|Reactivity||Human, Mouse, Rat|
|Product Name||Anti-NMDAR2B/GRIN2B Antibody|
|Storage & Handling||At -20°C for one year. After reconstitution, at 4°C for one month. It can also be aliquotted and stored frozen at -20°C for a longer time.Avoid repeated freezing and thawing.|
|Description||Rabbit IgG polyclonal antibody for Glutamate receptor ionotropic, NMDA 2B(GRIN2B) detection. Tested with WB in Human;Mouse;Rat.|
|Cite This Product||Anti-NMDAR2B/GRIN2B Antibody (Boster Biological Technology, Pleasanton CA, USA, Catalog # PA1059)|
|Contents/Buffer||Each vial contains 5mg BSA, 0.9mg NaCl, 0.2mg Na2HPO4, 0.05mg Thimerosal, 0.05mg NaN3.|
|Immunogen||A synthetic peptide corresponding to a sequence at the C-terminus of human NMDAR2B(1131-1146aa, DFYLDQFRTKENSPHW), identical to the related mouse and rat sequence.|
|Reactivity||Human, Mouse, Rat|
Assay Dilutions Overview
Western blot, 0.1-0.5μg/ml, Mouse, Rat, Human
Boster's Secondary Antibodies And IHC, WB Kits
The following reagents are used to generate the images below.Boster recommends Enhanced Chemiluminescent Kit with anti-Rabbit IgG (EK1002) for Western blot.
Images And Assay Conditions
Anti-NMDAR2B antibody, PA1059, Western blotting
Lane 1: Rat Brain Tissue Lysate
Lane 2: Rat Brain Tissue Lysate
Lane 3: Mouse Brain Tissue Lysate
Lane 4: Mouse Brain Tissue Lysate
Protein Target Info (Source: Uniprot.org)
|Protein Name||Glutamate receptor ionotropic, NMDA 2B|
|Tissue Specificity||Primarily found in the fronto-parieto-temporal cortex and hippocampus pyramidal cells, lower expression in the basal ganglia. .|
|Alternative Names||Glutamate receptor ionotropic, NMDA 2B;GluN2B;Glutamate [NMDA] receptor subunit epsilon-2;N-methyl D-aspartate receptor subtype 2B;NMDAR2B;NR2B;N-methyl-D-aspartate receptor subunit 3;NR3;hNR3;GRIN2B;NMDAR2B;|
|Subcellular Localization||Cell membrane; Multi-pass membrane protein. Cell junction, synapse, postsynaptic cell membrane; Multi-pass membrane protein.|
|Molecular Weight||166367 MW|
*if product is indicated to react with multiple species, protein info is based on the human gene.
|Protein Function||NMDA receptor subtype of glutamate-gated ion channels with high calcium permeability and voltage-dependent sensitivity to magnesium. Mediated by glycine. In concert with DAPK1 at extrasynaptic sites, acts as a central mediator for stroke damage. Its phosphorylation at Ser-1303 by DAPK1 enhances synaptic NMDA receptor channel activity inducing injurious Ca2+ influx through them, resulting in an irreversible neuronal death (By similarity). .|
|Research Areas||Ligand-Gated Ion Channels, Neurodegenerative Disease, Neurology Process, Neuroscience, Neurotransmission, Receptors / Channels, Sensory System
*You can search these to find other products in these research areas.
|Background||The N-methyl-D-aspartate receptor 2B, also names as GRIN2B. The sequence of the predicted 1,484-amino acid human protein is 98% and 96% identical to the sequences of the rat and mouse Nmdar2b proteins, respectively. Nmdar2B gene is located on mouse chromosome 6 between Rho and Ly49 centromerically and Glb telomerically. Mapping of the human NMDAR2B receptor subunit gene(GRIN2B) to chromosome 12p12 overexpression of NMDA receptor 2B(NR2B) in the forebrains of transgenic mice leads to enhanced activation of NMDA receptors, facilitating synaptic potentiation in response to stimulation at 10-100 Hz.|
Other Recommended Resources
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1. Post-translational modification:phosphorylation, methylation, glycosylation etc. These modifications prevent SDS molecules from binding to the target protein and thus make the band size appear larger than expected
2. Post-translational cleavage: this can cause smaller bands and or multiple bands
3. Alternative splicing: the same gene can have alternative splicing patterns generating different size proteins, all with reactivities to the antibody.
4. Amino Acid R chain charge: SDS binds to positive charges. The different size and charge of the Amino Acid side chains can affect the amount of SDS binding and thus affect the observed band size.
5. Multimers: Multimers are usually broken up in reducing conditions. However if the interactions between the multimers are strong, the band may appear higher.,