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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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Rabbit Monoclonal
KO-Validated
NEW
Immunohistochemical identification of Somatostatin Receptor 2 in human neuroendocrine tumor tissue.
SST2 [UMB11] (RM-IHC-grade), Somatostatin...
The SST2 receptor antibody is directed against the distal end of the carboxyl-terminal tail of mouse, rat and human Somatostatin Receptor 2. It detects selectively the canonical form of SST2 (also referred to as SST2A) and not the...
£ 495.00 *
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Citations
KO-Validated
Immunohistochemical identification of Somatostatin Receptor 2 in human neuroendocrine tumor tissue
SST2 (IHC-grade), Somatostatin Receptor 2 Antibody
The SST2 receptor antibody is directed against the distal end of the carboxyl-terminal tail of mouse, rat and human Somatostatin Receptor 2. It detects selectively the canonical form of SST2 (also referred to as SST2A) and not the...
£ 335.00 *
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Rabbit Monoclonal
KD-Validated
NEW
Western blot analysis of Somatostatin Receptor 1 in membrane preparations from cells of AtT-20 and BON-1 cell lines.
SST1 [UMB7] (RM-non-phospho-Somatostatin...
The SST1 receptor antibody is directed against the distal end of the carboxyl-terminal tail of human Somatostatin Receptor 1. It can be used to detect total SST1 receptors in Western blots independent of phosphorylation. The SST1...
£ 495.00 *
Details
Rabbit Monoclonal
KD-Validated
NEW
Immunohistochemical identification of Somatostatin Receptor 1 in human pituitary.
SST1 [UMB7] (RM-IHC-grade), Somatostatin...
The SST1 receptor antibody is directed against the distal end of the carboxyl-terminal tail of human Somatostatin Receptor 1. It can be used to detect total SST1 receptors in Western blots independent of phosphorylation. The SST1...
£ 495.00 *
Details
Citations
Immunohistochemical identification of Somatostatin Receptor 1 in human pituitary
SST1 (IHC-grade), Somatostatin Receptor 1 Antibody
The SST1 receptor antibody is directed against the distal end of the carboxyl-terminal tail of human Somatostatin Receptor 1. It can be used to detect total SST1 receptors in Western blots independent of phosphorylation. The SST1...
£ 335.00 *
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Citations
Agonist-induced Threonine333 phosphorylation of the Somatostatin Receptor 5.
pT333-SST5 (phospho-Somatostatin Receptor 5...
Threonine333 (T333) is a major phosphorylation site of the human somatostatin receptor 5 (SST5). The pT333-SST5 antibody detects phosphorylation in response to high-efficacy agonists such as pasireotide but not after activation of PKC....
£ 335.00 *
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Validation of the Somatostatin Receptor 3 in transfected HEK293 cells
mSST3 (non-phospho), Somatostatin Receptor 3...
The non-phospho-SST3 receptor antibody is directed against the distal end of the carboxyl-terminal tail of human SST3. In can be used to detect total SST3 receptors in Western blots independent of phosphorylation. The non-phospho-SST3...
£ 335.00 *
Details
Citations
KO-Validated
Immunohistochemical identification of Somatostatin Receptor 3 in neuronal cilia.
mSST3 (IHC-grade), Somatostatin Receptor 3...
The mouse SST3 antibody is directed against the distal end of the carboxyl-terminal tail of mouse and rat Somatostatin Receptor 3. It can be used to detect total SST3 receptors in Western blots independent of phosphorylation. The SST3...
£ 335.00 *
Details
NEW
Validation of the Proteinase-Activated Receptor 2 in transfected HEK293 cells
PAR2 (non-phospho), Proteinase-Activated...
The non-phospho-PAR2 receptor antibody is directed against the distal end of the carboxyl-terminal tail of human Proteinase-Activated Receptor 2. It can be used to detect total PAR2 receptors in Western blots independent of...
£ 335.00 *
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NEW
Agonist-induced Serine425/Serine429 phosphorylation of VPAC2 Receptor.
pS425/pS429-VPAC2 (phospho-VIP Receptor 2...
Serine425/Serine429 (S425/S429) is a major phosphorylation site of the VPAC2 receptor. The pS425/pS429-VPAC2 antibody detects phosphorylation in response to high-efficacy agonists. S425/S429 phosphorylation is a key regulator of VPAC2...
£ 335.00 *
Details
NEW
Agonist-induced Serine411/Serine415 phosphorylation of VPAC2 Receptor
pS411/pS415-VPAC2 (phospho-VIP Receptor 2...
Serine411/Serine415 (S411/S415) is a major phosphorylation site of the VPAC2 receptor. The pS411/pS415-VPAC2 antibody detects phosphorylation in response to high-efficacy agonists. S411/S415 phosphorylation is a key regulator of VPAC2...
£ 335.00 *
Details
NEW
Agonist-induced Serine408/Serine409 phosphorylation of VPAC2 Receptor
pS408/pS409-VPAC2 (phospho-VIP Receptor 2...
Serine408/Serine409 (S408/S409) is a major phosphorylation site of the VPAC2 receptor. The pS408/pS409-VPAC2 antibody detects phosphorylation in response to high-efficacy agonists. S408/S409 phosphorylation is a key regulator of VPAC2...
£ 335.00 *
Details
Citations
KO-Validated
Validation of the VIP Receptor 2 in transfected HEK293 cells
VPAC2 (non-phospho), VIP Receptor 2 Antibody
The VPAC2 antibody is directed against the distal end of the carboxyl-terminal tail of mouse, rat and human VIP receptor 2. It can be used to detect total VPAC2 receptors in Western blots independent of phosphorylation. The VPAC2...
£ 335.00 *
Details
NEW
Agonist-induced Serine422/Serine425 phosphorylation of VPAC1 Receptor
pS422/pS425-VPAC1 (phospho-VIP Receptor 1...
Serine422/Serine425 (S422/S425) is a major phosphorylation site of the VPAC1 receptor. The pS422/pS425-VPAC1 antibody detects phosphorylation in response to high-efficacy agonists. S422/S425 phosphorylation is a key regulator of VPAC1...
£ 335.00 *
Details
NEW
Agonist-induced Threonine429/Serine431/Threonine432 phosphorylation of VPAC1 Receptor
pT429/pS431/pT432-VPAC1 (phospho-VIP Receptor 1...
Threonine429/Serine431/Threonine432 (T429/S431/T432) is a major phosphorylation site of the VPAC1 receptor. The pT429/pS431/pT432-VPAC1 antibody detects phosphorylation in response to high-efficacy agonists. T429/S431/T432...
£ 335.00 *
Details
NEW
Agonist-induced and Agonist-independent Serine435/Threonine438 phosphorylation of VAPC1 Receptor
pS435/pT438-VPAC1 (phospho-VIP Receptor 1...
Serine435/Threonine438 (S435/T438) is a major phosphorylation site of the VPAC1 receptor. The pS435/pT438-VPAC1 antibody detects phosphorylation in response to high-efficacy agonists. S422/S425 phosphorylation is a key regulator of VPAC1...
£ 335.00 *
Details
29 From 43

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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