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Phosphorylation of intracellular serine and threonine residues is the most important post translational modification of G protein-coupled receptors (GPCRs) also called heptahelical or seven transmembrane receptors (7TMR). After agonist exposure, these receptors acquire an active conformation, which is recognized by a family of highly specialized GPCR kinases (GRKs). Agonist-driven phosphorylation by GRKs regulates acute receptor desensitization, arrestin recruitment, internalization, post-activation signaling, long-term tolerance and drug addiction. Phosphosite-specific 7TM antibodies are designed to specifically detect agonist-activated GPCRs. In fact, recent work shows that ligand profiling using phosphosite-specific 7TM antibodies provides valuble information on ligand bias beyond that obtained with conventional ß-arrestin recruitment assays. Phosphosite-specific 7TM antibodies are novel tools for GPCR research that can be used to:

  • profile agonist properties of novel GPCR ligands
  • decipher the phosphorylation barcode of GPCRs
  • determine the spatial and temporal dynamics of receptor phosphorylation
  • identify relevant kinases and phosphatases for GPCR phosphorylation and dephosphoryation

Lifecycle3

Schematic representation of the G protein-coupled receptor phosphorylation / dephosphorylation cycle. GRK, G protein-coupled receptor kinase; PKC, protein kinase C; cPP1, catalytic subunit of protein phosphatase 1; R*, activated GPCR; CCP, clathrin-coated pit. 

