Foundational characteristics of cancer include proliferation, angiogenesis, migration, evasion of apoptosis, and cellular immortality. Find key markers for these cellular processes and antibodies to detect them.
The SUMOplot™ Analysis Program predicts and scores sumoylation sites in your protein. SUMOylation is a post-translational modification involved in various cellular processes, such as nuclear-cytosolic transport, transcriptional regulation, apoptosis, protein stability, response to stress, and progression through the cell cycle.
The Autophagy Receptor Motif Plotter predicts and scores autophagy receptor binding sites in your protein. Identifying proteins connected to this pathway is critical to understanding the role of autophagy in physiological as well as pathological processes such as development, differentiation, neurodegenerative diseases, stress, infection, and cancer.
GRIN2A Antibody (C-term)
Affinity Purified Rabbit Polyclonal Antibody (Pab)
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Application 
| WB, IHC-P, FC, E |
|---|---|
| Primary Accession | Q12879 |
| Other Accession | Q00959, P35436, NP_001127879.1, NP_000824.1 |
| Reactivity | Human |
| Predicted | Mouse, Rat |
| Host | Rabbit |
| Clonality | Polyclonal |
| Isotype | Rabbit IgG |
| Calculated MW | 165283 Da |
| Antigen Region | 1291-1318 aa |
| Gene ID | 2903 |
|---|---|
| Other Names | Glutamate receptor ionotropic, NMDA 2A, GluN2A, Glutamate [NMDA] receptor subunit epsilon-1, N-methyl D-aspartate receptor subtype 2A, NMDAR2A, NR2A, hNR2A, GRIN2A, NMDAR2A |
| Target/Specificity | This GRIN2A antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 1291-1318 amino acids from the C-terminal region of human GRIN2A. |
| Dilution | WB~~1:1000 IHC-P~~1:50~100 FC~~1:10~50 |
| Format | Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is purified through a protein A column, followed by peptide affinity purification. |
| Storage | Maintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles. |
| Precautions | GRIN2A Antibody (C-term) is for research use only and not for use in diagnostic or therapeutic procedures. |
| Name | GRIN2A (HGNC:4585) |
|---|---|
| Synonyms | NMDAR2A |
| Function | Component of N-methyl-D-aspartate (NMDA) receptors (NMDARs) that function as heterotetrameric, ligand-gated cation channels with high calcium permeability and voltage-dependent block by Mg(2+) (PubMed:20890276, PubMed:23933818, PubMed:23933819, PubMed:23933820, PubMed:24504326, PubMed:26875626, PubMed:26919761, PubMed:28242877, PubMed:36117210, PubMed:38538865, PubMed:8768735). NMDARs participate in synaptic plasticity for learning and memory formation by contributing to the slow phase of excitatory postsynaptic current, long-term synaptic potentiation, and learning (By similarity). Channel activation requires binding of the neurotransmitter L-glutamate to the GluN2 subunit, glycine or D-serine binding to the GluN1 subunit, plus membrane depolarization to eliminate channel inhibition by Mg(2+) (PubMed:23933818, PubMed:23933819, PubMed:23933820, PubMed:24504326, PubMed:26875626, PubMed:26919761, PubMed:27288002, PubMed:28095420, PubMed:28105280, PubMed:28126851, PubMed:28182669, PubMed:29644724, PubMed:38307912, PubMed:8768735). NMDARs mediate simultaneously the potasium efflux and the influx of calcium and sodium (By similarity). Each GluN2 subunit confers differential attributes to channel properties, including activation, deactivation and desensitization kinetics, pH sensitivity, Ca2(+) permeability, and binding to allosteric modulators (PubMed:26875626, PubMed:26919761). Participates in the synaptic plasticity regulation through activation by the L- glutamate releaseed by BEST1, into the synaptic cleft, upon F2R/PAR-1 activation in astrocyte (By similarity). |
| Cellular Location | Cell projection, dendritic spine {ECO:0000250|UniProtKB:Q00959}. Cell membrane; Multi-pass membrane protein. Synapse {ECO:0000250|UniProtKB:P35436} Postsynaptic cell membrane {ECO:0000250|UniProtKB:Q00959}; Multi-pass membrane protein. Cytoplasmic vesicle membrane {ECO:0000250|UniProtKB:P35436}. Note=Expression at the dendrite cell membrane and at synapses is regulated by SORCS2 and the retromer complex. {ECO:0000250|UniProtKB:P35436} |
Thousands of laboratories across the world have published research that depended on the performance of antibodies from Abcepta to advance their research. Check out links to articles that cite our products in major peer-reviewed journals, organized by research category.
info@abcepta.com, and receive a free "I Love Antibodies" mug.
Provided below are standard protocols that you may find useful for product applications.
Background
N-methyl-D-aspartate (NMDA) receptors are a class of ionotropic glutamate-gated ion channels. These receptors have been shown to be involved in long-term potentiation, an activity-dependent increase in the efficiency of synaptic transmission thought to underlie certain kinds of memory and learning. NMDA receptor channels are heteromers composed of the key receptor subunit NMDAR1 (GRIN1) and 1 or more of the 4 NMDAR2 subunits: NMDAR2A (GRIN2A), NMDAR2B (GRIN2B), NMDAR2C (GRIN2C) and NMDAR2D (GRIN2D). Alternatively spliced transcript variants encoding different isoforms have been found for this gene.
References
Endele, S., et al. Nat. Genet. 42(11):1021-1026(2010)
Shimada, M., et al. Hum. Genet. 128(4):433-441(2010)
Saus, E., et al. J Psychiatr Res 44(14):971-978(2010)
Pinheiro, A.P., et al. Am. J. Med. Genet. B Neuropsychiatr. Genet. 153B (5), 1070-1080 (2010) :
King, J.E., et al. Am. J. Pathol. 176(6):2819-2830(2010)
If you have used an Abcepta product and would like to share how it has performed, please click on the "Submit Review" button and provide the requested information. Our staff will examine and post your review and contact you if needed.
If you have any additional inquiries please email technical services at tech@abcepta.com.
Ordering Information
Other Products
Shipping Information
