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
20 From 30
No results were found for the filter!
Citations
NTS2 (IHC-grade), Neurotensin Receptor 2 Antibody
NTS2 (IHC-grade), Neurotensin Receptor 2 Antibody
The NTS2 antibody is directed against the distal end of the carboxyl-terminal tail of human Neurotensin Receptor 2. It can be used to detect total NTS2 receptors in Western blots independent of phosphorylation. The NTS2 antibody can also...
$ 400.00 *
Details
NEW
Immunohistochemical identification of GPR158/mGlyR Receptor in small intestine
GPR158/mGlyR (IHC-grade), Glycin Receptor...
The non-phospho-GPR158 receptor antibody is directed against the distal end of the carboxyl-terminal tail of human GPR158. It also detects GPR158 in cultured cells and tissue sections by immunohistochemistry. It can be used to detect...
$ 400.00 *
Details
NEW
Validation of the Dopamine Receptor 1 in transfected HEK293 cells
D1 (non-phospho-Dopamine Receptor 1 Antibody)
The non-phospho-D1 receptor antibody is directed against the distal part of the carboxyl-terminal tail of human D1. It can be used to detect total D1 receptors in Western blots independent of phosphorylation. The non-phospho-D1 antibody...
$ 400.00 *
Details
NEW
Immunohistochemical identification of Dopamine Receptor 1 in striatum
D1 (IHC-grade), Dopamine Receptor 1 Antibody
The D1 receptor antibody is directed against the distal part of the carboxyl-terminal tail of human D1. It can be used to detect total D1 receptors in Western blots independent of phosphorylation. The D1 antibody can also be used to...
$ 400.00 *
Details
NEW
Validation of the Corticotropin-Releasing Factor Receptor 1 in transfected HEK293 cells
CRF1 (non-phospho-Corticotropin-Releasing...
The non-phospho-CRF1 receptor antibody is directed against the distal part of the carboxyl-terminal tail of human CRF1. It can be used to detect total CRF1 receptors in Western blots independent of phosphorylation. The non-phospho-CRF1...
$ 400.00 *
Details
Citations
KO-Validated
Immunohistochemical identification of FFA2 Receptor in pancreas
FFA2 (IHC-grade), FFA2 Receptor Antibody
The FFA2 receptor antibody is directed against the distal part of the carboxyl-terminal tail of human FFA2. It can be used to detect total FFA2 receptors in Western blots independent of phosphorylation. The FFA2 antibody can also be used...
$ 400.00 *
Details
NEW
Validation of the FFA2 in transfected HEK293 cells
FFA2 (non-phospho-FFA2 Antibody)
The non-phospho-FFA2 receptor antibody is directed against the distal part of the carboxyl-terminal tail of human FFA2. It can be used to detect total FFA2 receptors in Western blots independent of phosphorylation. The non-phospho-FFA2...
$ 400.00 *
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...
$ 400.00 *
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...
$ 400.00 *
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...
$ 400.00 *
Details
Citations
Validation of the VIP receptor 1 in transfected HEK293 cells
VPAC1 (non-phospho), VIP Receptor 1 Antibody
The VPAC1 antibody is directed against the distal end of the carboxyl-terminal tail of human VIP Receptor 1. It can be used to detect total VPAC1 receptors in Western blots independent of phosphorylation. The VPAC1 antibody can also be...
$ 400.00 *
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...
$ 400.00 *
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...
$ 400.00 *
Details
NEW
pS425/pS429-VPAC2 (phospho-VIP Receptor 2 Antibody)
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...
$ 400.00 *
Details
Citations
Validation of the Cholecystokinin Receptor 1 in transfected HEK293 cells
CCK1 (non-phospho), Cholecystokinin Receptor 1...
The CCK1 receptor antibody is directed against the distal end of the carboxyl-terminal tail of human Cholecystokinin Receptor 1 (previously called CCKA). It can be used to detect total CCK1 receptors in Western blots independent of...
$ 400.00 *
Details
NEW
pS417/pS419-CCK1 (phospho-Cholecystokinin Receptor 1 Antibody)
pS417/pS419-CCK1 (phospho-Cholecystokinin...
Serine417/Serine419 (S417/S419) is a major phosphorylation site of the CCK1 receptor. The pS417/pS419-CCK1 antibody detects phosphorylation in response to high-efficacy agonists. S417/S419 phosphorylation is a key regulator of CCK1...
$ 400.00 *
Details
20 From 30

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