Premium Phosphosite-Specific 7TM Antibodies
Your Resource for 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
2 From 43
No results were found for the filter!
NEW
Agonist-induced Threonine311/Serine312 phosphorylation of the A3 Adenosine Receptor.
pT311/pS312-A3 (phospho-A3 Adenosine Receptor...
Threonine311/Serine312 is a major phosphorylation site of the A3 Adenosine receptor. The pT311/pS312-A3 antibody detects phosphorylation in response to high-efficacy agonists but not after PKC activation. T311/S312 phosphorylation is a...
375.00 € *
Details
Citations
NEW
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...
375.00 € *
Details
NEW
Agonist-induced Threonine338 phosphorylation of the Hydroxycarboxylic Acid Receptor 2
pT338-HCA2 (phospho-Hydroxycarboxylic Acid...
Threonine338 (T338) is major phosphorylation site of the Hydroxycarboxylic Acid Receptor 2 (HCA2). The pT338-HCA2 antibody detects phosphorylation in response to agonists. T338 phosphorylation is likely to be involved in efficient ligand...
375.00 € *
Details
NEW
Immunohistochemical Identification of Serine594/Threonine597/Serine599 phosphorylation of the SMO Receptor in primary cilia in the mouse neural tube
pS594/pT597/pS599-SMO (IHC-grade phospho-SMO...
Serine594/Threonine597/Serine599 (S594/T597/S599) is major GRK2 phosphorylation site of the SMO receptor. The pS594/pT597/pS599-SMO antibody detects phosphorylation in response to agonists. The pS594/pT597/pS599-SMO antibody can be used...
550.00 € *
Details
NEW
Immunohistochemical identification of Proteinase-Activated Receptor 2 in Kidney
PAR2 (IHC-grade), Proteinase-Activated Receptor...
The PAR2 antibody is directed against the distal end of the carboxyl-terminal tail of mouse, rat and human PAR2. It can be used to detect total PAR2 receptors in Western blots independent of phosphorylation. The PAR2 antibody can also be...
375.00 € *
Details
NEW
Agonist-induced Serine362/Serine363/Serine364 phosphorylation of the Vasopressin Receptor 2
pS362/pS363/pS364-V2 (phospho-Vasopressin...
Serine362/Serine363/Serine364 (S362/S363/S364) is major phosphorylation site of the Vasopresssin Receptor 2 (V2). The pS362/pS363/pS364-V2 antibody detects phosphorylation in response to agonists. S362/S363/S364 phosphorylation is likely...
375.00 € *
Details
NEW
Agonist-induced Threonine359/Threonine360 phosphorylation of the Vasopressin Receptor 2.
pT359/pT360-V2 (phospho-Vasopressin Receptor 2...
Threonine359/Threonine360 (T359/T360) is major phosphorylation site of the Vasopressin Receptor 2 (V2). The pT359/pT360-V2 antibody detects phosphorylation in response to agonists. T359/T360 phosphorylation is likely to be involved in...
375.00 € *
Details
NEW
Agonist-induced Serine350 phosphorylation of the Vasopressin Receptor 2
pS350-V2 (phospho-Vasopressin Receptor 2 Antibody)
Serine350 (S350) is major phosphorylation site of the Vasopresssin Receptor 2 (V2). The pS350-V2 antibody detects phosphorylation in response to agonists. S350 phosphorylation is likely to be involved in efficient ligand sequestration by...
375.00 € *
Details
NEW
Validation of the Vasopressin Receptor 2 in transfected HEK293 cells
V2 (non-phospho), Vasopressin Receptor 2 Antibody
The non-phospho-V2 Receptor Antibody is directed against the distal end of the carboxyl-terminal tail of human V2. It can be used to detect total V2 receptors in Western blots independent of phosphorylation. The non-phospho-V2 antibody...
375.00 € *
Details
NEW
Agonist-induced Serine397/Threonine398 phosphorylation of the Vasopressin Receptor 1A
pS397/pT398-V1A (phospho-Vasopressin Receptor...
Serine397/Threonine398 (S397/T398) is major phosphorylation site of the Vasopressin Receptor 1A (V1A). The pS397/pT398-V1A antibody detects phosphorylation in response to agonists. S397/T398 phosphorylation is likely to be involved in...
375.00 € *
Details
NEW
Agonist-induced Threonine386/Serine389 phosphorylation of the Vasopressin Receptor 1A
pT386/pS389-V1A (phospho-Vasopressin Receptor...
Threonine386/Serine389 (T368/S389) is major phosphorylation site of the Vasopressin Receptor 1A (V1A). The pT386/pS389-V1A antibody detects phosphorylation in response to agonists. T386/S389 phosphorylation is likely to be involved in...
375.00 € *
Details
NEW
Agonist-induced Threonine378/Serine380 phosphorylation of the Vasopressin Receptor 1A
pT378/pS380-V1A (phospho-Vasopressin Receptor...
Threonine378/Serine380 (T378/S380) is major phosphorylation site of the Vasopressin Receptor 1A (V1A). The pT378/pS380-V1A antibody detects phosphorylation in response to agonists. T378/S380 phosphorylation is likely to be involved in...
375.00 € *
Details
NEW
Validation of the Vasopressin Receptor 1A in transfected HEK293 cells
V1A (non-phospho), Vasopressin Receptor 1A...
The non-phospho-V1A Receptor Antibody is directed against the distal end of the carboxyl-terminal tail of human V1A. It can be used to detect total V1A receptors in Western blots independent of phosphorylation. The non-phospho-V1A...
375.00 € *
Details
NEW
Agonist-induced Threonine369/Serine370 phosphorylation of the EP4 Prostanoid Receptor
pT369/pS370-EP4 (phospho-EP4 Prostanoid...
Threonine369/Serine370 (T369/S370) is major phosphorylation site of the EP4 Prostanoid Receptor (EP4). The pT369/pS370-EP4 antibody detects phosphorylation in response to agonists. T369/S370 phosphorylation is likely to be involved in...
375.00 € *
Details
NEW
Agonist-induced Serine374/Serine377 phosphorylation of the EP4 Prostanoid Receptor
pS374/pS377-EP4 (phospho-EP4 Prostanoid...
Serine374/Serine377 (S374/S377) is major phosphorylation site of the EP4 Prostanoid Receptor (EP4). The pS374/pS377-EP4 antibody detects phosphorylation in response to agonists. S374/S377 phosphorylation is likely to be involved in...
375.00 € *
Details
NEW
Agonist-induce Serine364/Serine366 phosphorylation of the EP4 Prostanoid Receptor
pS364/pS366-EP4 (phospho-EP4 Prostanoid...
Serine364/Serine366 (S364/S366) is major phosphorylation site of the EP4 Prostanoid Receptor (EP4). The pS364/pS366-EP4 antibody detects phosphorylation in response to agonists. S364/S366 phosphorylation is likely to be involved in...
375.00 € *
Details
2 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 »
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