research use only
Cat.No.: F5208
| Dilution |
|---|
|
| Application |
|---|
| WB |
| Reactivity |
|---|
| Mouse, Rat |
| Source |
|---|
| Rabbit Monoclonal Antibody |
| Storage Buffer |
|---|
| PBS, pH 7.2+50% Glycerol+0.05% BSA+0.01% NaN3 |
| Storage (from the date of receipt) |
|---|
| -20°C (avoid freeze-thaw cycles), 2 years |
| Predicted MW |
|---|
| 190 kDa |
| Specificity |
|---|
| Phospho-NMDA Receptor 2B/GluN2B (Ser1303) Antibody [F24J19] detects endogenous levels of total NMDA Receptor 2B/GluN2B protein only when it is phosphorylated at Ser1303. |
| Clone |
|---|
| F24J19 |
| Synonym(s) |
|---|
| Glutamate receptor ionotropic, NMDA 2B; GluN2B; GRIN2B |
| Background |
|---|
| Phospho‑NMDA receptor 2B (GluN2B, NR2B) at Ser1303 marks a key regulatory site on the C‑terminal tail of the GluN2B subunit of the N‑methyl‑D‑aspartate receptor (NMDAR), a heterotetrameric ion channel that couples glutamate and glycine binding to Ca²⁺ and Na⁺ influx in excitatory synapses. GluN2B‑containing receptors assemble with GluN1 or GluN1‑splice variants to form Ca²⁺‑permeable pores whose open probability and single‑channel behavior can be tuned by phosphorylation of the GluN2B C‑tail, including Ser1303, which lies within a region that also docks CaMKII and other signaling proteins. Phosphorylation of Ser1303 on GluN2B is mediated by protein kinase C (PKC) and, in response to excitotoxic or ischemic stimuli, by DAPK1, and this phospho‑switch stabilizes GluN2B‑containing receptor complexes at synaptic and extrasynaptic sites, enhancing Ca²⁺ influx through the channel and promoting prolonged Ca²⁺ signals that support both synaptic plasticity and excessive Ca²⁺ loading that underlies neuronal injury. Ser1303 phosphorylation modulates channel gating and desensitization kinetics, and CaMKII‑dependent phosphorylation of this site further fine‑tunes NMDAR current amplitude and duration, linking NMDAR activity to CaMKII‑driven long‑term potentiation and structural plasticity in learning‑relevant circuits, whereas pharmacological or genetic attenuation of Ser1303 phosphorylation reduces Ca²⁺ overload and confers protection in models of excitotoxicity and stroke. |
| References |
|---|
|
Tel: +1-832-582-8158 Ext:3
If you have any other enquiries, please leave a message.