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- Order number: 7TM0306B
- Content: 100 µl
- Host: Rabbit
Serine354Threonine356 (S354/T356) is a major phosphorylation site of the Neuropeptide Y Receptor 2. The pS354/pT356-NPY2 antibody detects phosphorylation in response to high- and low-efficacy agonists but not after PKC activation. S354/T356 phosphorylation is primarily mediated by GRKs and is a key regulator of NPY2 desensitization, β-arrestin recruitment and internalization.
Alternative Names | Y2, NPY 2 receptor, neuropeptide Y receptor type 2 |
IUPHAR Target ID | 306 |
UniProt ID | P49146 |
Western Blot (WB) | 1:1000 |
Immunocytochemistry (ICC) | - |
Species Reactivity | Human |
Host / Isotype | Rabbit / IgG |
Class | Polyclonal |
Immunogen | A synthetic phosphopeptide derived from human NPY2 around the phosphorylation site of Ser354/Thr356. |
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 Serine354/Threonine356 phosphorylation of the Neuropeptide Y receptor 2. Upper panel, HEK293 cells stably expressing the NPY2-Receptor (NPY2) were either not exposed or exposed to 1 µM of NPY2 receptor agonist Neuropeptide Y for 30 minutes. Cells were lysed and immunoblotted with the anti-pS354/pT356-NPY2 antibody (7TM0306B) at a dilution of 1:1000. Lower panel, blot was stripped and reprobed with an phosphorylation-independent anti-NPY2 antibody to confirm equal loading of the gel.
Figure 2. Analysis of dose-dependent NPY2 receptor phosphorylation using a panel of phosphosite-specific antibodies. Upper four panels, HEK293 cells stably expressing the NPY2 receptor (NPY2) were either not exposed or exposed to increasing concentrations of Neuropeptide Y ranging from 100 pM to 1 μM for 30 minutes. Cells were lysed and immunoblotted with the anti-pS351/pS354-NPY2 antibody (7TM0306A) or anti-pS354/pT356-NPY2 antibody (7TM0306B) or anti-pS369/pS374-NPY2 antibody (7TM0306C) at a dilution of 1:1000. Lower panel, blot was stripped and reprobed with an phosphorylation-independent anti-NPY2 antibody to confirm equal loading of the gel.
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