pT353/pT354-SST2 (phospho-Somatostatin Receptor 2 Antibody)

Preview: Agonist-induced Threonine353/Threonine354 phosphorylation of the Somatostatin Receptor 2.

Agonist-induced Threonine353/Threonine354 phosphorylation of the Somatostatin Receptor 2.

pT353/pT354-SST2 (phospho-Somatostatin Receptor 2 Antibody)

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Order number: 7TM0356B
Content: 100 µl
Host: Rabbit

Threonine353/Threonine354 (T353/T354) is a major phosphorylation site of the somatostatin... more

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Threonine353/Threonine354 (T353/T354) is a major phosphorylation site of the somatostatin receptor 2 (SST2). The pT353/pT354-SST2 antibody detects phosphorylation in response to high-efficacy agonists such as octreotide and low-efficacy agonists such as pasireotide. T353/T354 phosphorylation is a key regulator of SST2 desensitization, β-arrestin recruitment and internalization. The pT353/pT354-SST2 antibody can detect phosphorylated SST2 in mouse tissues in vivo.

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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
Species Reactivity	Human, Mouse
Host / Isotype	Rabbit / IgG
Class	Polyclonal
Immunogen	A synthetic phosphopeptide derived from human SST2 around the phosphorylation site of Thr353/Thr354
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 Threonine353/Threonine354 phosphorylation of the Somatostatin... more

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Figure 1. Agonist-induced Threonine353/Threonine354 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-pT353/pT354-SST2 antibody (7TM0356B) 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.

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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