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- Order number: 7TM0318B
- Content: 100 µl
- Host: Rabbit
Threonine363 is a major phosphorylation site of the kappa-opioid receptor (KOP). The pT363-KOP antibody detects phosphorylation in response to high-efficacy agonists. T363 phosphorylation is a key regulator of KOP desensitization, β-arrestin recruitment and internalization.
Alternative Names | KOP, OPRK1, κ-Opioid Receptor |
IUPHAR Target ID | 318 |
UniProt ID | P41145 (human) P33534 (mouse) P34975 (rat) |
Western Blot (WB) | 1:1000 |
Species Reactivity | Human, Mouse, Rat |
Host / Isotype | Rabbit / IgG |
Class | Polyclonal |
Immunogen | A synthetic phosphopeptide derived from human KOP around the phosphorylation site of Thr363 |
Form | Liquid |
Purification | Antigen affinity chromatography |
Storage buffer | Dulbecco's PBS, pH 7.4, with 150 mM NaCl, 0.02% sodium azide |
Storage conditions | short-term 4°C, long-term -20°C |
Figure 1. Agonist-induced Threonine363 phosphorylation of the κ-Opioid Receptor. Upper panel, HEK293 cells stably expressing the κ-Opioid Receptor (KOP) were either not exposed or exposed to 10 μM of selective κ-opioid receptor agonist U50,488H for 30 minutes. Cells were lysed and immunoblotted with the anti-pT363-KOP antibody (7TM0318B) at a dilution of 1:1000. Lower panel, blot was stripped and reprobed with the phosphorylation-independent anti-KOP antibody (7TM0318N-WB) to confirm equal loading of the gel.
Figure 2. Analysis of dose-dependent κ-Opioid Receptor phosphorylation using two phosphosite-specific antibodies. Upper two panels, HEK293 cells stably expressing the κ-Opioid Receptor (KOP) were either not exposed or exposed to increasing concentrations of selective κ-opioid receptor agonist U50,488H ranging from 0.1 nM to 1 μM for 30 minutes. Cells were lysed and immunoblotted with the anti-pS356/pT357-KOP antibody (7TM0318A) or anti-pT363-KOP antibody (7TM0318B) at a dilution of 1:1000. Lower panel, blot was stripped and reprobed with the phosphorylation-independent anti-KOP antibody (7TM0318N-WB) to confirm equal loading of the gel.