Premium Phosphosite-Specific 7TM Antibodies
Novel Tools for Your GPCR Research
Select Your Country of Delivery below

Premium Phosphosite-Specific 7TM Antibodies

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. 

Close filters
14 From 18
No results were found for the filter!
NEW
pS351/pT356-GPR17 (phospho-GPR17 Antibody)
pS351/pT356-GPR17 (phospho-GPR17 Antibody)
Serine351/Threonine356 (S351/T356) is a major phosphorylation site of the human GPR17 receptor. The pS351/pT356-GPR17 antibody detects phosphorylation in response to high-efficacy agonists. S351/T356 phosphorylation is a key regulator of...
$ 375.00 *
Details
NEW
Validation of the G Protein-coupled Receptor 17 in transfected HEK293 cells
GPR17 (non-phospho), G Protein-coupled Receptor...
The non-phospho-GPR17 receptor antibody is directed against the distal part of the carboxyl-terminal tail of human GPR17. It can be used to detect total GPR17 receptors in Western blots independent of phosphorylation. The...
$ 375.00 *
Details
NEW
Agonist-induced Threonine401/Serine403 phosphorylation of Orexin Receptor 2
pT401/pS403-OX2 (phospho-Orexin Receptor 2...
Threonine401/Serine403 (T401/S403) is a major phosphorylation site of the Orexin receptor 2 (OX2). The pT401/pS403-OX2 antibody detects phosphorylation in response to high-efficacy agonists. T401/S403 phosphorylation is a key regulator...
$ 375.00 *
Details
NEW
Agonist-induced Threonine408/Threonine409 phosphorylation of Orexin Receptor 2
pT408/pT409-OX2 (phospho-Orexin Receptor 2...
Threonine408/Threonine409 (T408/T409) is a major phosphorylation site of the Orexin receptor 2 (OX2). The pT408/pT409-OX2 antibody detects phosphorylation in response to high-efficacy agonists. T408/T409 phosphorylation is a key...
$ 375.00 *
Details
NEW
Agonist-induced Serine385 phosphorylation of Orexin Receptor 1
pS385-OX1 (phospho-Orexin Receptor 1 Antibody)
Serine385 (S385) is a major phosphorylation site of the Orexin receptor 1 (OX1). The pS385-OX1 antibody detects phosphorylation in response to high-efficacy agonists. S385 phosphorylation is a key regulator of OX1 desensitization,...
$ 375.00 *
Details
NEW
Agonist-induced Serine393/Serine394 phosphorylation of Orexin Receptor 1
pS393/pS394-OX1 (phospho-Orexin Receptor 1...
Serine393/Serine394 (S393/S394) is a major phosphorylation site of the Orexin receptor 1 (OX1). The pS393/pS394-OX1 antibody detects phosphorylation in response to high-efficacy agonists. S393/S394 phosphorylation is a key regulator of...
$ 375.00 *
Details
NEW
Agonist-induced Serine399/Serine401 phosphorylation of Orexin Receptor 1
pS399/pS401-OX1 (phospho-Orexin Receptor 1...
Serine399/Serine401 (S399/S401) is a major phosphorylation site of the Orexin receptor 1 (OX1). The pS399/pS401-OX1 antibody detects phosphorylation in response to high-efficacy agonists. S399/S401 phosphorylation is a key regulator of...
$ 375.00 *
Details
Citations
KO-Validated
Validation of the Nociceptin/Orphanin FQ Receptor in transfected HEK293 cells.
NOP (non-phospho), Nociceptin/Orphanin FQ...
The non-phospho-NFQ receptor (NOP) antibody is directed against the distal end of the carboxyl-terminal tail of mouse, rat and human NOP. It can be used to detect total NOP receptors in Western blots independent of phosphorylation. The...
$ 300.00 *
Details
Citations
Agonist-induced Serine356/Threonine357 phosphorylation of the κ-Opioid Receptor.
pS356/pT357-KOP (phospho-κ-Opioid Receptor...
Serine356/Threonine357 is a major phosphorylation site of the kappa-opioid receptor (KOP). The pS356/pT357-KOP antibody detects phosphorylation in response to agonists as well as after PKC activation. S356/T357 phosphorylation is a key...
$ 375.00 *
Details
Citations
Agonist-induced Threonine363 phosphorylation of the κ-Opioid Receptor.
pT363-KOP (phospho-κ-Opioid Receptor Antibody)
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,...
$ 375.00 *
Details
Citations
Validation of the κ-Opioid Receptor in transfected HEK293 cells.
KOP (non-phospho) κ-Opioid Receptor Antibody
The non-phospho-kappa-opioid receptor antibody is directed against the distal end of the carboxyl-terminal tail of mouse, rat and human KOP. It can be used to detect total KOP receptors in Western blots independent of phosphorylation.
$ 300.00 *
Details
Citations
Figure 1. Agonist-induced Serine375 phosphorylation of the µ-opioid receptor.
pS375-MOP (phospho-µ-Opioid Receptor Antibody)
Serine375 (S375) is the primary phosphorylation site in a hierarchical phosphorylation cascade. The pS375-MOP antibody detects phosphorylation in response to high- and low-efficacy agonists but not after PKC activation. S375...
$ 375.00 *
Details
Citations
KO-Validated
MOP (non-phospho), µ-Opioid Receptor Antibody
MOP (non-phospho), µ-Opioid Receptor Antibody
The non-phospho-µ-opioid receptor antibody is directed against the distal end of the carboxyl-terminal tail of mouse, rat and human MOP. It detects selectively the canonical form of MOP and none of the putative splice variants. It can be...
$ 375.00 *
Details
Citations
Figure 1. Agonist-induced Threonine370 phosphorylation of the µ-opioid receptor.
pT370-MOP (phospho-µ-Opioid Receptor Antibody)
Threonine370 (T370) is a major phosphorylation site of the µ-opioid receptor (MOP). The pT370-MOP antibody detects phosphorylation in response to high-efficacy agonists but to low-efficacy agonists. The pT370-MOP antibody also detects...
$ 375.00 *
Details
Citations
Agonist-induced Threonine376 phosphorylation of the µ-Opioid Receptor.
pT376-MOP (phospho-µ-Opioid Receptor Antibody)
Threonine376 (T376) is a major phosphorylation site of the µ-opioid receptor (MOP). The pT376-MOP antibody detects phosphorylation in response to high-efficacy agonists but to low-efficacy agonists or after PKC activation. T376...
$ 375.00 *
Details
Citations
Agonist-induced Threonine379 phosphorylation of the µ-Opioid Receptor.
pT379-MOP (phospho-µ-Opioid Receptor Antibody)
Threonine379 (T379) is a major phosphorylation site of the µ-opioid receptor (MOP). The pT379-MOP antibody detects phosphorylation in response to high-efficacy agonists but to low-efficacy agonists or after PKC activation. T379...
$ 375.00 *
Details
14 From 18

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 »
Close window
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.

Recently viewed