|Description||Serine Phosphopeptide (RRApSVA)|
|Safety Information according to GHS|
|Storage and Shipping Information|
|Storage Conditions||Lyophilized: Stable for 2 years at 4°C . Rehydrated: Stable for 1 year at -20°C.|
|Material Size||1 mg|
|Reference overview||Application||Pub Med ID|
|Phosphorylated synthetic peptides as tools for studying protein phosphatases |
Pinna, L. A. and Donella-Deana, A.
Biochim Biophys Acta, 1222:415-31 (1994) 1994
|Characterization and kinetic analysis of the intracellular domain of human protein tyrosine phosphatase beta (HPTP beta) using synthetic phosphopeptides |
Harder, K. W., et al
Biochem J, 298 ( Pt 2):395-401 (1994) 1994
|Further definition of the substrate specificity of the alpha-herpesvirus protein kinase and comparison with protein kinases A and C |
Leader, D. P., et al
Biochim Biophys Acta, 1091:426-31 (1991) 1991
|The use of phosphopeptides to distinguish between protein phosphatase and acid/alkaline phosphatase activities: opposite specificity toward phosphoseryl/phosphothreonyl substrates. |
Donella-Deana, A, et al.
Biochim. Biophys. Acta, 1094: 130-3 (1991) 1991
The four main classes of protein phosphatases (PP-1, 2A, 2B and 2C), although differing in their ability to dephosphorylate phosphopeptide substrates, invariably display a marked preference toward phosphothreonyl peptides over their phosphoseryl counterparts. Conversely, all the acidic and alkaline phosphatases tested so far dephosphorylate phosphoseryl derivatives far more readily than phosphothreonyl ones. This opposite behaviour provides a criterion for discriminating between protein dephosphorylating activity due to authentic protein phosphatases as compared to nonspecific acid and/or alkaline phosphatases. In particular the phosphothreonyl peptides RRATPVA and RRREEETPEEEAA appear to be especially suited for detecting the activity of PP-2C and PP-2A, since they are hardly dephosphorylated by acid and alkaline phosphatases. Conversely, the phosphoseryl peptides SPEEEEE and RRASPVA can provide a sensitive evaluation of the majority of acid and alkaline phosphatases, while being refractory to protein phosphatases.
|Synthetic peptides as model substrates for the study of the specificity of the polycation-stimulated protein phosphatases. |
Agostinis, P, et al.
Eur. J. Biochem., 189: 235-41 (1990) 1990
The substrate specificity of the different forms of the polycation-stimulated (PCS, type 2A) protein phosphatases and of the active catalytic subunit of the ATP, Mg-dependent (type 1) phosphatase (AMDC) was investigated, using synthetic peptides phosphorylated by either cyclic-AMP-dependent protein kinase or by casein kinase-2. The PCS phosphatases are very efficient toward the Thr(P) peptides RRAT(P)VA and RRREEET(P)EEE when compared with the Ser(P) analogues RRAS(P)VA and RRREEES(P)EEEAA. Despite their distinct sequence, both Thr(P) peptides are excellent substrates for the PCSM and PCSH1 phosphatases, being dephosphorylated faster than phosphorylase a. The slow dephosphorylation of RRAS(P)VA by the PCS phosphatases could be increased substantially by the insertion of N-terminal (Arg) basic residues. In contrast with the latter, the AMDC phosphatase shows very poor activity toward all the phosphopeptides tested, without preference for either Ser(P) or Thr(P) peptides. However, N-terminal basic residues also favor the dephosphorylation of otherwise almost inert substrates by the AMDC phosphatase. Hence, while the dephosphorylation of Thr(P) substrates by the PCS phosphatases is highly favored by the nature of the phosphorylated amino acid, phosphatase activity toward Ser(P)-containing peptides may require specific determinants in the primary structure of the phosphorylation site.
|Dephosphorylation of phosphoproteins and synthetic phosphopeptides. Study of the specificity of the polycation-stimulated and MgATP-dependent phosphorylase phosphatases |
Agostinis, P., et al
J Biol Chem, 262:1060-4 (1987) 1987
|What is the mass of this peptide?||The mass is 738 Daltons.|