![Figure 1. Agonist-induced Serine363 phosphorylation of the δ-Opioid receptor. Upper panel, HEK293 cells stably expressing the δ-Opioid Receptor (DOP) were either not exposed or exposed to 10 μM DPDPE ([D-Pen2,D-Pen5]-enkephalin) or 0.1 μM PMA (Phorbol 12-Myristate 13-Acetate) for 30 minutes. Cells were lysed and immunoblotted with the anti-pS363-DOP antibody (7TM0317B) at a dilution of 1:1000. Lower panel, blot was stripped and reprobed with a phosphorylation-independent anti-DOP antibody to confirm equal loading of the gel.](https://resource.amerigoscientific.com/p-img/pS363-DOP-DP-F1.png)
![Figure 3. Immunocytochemical identification of Serine363 phosphorylation of the δ-Opioid Receptor. HEK293 cells stably expressing the δ-Opioid Receptor (DOP) were either not exposed or exposed to 10 μM DPDPE ([D-Pen2,D-Pen5]-enkephalin) for 2, 5 or 30 min and immunocytochemically stained with the anti-pS363-DOP antibody (7TM0317B) at a dilution of 1:200. Note, Serine363-phosphorylated DOP receptors were not detectable in untreated cells (0 min). Serine363-phosphorylated DOP receptors were seen at the plasma membrane (2 min) and with increased time of stimulation (5 and 30 min) as perinuclear clusters.](https://resource.amerigoscientific.com/p-img/pS363-DOP-DP-F3.png)
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Overview
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Serine363 (S363) is the primary phosphorylation site in a hierarchical phosphorylation cascade of the delta-opioid receptor (DOP). The pS363-DOP antibody detects phosphorylation in response to high- and low-efficacy agonists but not after PKC activation. S363 phosphorylation is a key regulator of DOP desensitization, β-arrestin recruitment and internalization. The pS363-DOP antibody can detect phosphorylated DOP in mouse brain in vivo. The pS363-DOP antibody can by used for detection of the subcellular location of phosphorylated DOP by immunocytochemistry.
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