Key Specifications Table
|Species Reactivity||Key Applications||Host||Format||Antibody Type|
|R||WB||Rb||Affinity Purified||Polyclonal Antibody|
|Description||Anti-NMDAR2B Antibody, phosphoTyr 1472|
|Presentation||Affinity purified immunoglobulin. Liquid in 10 mM HEPES (pH 7.5), 150 mM NaCl with 100 μg/mL BSA, 50% glycerol and 0.09% sodium azide.|
|Application||Anti-NMDAR2B Antibody, phosphoTyr 1472 is an antibody against NMDAR2B for use in WB.|
|Application Notes||Western blot: 1:1,000
Optimal working dilutions must be determined by the end user.
|Safety Information according to GHS|
|Storage and Shipping Information|
|Storage Conditions||Maintain at -20°C in undiluted for up to 6 months after date of receipt. Avoid repeated freeze/thaw cycles. Do not store in a self defrosting freezer.|
|Material Size||100 µL|
|Reference overview||Pub Med ID|
|A polyamine-deficient diet prevents oxaliplatin-induced acute cold and mechanical hypersensitivity in rats. |
Ferrier, J; Bayet-Robert, M; Pereira, B; Daulhac, L; Eschalier, A; Pezet, D; Moulinoux, JP; Balayssac, D
PloS one 8 e77828 2013
Oxaliplatin is an anticancer drug used for the treatment of advanced colorectal cancer, but it can also cause painful peripheral neuropathies. The pathophysiology of these neuropathies has not been yet fully elucidated, but may involve spinal N-methyl-D-aspartate (NMDA) receptors, particularly the NR2B subunit. As polyamines are positive modulators of NMDA-NR2B receptors and mainly originate from dietary intake, the modulation of polyamines intake could represent an interesting way to prevent/modulate neuropathic pain symptoms by opposing glutamate neurotransmission.The effect of a polyamine deficient diet was investigated in an animal model of oxaliplatin-induced acute pain hypersensitivity using behavioral tests (mechanical and cold hypersensitivity). The involvement of spinal glutamate neurotransmission was monitored by using a proton nuclear magnetic resonance spectroscopy based metabolomic approach and by assessing the expression and phosphorylation of the NR2B subunit of the NMDA receptor.A 7-day polyamine deficient diet totally prevented oxaliplatin-induced acute cold hypersensitivity and mechanical allodynia. Oxaliplatin-induced pain hypersensitivity was not associated with an increase in NR2B subunit expression or phosphorylation, but with an increase of glutamate level in the spinal dorsal horn which was completely prevented by a polyamine deficient diet. As a validation that the oxaliplatin-induced hypersensitivity could be due to an increased activity of the spinal glutamate system, an intrathecal administration of the specific NR2B antagonist, ifenprodil, totally reversed oxaliplatin-induced mechanical and cold hypersensitivity.A polyamine deficient diet could represent a promising and valuable nutritional therapy to prevent oxaliplatin-induced acute pain hypersensitivity.
|cAMP-dependent protein kinase activated Fyn in spinal dorsal horn to regulate NMDA receptor function during inflammatory pain. |
Hong-Bin Yang,Xian Yang,Jing Cao,Shuai Li,Yan-Ni Liu,Zhan-Wei Suo,Hong-Bin Cui,Zhong Guo,Xiao-Dong Hu
Journal of neurochemistry 116 2011
ABSTRACT: Selective inhibition of GluN2B-containing NMDA receptor (GluN2BR) in spinal dorsal horn effectively alleviates inflammatory pain, suggesting the up-regulation of GluN2BR function involved in central sensitization. Previous studies have demonstrated that the increase in GluN2BR synaptic expression serves as a key step to enhance GluN2BR function after intradermal injection of Complete Freund's Adjuvant (CFA). Here, we showed that cAMP-dependent protein kinase (PKA) played an important role in redistributing GluN2BR at synapses, because inhibition of PKA activity impaired GluN2BR accumulation at post-synaptic density (PSD)-enriched fraction in CFA-injected mice, and direct stimulation of PKA in naïve mice mimicked the effect of CFA by recruiting GluN2BR at PSD fraction to evoke pain sensitization. Analysis of PKA-initiated signalings unraveled that PKA was able to activate Src-family protein tyrosine kinases member Fyn, possibly by disrupting Fyn association with its inhibitory partner striatal-enriched protein tyrosine phosphatase 61. The active Fyn then promoted GluN2B phosphorylation at Tyr1472, a molecular event known to prevent GluN2BR endocytosis. As a result, pharmacological or genetic manipulation of Fyn activity greatly depressed GluN2BR accumulation at PSD-enriched fraction and ameliorated mechanical allodynia induced by PKA. Our data thus elucidated a critical role of PKA/Fyn/GluN2B signaling in triggering GluN2BR hyperfunction and pain hypersensitivity.
|Pathways and Biomarkers of Glutamatergic Synapse Flyer (EMD)|
|RABBIT ANTI-NMDAR2B phosphoTyr1472 AFFINITY PURIFIED POLYCLONAL ANTIBODY|