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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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Agonist-induced Serine335/Threonine336 phosphorylation of the Angiotensin Receptor 1
pS335/pT336-AT1 (phospho-Angiotensin Receptor 1...
Serine335/Threonine336 (S335/T336) is major phosphorylation site of the Angiotensin Receptor 1 (AT1). The pS335/pT336-AT1 antibody detects phosphorylation in response to agonists. S335/T336 phosphorylation is likely to be involved in...
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Agonist-induced Serine346/Serine347 phosphorylation of the Angiotensin Receptor 1
pS346/pS347-AT1 (phospho-Angiotensin Receptor 1...
Serine346/Serine347 (S346/S347) is major phosphorylation site of the Angiotensin Receptor 1 (AT1). The pS346/pS347-AT1 antibody detects phosphorylation in response to agonists. S346/S347 phosphorylation is likely to be involved in...
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Agonist-induced Serine355/Serine356 phosphorylation of the β2 Adrenoceptor
pS355/pS356-β2 (phospho-β2-Adrenoceptor Antibody)
Serine355/Serine356 (S355/S356) is a major phosphorylation site of the β2 adrenoceptor. The pS355/pS356-β2 antibody detects phosphorylation in response to high- and low-efficacy agonists but not after PKC activation. S355/S356...
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Agonist-induced Threonine360/Serine364 phosphorylation of the β2 Adrenoceptor
pT360/pS364-β2 (phospho-β2-Adrenoceptor Antibody)
Threonine360/Serine364 (T360/S364) is a major phosphorylation site of the β2 adrenoceptor. The pT360/pS364-β2 antibody detects phosphorylation in response to high- and low-efficacy agonists but not after PKC activation. T360/S364...
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Agonist-induced Serine355 phosphorylation of the β2-Adrenoceptor
pS355-β2 (phospho-β2-Adrenoceptor Antibody)
Serine355 (S355) is a major phosphorylation site of the β2 adrenoceptor. The pS355-β2 antibody detects phosphorylation in response to high- and low-efficacy agonists but not after PKC activation. S355 phosphorylation is primarily...
$ 375.00 *
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Agonist-induced Serine356 phosphorylation of the β2-Adrenoceptor
pS356-β2 (phospho-β2-Adrenoceptor Antibody)
Serine356 (S356) is a major phosphorylation site of the β2 adrenoceptor. The pS356-β2 antibody detects phosphorylation in response to high- and low-efficacy agonists but not after PKC activation. S356 phosphorylation is primarily...
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Agonist-induced Serine364 phosphorylation of the β2-Adrenoceptor
pS364-β2 (phospho-β2-Adrenoceptor Antibody)
Serine364 (S364) is a major phosphorylation site of the β2 adrenoceptor. The pS364-β2 antibody detects phosphorylation in response to high- and low-efficacy agonists but not after PKC activation. S364 phosphorylation is primarily...
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Validation of the β2-Adrenoceptor in transfected HEK293 cells
β2 (non-phospho), β2-Adrenoceptor Antibody
The non-phospho- β2 antibody is directed against the third intracellular loop of human β2 . It can be used to detect total β2 receptors in Western blots independent of phosphorylation. The non-phospho- β2 antibody can also be used to...
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Agonist-induced Threonine404 phosphorylation of the β1-Adrenoceptor
pT404-β1 (phospho-β1-Adrenoceptor Antibody)
Threonine404 (T404) is a major phosphorylation site of the β1 adrenoceptor. The pT404-β1 antibody detects phosphorylation in response to high- and low-efficacy agonists but not after PKC activation. T404 phosphorylation is primarily...
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Agonist-induced Serine412 phosphorylation of the β1-Adrenoceptor
pS412-β1 (phospho-β1-Adrenoceptor Antibody)
Serine412 (S412) is a major phosphorylation site of the β1 adrenoceptor. The pS412-β1 antibody detects phosphorylation in response to high- and low-efficacy agonists but not after PKC activation. S412 phosphorylation is primarily...
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Validation of the β1-Adrenoceptor in transfected HEK293 cells
β1 (non-phospho), β1-Adrenoceptor Antibody
The non-phospho- β1 antibody is directed against the carboxyl-terminal tail of human β1 . It can be used to detect total β1 receptors in Western blots independent of phosphorylation. The non-phospho- β1 antibody can also be used to...
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Agonist-induced Serine261/Serine262 phosphorylation of the β2-Adrenoceptor
pS261pS262-β2 (phospho-β2-Adrenoceptor Antibody)
Serine261/Serine262 (S261/S262) is a major phosphorylation site of the β2 adrenoceptor. The pS261/pS262-β2 antibody detects phosphorylation in response to high- and low-efficacy agonists but not after PKC activation. S261/S262...
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Agonist-induced Serine329 phosphorylation of the A2A Adenosine Receptor
pS329-A2A (phospho-A2A Adenosine Receptor...
Serine329 is a major phosphorylation site of the A2A Adenosine receptor. The pS329-A2A antibody detects phosphorylation in response to high-efficacy agonists but not after PKC activation. S329 phosphorylation is a key regulator of A2A...
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Agonist-induced Serine298 phosphorylation of the M1 Muscarinic Acetylcholine Receptor
pS298-M1 (phospho-M1 Muscarinic Acetylcholine...
Serine298 is a major phosphorylation site of the M1 muscarinic acetylcholine receptor. The pS298-M1 antibody detects phosphorylation in response to high-efficacy agonists.
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Agonist-induced Threonine271 phosphorylation of the M2 Muscarinic Acetycholine Receptor
pT271-M2 (phospho-M2 Muscarinic Acetylcholine...
Threonine271 is a major phosphorylation site of the M2 Muscarinic Acetylcholine Receptor. The pT271-M2 antibody detects phosphorylation in response to high-efficacy agonists but not after PKC activation. T271 phosphorylation is a key...
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Agonist-induced Serine282/Serine283 phosphorylation of the M2 Muscarinic Acetylcholine Receptor
pS282/pS283-M2 (phospho-M2 Muscarinic...
Serine282/Serine283 is a major phosphorylation site of the M2 Muscarinic Acetylcholine Receptor. The pS282/pS283-M2 antibody detects phosphorylation in response to high-efficacy agonists but not after PKC activation. S282/S283...
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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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Premium Phosphosite-Specific 7TM Antibodies

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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