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Submit ReviewPhospho-Glycogen Synthase Peptide-2 (substrate) is a synthetic peptide suitable as a substrate for glycogen synthase kinase-3 (GSK-3).
M. Wt | 3029 |
Formula | C123H191N40O48P |
Sequence |
YRRAAVPPSPSLSRHSSPHQSEDEEE (Modifications: Ser-21 = OPO3H2) |
Storage | Desiccate at -20°C |
CAS Number | 851366-97-7 |
PubChem ID | 90479786 |
InChI Key | IIMKCITWGMPAKU-LKAJVXBKSA-N |
Smiles | [H]N[C@@H](CC1=CC=C(O)C=C1)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](C)C(=O)N[C@@H](C)C(=O)N[C@@H](C(C)C)C(=O)N1CCC[C@H]1C(=O)N1CCC[C@H]1C(=O)N[C@@H](CO)C(=O)N1CCC[C@H]1C(=O)N[C@@H](CO)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CO)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CC1=CNC=N1)C(=O)N[C@@H](CO)C(=O)N[C@@H](CO)C(=O)N1CCC[C@H]1C(=O)N[C@@H](CC1=CNC=N1)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](COP(O)(O)=O)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CC(O)=O)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CCC(O)=O)C(O)=O |
The technical data provided above is for guidance only. For batch specific data refer to the Certificate of Analysis.
Tocris products are intended for laboratory research use only, unless stated otherwise.
References are publications that support the biological activity of the product.
Sutherland et al (1993) Inactivation of glycogen synthase kinase-3β by phosphorylation: new kinase connections in Ins and growth factor signalling. Biochem.J. 296 15 PMID: 8250835
Woodgett (1989) Use of peptide substrates for affinity purification of protein-serine kinases. Anal.Biochem. 180 237 PMID: 2554753
Keywords: Phospho-Glycogen Synthase Peptide-2 (substrate), Phospho-Glycogen Synthase Peptide-2 (substrate) supplier, GSK-3, synthetic, Glycogen, synthase, kinase-3, kinases, Carbohydrate, Metabolism, Enzyme, Substrates, Activators, GSpeptide2, GS, peptide-2, /, Synthase, Kinase, 3, 1352, Tocris Bioscience
Citations are publications that use Tocris products. Selected citations for Phospho-Glycogen Synthase Peptide-2 (substrate) include:
Stoothoff et al (2005) FRAT-2 preferentially increases glycogen synthase kinase 3 β-mediated phosphorylation of primed sites, which results in enhanced tau phosphorylation. PLoS One 280 270 PMID: 15522877
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