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
26 From 28
No results were found for the filter!
NEW
Validation of the Urotensin Receptor in transfected HEK293 cells
UT (non-phospho), Urotensin Receptor Antibody
The UT receptor antibody is directed against the distal end of the carboxyl-terminal tail of human Urotensin Receptor. It can be used to detect total UT receptors in Western blots independent of phosphorylation. The UT antibody can also...
375.00 € *
Details
NEW
Validation of Atypical Chemokine Receptor 4 in transfected HEK293 cells
ACKR4 (non-phospho), Atypical Chemokine...
The ACKR4 receptor antibody is directed against the distal end of the carboxyl-terminal tail of human Atypical Chemokine Receptor 4. It can be used to detect total ACKR4 receptors in Western blots independent of phosphorylation. The...
375.00 € *
Details
Citations
Validation of the Tachykinin Receptor 1 in transfected HEK293 cells
NK1 (non-phospho), Tachykinin Receptor 1 Antibody
The NK1 antibody is directed against the distal end of the carboxyl-terminal tail of human Tachykinin Receptor 1 (also called Substance P Receptor). It detects selectively the canonical full-length NK1 Tachykinin Receptor. It can be used...
375.00 € *
Details
Citations
Validation of the Cholecystokinin Receptor 2 in transfected HEK293 cells
CCK2 (non-phospho), Cholecystokinin Receptor 2...
The CCK2 receptor antibody is directed against the distal end of the carboxyl-terminal tail of human Cholecystokinin Receptor 2 (previously called CCKB). It can be used to detect total CCK2 receptors in Western blots independent of...
375.00 € *
Details
NEW
pT408/pT409-CCK1 (phospho-Cholecystokinin Receptor 1 Antibody)
pT408/pT409-CCK1 (phospho-Cholecystokinin...
Threonine408/Threonine409 (T408/T409) is a major phosphorylation site of the CCK1 receptor. The pT408/pT409-CCK1 antibody detects phosphorylation in response to high-efficacy agonists. T408/T409 phosphorylation is a key regulator of CCK1...
375.00 € *
Details
NEW
pS412/pS414-CCK1 (phospho-Cholecystokinin Receptor 1 Antibody)
pS412/pS414-CCK1 (phospho-Cholecystokinin...
Serine412/Serine414 (S412/S414) is a major phosphorylation site of the CCK1 receptor. The pS412/pS414-CCK1 antibody detects phosphorylation in response to high-efficacy agonists. S412/S414 phosphorylation is a key regulator of CCK1...
375.00 € *
Details
Citations
Figure 1. Agonist-induced and Agonist-independent Serine363 phosphorylation of the µ-Opioid Receptor
pS363-MOP (phospho-µ-Opioid Receptor Antibody)
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.
375.00 € *
Details
Citations
KO-Validated
Validation of the CXC Chemokine Receptor 4 in transfected HEK293 cells.
CXCR4 (non-phospho), CXC Chemokine Receptor 4...
The non-phospho-CXCR4 receptor antibody is directed against the distal end of the carboxyl-terminal tail of mouse, rat and human CXCR4. It can be used to detect CXCR4 receptors in Western blots in a phosphorylation-sensitive manner....
375.00 € *
Details
Citations
pS346/pS347-CXCR4 (phospho-CXC Chemokine Receptor 4 Antibody)
pS346/pS347-CXCR4 (phospho-CXC Chemokine...
Serine346/serine347 (S346/S347) is a major phosphorylation site of the CXCR4 receptor. The pS346/pS347-CXCR4 antibody detects phosphorylation in response to agonists and after PKC activation. S346/S347 phosphorylation is a key regulator...
375.00 € *
Details
Citations
Agonist-induced Serine324/Serine325 phosphorylation of the CXC Chemokine Receptor 4.
pS324/pS325-CXCR4 (phospho-CXC Chemokine...
Serine324/serine325 (S324/S325) is a major phosphorylation site of the CXCR4 receptor. The pS324/pS325-CXCR4 antibody detects phosphorylation in response to agonists but not after PKC activation. S324/S325 phosphorylation is a key...
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
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
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
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
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
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
26 From 28

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