pS363-MOP (phospho-µ-Opioid Receptor Antibody)

Preview: Figure 1. Agonist-induced and Agonist-independent Serine363 phosphorylation of the µ-Opioid Receptor

Preview: Figure 2. Analysis of agonist-independent µ-Opioid Receptor phosphorylation using different protein kinase C (PKC) inhibitors.

Figure 1. Agonist-induced and Agonist-independent Serine363 phosphorylation of the µ-Opioid Receptor

Figure 2. Analysis of agonist-independent µ-Opioid Receptor phosphorylation using different protein kinase C (PKC) inhibitors.

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Order number: 7TM0319A
Content: 100 µl
Host: Rabbit

Serine363 (S363) is a constitutive phosphorylation site of the µ-opioid receptor (MOP). The... more

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Serine363 (S363) is a constitutive phosphorylation site of the µ-opioid receptor (MOP). The pT363-MOP antibody detects phosphorylated MOP in cultured cells. S363 is a substrate for PKC-mediated phosphorylation.

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Alternative Names MOP, OPRM1, µ-Opioid Receptor, Mu Receptor IUPHAR... more

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Alternative Names	MOP, OPRM1, µ-Opioid Receptor, Mu Receptor
IUPHAR Target ID	319
UniProt ID	P35372 (human) P42866 (mouse) P33535 (rat)
Western Blot (WB)	1:1000
Species Reactivity	Human, Mouse, Rat
Host / Isotype	Rabbit / IgG
Class	Polyclonal
Immunogen	A synthetic phosphopeptide derived from human MOP around the phosphorylation site of Ser363
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 and Agonist-independent Serine363 phosphorylation of the µ-Opioid... more

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Figure 1. Agonist-induced and Agonist-independent Serine363 phosphorylation of the µ-Opioid Receptor. Upper panel, HEK293 cells stably expressing the µ-Opioid Receptor (MOP) were either not exposed or exposed to 10 μM DAMGO ([D-Ala2,N-MePhe4, Gly-ol]-enkephalin) or 0.1 μM PMA (Phorbol 12-Myristate 13-Acetate) for 30 minutes. Cells were lysed and immunoblotted with the anti-pS363-MOP antibody (7TM0319A) at a dilution of 1:1000. Lower panel, blot was stripped and reprobed with the phosphorylation-independent anti-MOP antibody (7TM0319N-WB) at a dilution of 1:1000 to confirm equal loading of the gel. Note, Serine363 ist phosphorylated under basal conditions.

Figure 2. Analysis of agonist-independent µ-Opioid Receptor phosphorylation using different protein kinase C (PKC) inhibitors. Upper panel, HEK293 cells stably expressing the µ-Opioid Receptor (MOP) were either not exposed or exposed to PKC inhibitors BIM2 (10 µM, blocks all PKC isoforms) or Ro032-0432 (10 µM, blocks only conventional PKC isoforms) for 30 minutes. Cells were lysed and immunoblotted with the anti-pS363-MOP antibody (7TM0319A) at a dilution of 1:1000. Lower panel, blot was stripped and reprobed with the phosphorylation-independent anti-MOP antibody (7TM0319N-WB) at a dilution of 1:1000 to confirm equal loading of the gel. Note, Serine363 phosphorylation is still detectable after blocking of conventional PKC isoforms.

Illing S, Mann A, Schulz S. Heterologous regulation of agonist-independent μ-opioid receptor... more

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Illing S, Mann A, Schulz S. Heterologous regulation of agonist-independent μ-opioid receptor phosphorylation by protein kinase C. Br J Pharmacol. 2014 Mar;171(5):1330-40. doi: 10.1111/bph.12546. PubMed PMID: 24308893; PubMed Central PMCID: PMC3952808.

Doll C, Konietzko J, Pöll F, Koch T, Höllt V, Schulz S. Agonist-selective patterns of µ-opioid receptor phosphorylation revealed by phosphosite-specific antibodies. Br J Pharmacol. 2011 Sep;164(2):298-307. doi: 10.1111/j.1476-5381.2011.01382.x. PubMed PMID: 21449911; PubMed Central PMCID: PMC3174411.

Glück L, Loktev A, Moulédous L, Mollereau C, Law PY, Schulz S. Loss of morphine reward and dependence in mice lacking G protein-coupled receptor kinase 5. Biol Psychiatry. 2014 Nov 15;76(10):767-74. doi: 10.1016/j.biopsych.2014.01.021. Epub 2014 Feb 3. PubMed PMID: 24629717; PubMed Central PMCID: PMC4119866.

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