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pS338/pS339-DP2 (phospho-DP2 Prostanoid Receptor Antibody)
pS338/pS339-DP2 (phospho-DP2 Prostanoid...
Serine338/Serine339 (S338/S339) is major phosphorylation site of the DP2 Prostanoid Receptor (DP2). The pS338/pS339-DP2 antibody detects phosphorylation in response to agonists. S338/S339 phosphorylation is likely to be involved in...
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Agonist-induced Threonine344/Serine345 phosphorylation of the Prostanoid Receptor 2
pT344/pS345-DP2 (phospho-DP2 Prostanoid...
Threonine344/Serine345 (T344/S345) is major phosphorylation site of the DP2 Prostanoid Receptor (DP2). The pT344/pS345-DP2 antibody detects phosphorylation in response to agonists. T344/S345 phosphorylation is likely to be involved in...
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pS493/pS495-PTH1 (phospho-Parathyroid Hormone Receptor 1 Antibody)
pS493/pS495-PTH1 (phospho-Parathyroid Hormone...
Serine493/Serine495 (S493/S495) is major phosphorylation site of the Parathyroid Hormone Receptor 1 (PTH1). The pS493/pS495-PTH1 antibody detects phosphorylation in response to agonists. S493/S495 phosphorylation is likely to be involved...
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Agonist-induced Threonine503/Serine504 phosphorylation of the Parathyroid Hormone Receptor 1
pT503/pS504-PTH1 (phospho-Parathyroid Hormone...
Threonine503/Serine504 (T503/S504) is major phosphorylation site of the Parathyroid Hormone Receptor 1 (PTH1). The pT503/pS504-PTH1 antibody detects phosphorylation in response to agonists. T503/S504 phosphorylation is likely to be...
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Agonist-induced Serine323 phosphorylation of the P2Y Receptor 12.
pS323-P2Y12 (phospho-P2Y Purinoceptor 12 Antibody)
Serine323 (S323) is a major phosphorylation site of the P2Y12 receptor. The pS323-P2Y12 antibody detects phosphorylation in response to high- and low-efficacy agonists and after PKC activation. S323 phosphorylation is a key regulator of...
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Agonist-induced Serine344/Serine345 phosphorylation of the P2Y Receptor
pS344/pS345-P2Y4 (phospho-P2Y Purinoceptor 4...
Serine344/Serine345 (S344/S345) is a major phosphorylation site of the P2Y4 receptor. The pS344/pS345-P2Y4 antibody detects phosphorylation in response to high- and low-efficacy agonists and after PKC activation. S344/S345...
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Agonist-induced Serine339 phosphorylation of the P2Y Receptor 4
pS339-P2Y4 (phospho-P2Y Purinoceptor 4 Antibody)
Serine339 (S339) is a major phosphorylation site of the P2Y4 receptor. The pS339-P2Y4 antibody detects phosphorylation in response to high- and low-efficacy agonists and after PKC activation. S339 phosphorylation is a key regulator of...
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Agonist-induced Threonine351 phosphorylation of the P2Y Receptor 4
pT351-P2Y4 (phospho-P2Y Purinoceptor 4 Antibody)
Threonine351 (T351) is a major phosphorylation site of the P2Y4 receptor. The pT351-P2Y4 antibody detects phosphorylation in response to high- and low-efficacy agonists and after PKC activation. T351 phosphorylation is a key regulator of...
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Agonist-induced Serine343 phosphorylation of GPR183
pS343-GPR183 (phospho-GPR183 Antibody)
Serine343 (S343) is major phosphorylation site of human GPR183 receptor. The pS343-GPR183 antibody detects phosphorylation in response to agonists. S343 phosphorylation is likely to be involved in efficient ligand sequestration by GPR183.
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Agonist-induced Threoine347/Serine349 phosphorylation of GPR183
pT347/pT349-GPR183 (phospho-GPR183 Antibody)
Threonine347/threonine349 (T347/T349) is major phosphorylation site of human GPR183 receptor. The pT347/pT349-GPR183 antibody detects phosphorylation in response to agonists. T347/T349 phosphorylation is likely to be involved in...
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Agonist-induced Serine355 phosphorylation of GPR183
pS355-GPR183 (phospho-GPR183 Antibody)
Serine355 (S355) is major phosphorylation site of human GPR183 receptor. The pS355-GPR183 antibody detects phosphorylation in response to agonists. S355 phosphorylation is likely to be involved in efficient ligand sequestration by GPR183.
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Agonist-induced Threonine361 phosphorylation of the δ-Opioid Receptor.
pT361-DOP (phospho-∂-Opioid Receptor Antibody)
Threonine361 (T361) is a major phosphorylation site of the delta-opioid receptor (DOP). The pT361-DOP antibody detects phosphorylation in response to agonists but not after PKC activation. T361 phosphorylation is a key regulator of DOP...
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Agonist-induced Serine363 phosphorylation of the δ-Opioid receptor.
pS363-DOP (phospho-∂-Opioid Receptor Antibody)
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...
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Validation of the δ-Opioid Receptor in transfected HEK293 cells
DOP (non-phospho) ∂-Opioid Receptor Antibody
The non-phospho-∂-opioid receptor antibody is directed against the distal end of the carboxyl-terminal tail of mouse, rat and human DOP. It can be used to detect total DOP receptors in Western blots independent of phosphorylation.
$ 300.00 *
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Agonist-induced Threonine358/Threonrine361 phosphorylation of the δ-Opioid receptor
pT358/pT361-DOP (phospho-∂-Opioid Receptor...
Threonine358/Threonine361 (T358/T361) is the primary phosphorylation site in a hierarchical phosphorylation cascade of the delta-opioid receptor (DOP). The pT358/T361-DOP antibody detects phosphorylation in response to high- and...
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Agonist-induced Threonine361/Serine363 phosphorylation of the δ-Opioid receptor
pT361/pS363-DOP (phospho-∂-Opioid Receptor...
Threonine361/Serine363 (T361/S363) is the primary phosphorylation site in a hierarchical phosphorylation cascade of the delta-opioid receptor (DOP). The pT361/pS363-DOP antibody detects phosphorylation in response to high- and...
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For further reading refer to:

Kliewer A, Reinscheid RK, Schulz S. Emerging Paradigms of G Protein-Coupled Receptor Dephosphorylation. Trends Pharmacol Sci. 2017 Jul;38(7):621-636. doi:10.1016/j.tips.2017.04.002. Epub 2017 May 4. Review. PubMed PMID: 28478994.

Miess E, Gondin AB, Yousuf A, Steinborn R, Mösslein N, Yang Y, Göldner M, Ruland JG, Bünemann M, Krasel C, Christie MJ, Halls ML, Schulz S, Canals M. Multisite phosphorylation is required for sustained interaction with GRKs and arrestins during rapid μ-opioid receptor desensitization. Sci Signal. 2018 Jul 17;11(539). pii: eaas9609. doi: 10.1126/scisignal.aas9609. PubMed PMID: 30018083.

