12-220
Serine Phosphopeptide (RRApSVA)
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About This Item
Produits recommandés
Fabricant/nom de marque
Upstate®
Niveau de qualité
Technique(s)
activity assay: suitable
Conditions d'expédition
wet ice
Actions biochimiques/physiologiques
Protein Target: Alkaline Phosphatase
Qualité
Routinely evaluated by using the phosphopeptide as a substrate for Alkaline Phosphatase in a non-radioactive malachite green based enzyme assay. The assay was performed using the Alkaline/Acid Phosphatase Assay Kit (R-R-A-pS-V-A), (17-128).
Forme physique
Lyophilized powder
Stockage et stabilité
Lyophilized: Stable for 2 years at 4°C . Rehydrated: Stable for 1 year at -20°C.
Informations légales
UPSTATE is a registered trademark of Merck KGaA, Darmstadt, Germany
Clause de non-responsabilité
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.
Code de la classe de stockage
11 - Combustible Solids
Classe de danger pour l'eau (WGK)
WGK 3
Point d'éclair (°F)
Not applicable
Point d'éclair (°C)
Not applicable
Certificats d'analyse (COA)
Recherchez un Certificats d'analyse (COA) en saisissant le numéro de lot du produit. Les numéros de lot figurent sur l'étiquette du produit après les mots "Lot" ou "Batch".
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Retrouvez la documentation relative aux produits que vous avez récemment achetés dans la Bibliothèque de documents.
Synthetic peptides as model substrates for the study of the specificity of the polycation-stimulated protein phosphatases.
European Journal of Biochemistry, 189, 235-241 (1990)
Dephosphorylation of phosphoproteins and synthetic phosphopeptides. Study of the specificity of the polycation-stimulated and MgATP-dependent phosphorylase phosphatases
The Journal of Biological Chemistry, 262, 1060-1064 (1987)
Further definition of the substrate specificity of the alpha-herpesvirus protein kinase and comparison with protein kinases A and C
Biochimica et Biophysica Acta, 1091, 426-431 (1991)
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
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