12-219
Threonine Phosphopeptide
lyophilized powder, K-R-pT-I-R-R
Synonym(s):
Phosphopeptide K-R, Phosphopeptide K-R-pT-I-R-R, Threonine Phosphopeptide
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About This Item
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product name
Threonine Phosphopeptide (K-R-pT-I-R-R),
manufacturer/tradename
Upstate®
Quality Level
technique(s)
activity assay: suitable (kinase)
shipped in
wet ice
Biochem/physiol Actions
Protein Target: PP2A
Quality
Routinely evaluated by using this phosphopeptide as a substrate for PP2A (14-111) using the PP2A Immunoprecipitation Phosphatase Assay Kit (17-313). Testing may also be performed using the Ser/Thr Phosphatase Assay Kit 1 (17-127).
Physical form
Lyophilized powder
Storage and Stability
Lyophilized: Stable for 2 years at 4°C . Rehydrated: Stable for 1 year at -20°C.
Legal Information
UPSTATE is a registered trademark of Merck KGaA, Darmstadt, Germany
Disclaimer
Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
Storage Class
11 - Combustible Solids
wgk_germany
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
Certificates of Analysis (COA)
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The Journal of biological chemistry, 273(21), 13119-13128 (1998-05-28)
Although the available evidence suggests that whereas the caspase family plays a major role in apoptosis, they are not the sole stimulators of death. A random yeast two-hybrid screen of a lymphocyte cDNA library (using caspase-3 as the bait) found
European journal of biochemistry, 205(1), 241-248 (1992-04-01)
p34cdc2 kinase, a critical regulator of the cell cycle, has been shown to recognize the consensus sequence S/TP in proteins such as histone H1, the retinoblastoma gene product RB and the carboxyl-terminal domain of eukaryotic RNA polymerase II. Using phosphorylated
Phosphorylated synthetic peptides as tools for studying protein phosphatases.
Biochimica et biophysica acta, 1222(3), 415-431 (1994-07-21)
The Biochemical journal, 298 ( Pt 2), 395-401 (1994-03-01)
The intracellular domain of human protein tyrosine phosphatase beta (HPTP beta) (44 kDa) was expressed in bacteria, purified using epitope 'tagging' immunoaffinity chromatography, and characterized with respect to kinetic profile, substrate specificity and potential modulators of enzyme activity. A chromogenic
Biochimica et biophysica acta, 1094(1), 130-133 (1991-08-13)
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
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