07-398
Anti-phospho-NR2B (Ser1303) Antibody
Upstate®, from rabbit
Synonym(s):
Anti-DEE27, Anti-GluN2B, Anti-MRD6, Anti-NMDAR2B, Anti-NR2B, Anti-NR3, Anti-hNR3
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About This Item
UNSPSC Code:
12352203
eCl@ss:
32160702
NACRES:
NA.41
Recommended Products
biological source
rabbit
Quality Level
antibody form
purified immunoglobulin
antibody product type
primary antibodies
clone
polyclonal
species reactivity
rat, human, mouse
manufacturer/tradename
Upstate®
technique(s)
western blot: suitable
isotype
IgG
NCBI accession no.
UniProt accession no.
shipped in
dry ice
target post-translational modification
phosphorylation (pSer1303)
Gene Information
human ... GRIN2B(2904)
mouse ... Grin2B(14812)
rat ... Grin2B(24410)
Specificity
Recognizes phospho-NR2B.
Immunogen
Peptide corresponding to amino acids 1297-1309 of human phospho-NR2B
Application
Anti-phospho-NR2B (Ser1303) Antibody detects level of phospho-NR2B (Ser1303) & has been published & validated for use in WB.
Research Category
Neuroscience
Neuroscience
Research Sub Category
Oxidative Stress
Neurodegenerative Diseases
Oxidative Stress
Neurodegenerative Diseases
Quality
routinely evaluated by immunoblot in a rat brain microsomal protein preparation
Target description
~180 kDa
Linkage
Replaces: 04-1148
Physical form
Format: Purified
Protein A Purified immunoglobulin in 30% glycerol, 0.07M Tris-glycine, pH 7.4, 0.105 M NaCl, 0.035% sodium azide as a preservative.
Protein A purified
Storage and Stability
Maintain for 2 years at -20°C from date of shipment. Aliquot to avoid repeated freezing and thawing. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap.
Analysis Note
Control
Brain tissue
Brain tissue
Other Notes
Concentration: Please refer to the Certificate of Analysis for the lot-specific concentration.
Legal Information
UPSTATE is a registered trademark of Merck KGaA, Darmstadt, Germany
Disclaimer
Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
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Storage Class Code
10 - Combustible liquids
WGK
WGK 2
Certificates of Analysis (COA)
Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.
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Substrate-selective and calcium-independent activation of CaMKII by ?-actinin.
Jalan-Sakrikar, N; Bartlett, RK; Baucum, AJ; Colbran, RJ
The Journal of Biological Chemistry null
C Castillo et al.
Neuroscience, 177, 308-320 (2011-01-11)
The involvement of substance P (SP) in neuronal sensitization through the activation of the neurokinin-1-receptor (NK1r) in postsynaptic dorsal horn neurons has been well established. In contrast, the role of SP and NK1r in primary sensory dorsal root ganglion (DRG)
Johanna G Pasek et al.
Molecular and cellular neurosciences, 68, 234-243 (2015-08-10)
Calcium signaling regulates synaptic plasticity and many other functions in striatal medium spiny neurons to modulate basal ganglia function. Ca(2+)/calmodulin-dependent protein kinase II (CaMKII) is a major calcium-dependent signaling protein that couples calcium entry to diverse cellular changes. CaMKII activation
S Strack et al.
The Journal of biological chemistry, 275(31), 23798-23806 (2000-04-15)
Calcium influx through the N-methyl-d-aspartate (NMDA)-type glutamate receptor and activation of calcium/calmodulin-dependent kinase II (CaMKII) are critical events in certain forms of synaptic plasticity. We have previously shown that autophosphorylation of CaMKII induces high-affinity binding to the NR2B subunit of
Sean McKay et al.
Cell reports, 25(4), 841-851 (2018-10-26)
The GluN2 subtype (2A versus 2B) determines biophysical properties and signaling of forebrain NMDA receptors (NMDARs). During development, GluN2A becomes incorporated into previously GluN2B-dominated NMDARs. This "switch" is proposed to be driven by distinct features of GluN2 cytoplasmic C-terminal domains
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