal motor neurons of individuals affected by amyotrophic lateral sclerosis PMID: 14985749 R/G editing status: the relative amount of edited GLUR2 mRNA was increased in epileptic hippocampi, whereas no changes were found in neocortical tissues. PMID: 15006707 Control of GLUR2 translation was mediated by a sequence containing a 34-42 nucleotide imperfect GU repeat predicted to form secondary structure in vivo. This translation suppression domain is included in some rat and human GluR2 transcripts in vivo PMID: 15071096 GluR2 was localized to the perikarya and proximal dendrites of BLA neurons; dense labeling was also present over the pyramidal cell layer of hippocampal subfields CA1 and CA3 PMID: 16045445 Circumstance data have indicated that the GluR2 subunits dictate Ca2+/Zn2+ permeability of AMPA receptor channels and gate injurious Ca2+/Zn2+ signals in vulnerable neurons. PMID: 16215279 Laser capture microdissection combined with quantitative PCR was used to examine the expression of AMPA (GRIA1-4) and NMDA (GRIN1, 2A and 2B) subunit mRNA levels in Layer II/III and Layer V pyramidal cells PMID: 17942280 Of the three AMPA genes analyzed here, only GRIA3 seems to be involved in the pathogenesis of schizophrenia, but only in females. PMID: 18163426 utilized reverse-transcription polymerase chain reaction and BbvI digestion to demonstrate that neural progenitor cells contain Q/R-unedited GluR2, and differentiated cells contain Q/R-edited GluR2 subunits PMID: 18403631 the GluR4 subunit exhibits a different correlation between receptor activation and ligand-binding domain cleft closure than does GluR2 PMID: 19102704 These findings indicate that the absence of the GluR2 subunit favours malignancy in gliomas PMID: 19558602 This dimeric structure provides a mechanism for how the ATDs can drive receptor assembly and subtype-restricted composition. PMID: 19651138

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

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