Recombinant Mouse NMDAR1 Protein Standard
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Recombinant Mouse NMDAR1 Protein Standard is a Mouse Fragment protein, expressed in HEK 293 cells, with >80%, suitable for SDS-PAGE, sELISA.
View Alternative Names
Glurz1, Grin1, GluN1, Glutamate [NMDA] receptor subunit zeta-1, N-methyl-D-aspartate receptor subunit NR1, NMD-R1
- sELISA
Supplier Data
Sandwich ELISA - Recombinant Mouse NMDAR1 Protein Standard (AB316701)
Sandwich ELISA with the capture antibody dilution at 2 µg/mL and detector antibody dilution at 0.5 µg/mL.
- SDS-PAGE
Supplier Data
SDS-PAGE - Recombinant Mouse NMDAR1 Protein Standard (AB316701)
SDS-PAGE analysis of ab316701 under reducing conditions for 2ug protein.
Reactivity data
Product details
While the standard is the same as the one provided in the corresponding SimpleStep ELISA Kit, it cannot be treated as the consumable provided with our SimpleStep ELISA Kit due to differences in its concentration calibration.
Abcam guarantee that this protein standard is suitable for use in a sandwich ELISA. Individual results may vary due to differences in technique, laboratory equipment, buffers, and other experimental factors. The detection range provided for this protein standard is based on initial sandwich ELISA validation data.
The protein concentration is the concentration after validation on our sandwich ELISA platform. This Standard protein is guaranteed to work with our Capture and Detector antibodies in sELISA. Please contact our Scientific Support team to know which antibody pair is suitable for this protein.
Sequence info
Properties and storage information
Shipped at conditions
Appropriate short-term storage conditions
Appropriate long-term storage conditions
Aliquoting information
Storage information
Supplementary information
This supplementary information is collated from multiple sources and compiled automatically.
Biological function summary
NMDA receptors including the NMDAR1 subunit serve essential functions in synaptic plasticity and memory processes. As part of the receptor complex NMDAR1 contributes to the control of synaptic strength. It requires co-activation by glutamate and glycine or D-serine linking its function to excitatory neurotransmission. The receptor's capacity to modulate synaptic connections forms the basis of learning and long-term memory.
Pathways
NMDAR1 plays a critical role in the glutamatergic pathway influencing synaptic plasticity and memory function. It interacts with other proteins like PSD-95 within the postsynaptic density. NMDAR1 is also involved in the calcium signaling pathway due to its ability to facilitate calcium entry into neurons upon synaptic activity. This positions the receptor as an important modulator in pathways that control neuronal communication and plasticity.
Specifications
Form
Liquid
General info
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 : 12008020, PubMed : 12860921, PubMed : 14602821, PubMed : 1532151, PubMed : 8060614, PubMed : 9049108). NMDARs participate in synaptic plasticity for learning and memory formation by contributing to the long-term potentiation (LTP) (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 : 12008020, PubMed : 1532151, PubMed : 7790891, PubMed : 8060614). NMDARs mediate simultaneously the potassium efflux and the influx of calcium and sodium (PubMed : 12860921). Each GluN2 or GluN3 subunit confers differential attributes to channel properties, including activation, deactivation and desensitization kinetics, pH sensitivity, Ca2(+) permeability, and binding to allosteric modulators (PubMed : 12008020, PubMed : 14602821).
Sequence similarities
Belongs to the glutamate-gated ion channel (TC 1.A.10.1) family. NR1/GRIN1 subfamily.
Post-translational modifications
NMDA is probably regulated by C-terminal phosphorylation of an isoform of GRIN1 by PKC. Dephosphorylated on Ser-897 probably by protein phosphatase 2A (PPP2CB). Its phosphorylated state is influenced by the formation of the NMDAR-PPP2CB complex and the NMDAR channel activity.
Target data
Product promise
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