Kliewer A, Schmiedel F, Sianati S, Bailey A, Bateman JT, Levitt ES, Williams JT, Christie MJ, Schulz S. Phosphorylation-deficient G-protein-biased μ-opioid receptors improve analgesia and diminish tolerance but worsen opioid side effects. Nat Commun. 2019 Jan 21;10(1):367. doi: 10.1038/s41467-018-08162-1. PubMed PMID: 30664663; PubMed Central PMCID: PMC6341117.

Mann A, Moulédous L, Froment C, O'Neill PR, Dasgupta P, Günther T, Brunori G, Kieffer BL, Toll L, Bruchas MR, Zaveri NT, Schulz S. Agonist-selective NOP receptor phosphorylation correlates in vitro and in vivo and reveals differential post-activation signaling by chemically diverse agonists. Sci Signal. 2019 Mar 26;12(574). pii: eaau8072. doi: 10.1126/scisignal.aau8072. PubMed PMID: 30914485; PubMed Central PMCID: PMC6934085.

Saaber F, Schütz D, Miess E, Abe P, Desikan S, Ashok Kumar P, Balk S, Huang K, Beaulieu JM, Schulz S, Stumm R. ACKR3 Regulation of Neuronal Migration Requires ACKR3 Phosphorylation, but Not β-Arrestin. Cell Rep. 2019 Feb 5;26(6):1473-1488.e9. doi: 10.1016/j.celrep.2019.01.049. PubMed PMID: 30726732.

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.

For further reading refer to: Kliewer A, Reinscheid RK, Schulz S. Emerging Paradigms of G Protein-Coupled Receptor Dephosphorylation. Trends Pharmacol Sci. 2017 Jul;38(7):621-636.... read more »
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For further reading refer to:

Kliewer A, Reinscheid RK, Schulz S. Emerging Paradigms of G Protein-Coupled Receptor Dephosphorylation. Trends Pharmacol Sci. 2017 Jul;38(7):621-636. doi:10.1016/j.tips.2017.04.002. Epub 2017 May 4. Review. PubMed PMID: 28478994.

Miess E, Gondin AB, Yousuf A, Steinborn R, Mösslein N, Yang Y, Göldner M, Ruland JG, Bünemann M, Krasel C, Christie MJ, Halls ML, Schulz S, Canals M. Multisite phosphorylation is required for sustained interaction with GRKs and arrestins during rapid μ-opioid receptor desensitization. Sci Signal. 2018 Jul 17;11(539). pii: eaas9609. doi: 10.1126/scisignal.aas9609. PubMed PMID: 30018083.

Kliewer A, Schmiedel F, Sianati S, Bailey A, Bateman JT, Levitt ES, Williams JT, Christie MJ, Schulz S. Phosphorylation-deficient G-protein-biased μ-opioid receptors improve analgesia and diminish tolerance but worsen opioid side effects. Nat Commun. 2019 Jan 21;10(1):367. doi: 10.1038/s41467-018-08162-1. PubMed PMID: 30664663; PubMed Central PMCID: PMC6341117.

Mann A, Moulédous L, Froment C, O'Neill PR, Dasgupta P, Günther T, Brunori G, Kieffer BL, Toll L, Bruchas MR, Zaveri NT, Schulz S. Agonist-selective NOP receptor phosphorylation correlates in vitro and in vivo and reveals differential post-activation signaling by chemically diverse agonists. Sci Signal. 2019 Mar 26;12(574). pii: eaau8072. doi: 10.1126/scisignal.aau8072. PubMed PMID: 30914485; PubMed Central PMCID: PMC6934085.

Saaber F, Schütz D, Miess E, Abe P, Desikan S, Ashok Kumar P, Balk S, Huang K, Beaulieu JM, Schulz S, Stumm R. ACKR3 Regulation of Neuronal Migration Requires ACKR3 Phosphorylation, but Not β-Arrestin. Cell Rep. 2019 Feb 5;26(6):1473-1488.e9. doi: 10.1016/j.celrep.2019.01.049. PubMed PMID: 30726732.

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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