pT356/pT359-SST2 (phospho-Somatostatin Receptor 2 Antibody)

Preview: Agonist-induced Threonine356/Threonine359 phosphorylation of the Somatostatin Receptor 2.

Preview: Immunocytochemical identification of Threonine356/Threonine359 phosphorylation of the Somatostatin Receptor 2.

Agonist-induced Threonine356/Threonine359 phosphorylation of the Somatostatin Receptor 2.

pT356/pT359-SST2 (phospho-Somatostatin Receptor 2 Antibody)

Immunocytochemical identification of Threonine356/Threonine359 phosphorylation of the Somatostatin Receptor 2.

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Order number: 7TM0356C
Content: 100 µl
Host: Rabbit

Threonine356/Threonine359 (T356/T359) is a major phosphorylation site of the somatostatin... more

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Threonine356/Threonine359 (T356/T359) is a major phosphorylation site of the somatostatin receptor 2 (SST2). The pT356/pT359-SST2 antibody detects phosphorylation in response to high-efficacy agonists such as octreotide and low-efficacy agonists such as pasireotide. T356/T359 phosphorylation is a key regulator of SST2 desensitization, β-arrestin recruitment and internalization. The pT356/pT359-SST2 antibody can detect phosphorylated SST2 in mouse tissues in vivo. The pT356/pT359-SST2 antibody can be used for detection of the subcellular location of phosphorylated SST2 by immunocytochemistry.

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Alternative Names SST2, SSTR2, Somatostatin Receptor 2 IUPHAR... more

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Alternative Names	SST2, SSTR2, Somatostatin Receptor 2
IUPHAR Target ID	356
UniProt ID	P30874 (human) P30875 (mouse)
Western Blot (WB)	1:1000
Immunocytochemistry (ICC)	1:200
Species Reactivity	Human, Mouse
Host / Isotype	Rabbit / IgG
Class	Polyclonal
Immunogen	A synthetic phosphopeptide derived from human SST2 around the phosphorylation site of Thr356/Thr359
Form	Liquid
Purification	Antigen affinity chromatography
Storage buffer	Dulbecco's PBS, pH 7.4, with 150 mM NaCl, 0.02% sodium azide
Storage conditions	short-term 4°C, long-term -20°C

Figure 1. Agonist-induced Threonine356/Threonine359 phosphorylation of the Somatostatin... more

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Figure 1. Agonist-induced Threonine356/Threonine359 phosphorylation of the Somatostatin Receptor 2. Upper panel, HEK293 cells stably expressing the Somatostatin Receptor 2 (SST2) were either not exposed or exposed to 1 μM SRIF (somatotropin-release inhibiting factor) or 1 μM of artificial somatostatin receptor agonist Octreotide for 30 minutes. Cells were lysed and immunoblotted with the anti-pT356/pT359-SST2 antibody (7TM0356C) at a dilution of 1:1000. Lower panel, blot was stripped and reprobed with the phosphorylation-independent anti-SST2 antibody (7TM0356N-WB) at a dilution of 1:1000 to confirm equal loading of the gel.

Figure 2. Analysis of dose-dependent Somatostatin Receptor 2 phosphorylation using a panel of phosphosite-specific antibodies. Upper three panels, HEK293 cells stably expressing the Somatostatin Receptor 2 (SST2) were either not exposed or exposed to increasing concentrations of SRIF (somatotropin-release inhibiting factor) ranging from 1 nM to 10 μM for 30 minutes. Cells were lysed and immunoblotted with the anti-pS341/pS343-SST2 antibody (7TM0356A) or anti-pT353/pT354-SST2 antibody (7TM0356B) or anti-pT356/pT359-SST2 antibody (7TM0356C) at a dilution of 1:1000. Lower panel, blot was stripped and reprobed with the phosphorylation-independent anti-SST2 antibody (7TM0356N-WB) at a dilution of 1:1000 to confirm equal loading of the gel.

Figure 3. Immunocytochemical identification of Threonine356/Threonine359 phosphorylation of the Somatostatin Receptor 2. HEK293 cells stably expressing the Somatostatin Receptor 2 (SST2) were either not exposed or exposed to 1 μM SRIF (somatotropin-release inhibiting factor) and immunocytochemically stained with the anti-pT356/pT359-SST2 antibody (7TM0356C) at a dilution of 1:200. Note, Threonine356/Threonine359-phosphorylated SST2 receptors were not detectable in untreated cells (0 min). Threonine356/threonine359-phosphorylated SST2 receptors were seen at the plasma membrane and in perinuclear clusters of vesicles after 30 min.

Pöll F, Lehmann D, Illing S, Ginj M, Jacobs S, Lupp A, Stumm R, Schulz S. Pasireotide and... more

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Pöll F, Lehmann D, Illing S, Ginj M, Jacobs S, Lupp A, Stumm R, Schulz S. Pasireotide and octreotide stimulate distinct patterns of sst2A somatostatinreceptor phosphorylation. Mol Endocrinol. 2010 Feb;24(2):436-46. doi: 10.1210/me.2009-0315. Epub 2010 Jan 5. PubMed PMID: 20051480; PubMed Central PMCID: PMC5428126.

Lehmann A, Kliewer A, Schütz D, Nagel F, Stumm R, Schulz S. Carboxyl-terminal multi-site phosphorylation regulates internalization and desensitization of the human sst2 somatostatin receptor. Mol Cell Endocrinol. 2014 Apr 25;387(1-2):44-51. doi: 10.1016/j.mce.2014.02.009. Epub 2014 Feb 22. PubMed PMID: 24565897.

Nagel F, Doll C, Pöll F, Kliewer A, Schröder H, Schulz S. Structural determinants of agonist-selective signaling at the sst(2A) somatostatin receptor. Mol Endocrinol. 2011 May;25(5):859-66. doi: 10.1210/me.2010-0407. Epub 2011 Feb 17. PubMed PMID: 21330405; PubMed Central PMCID: PMC5417258.

Pöll F, Doll C, Schulz S. Rapid dephosphorylation of G protein-coupled receptors by protein phosphatase 1β is required for termination of β-arrestin-dependent signaling. J Biol Chem. 2011 Sep 23;286(38):32931-6. doi: 10.1074/jbc.M111.224899. Epub 2011 Jul 27. PubMed PMID: 21795688; PubMed Central PMCID: PMC3190940.

Kliewer A, Mann A, Petrich A, Pöll F, Schulz S. A transplantable phosphorylation probe for direct assessment of G protein-coupled receptor activation. PLoS One. 2012;7(6):e39458. doi: 10.1371/journal.pone.0039458. Epub 2012 Jun 26. PubMed PMID: 22745760; PubMed Central PMCID: PMC3383726.

Lehmann A, Kliewer A, Märtens JC, Nagel F, Schulz S. Carboxyl-terminal receptor domains control the differential dephosphorylation of somatostatin receptors by protein phosphatase 1 isoforms. PLoS One. 2014 Mar 17;9(3):e91526. doi: 10.1371/journal.pone.0091526. eCollection 2014. PubMed PMID: 24637622; PubMed Central PMCID: PMC3956607.

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