P6993
Protein Phosphatase 2A1 bovine
≥1500 units/mg protein
Synonyme(s) :
PPA2A1
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About This Item
Produits recommandés
Source biologique
bovine
Niveau de qualité
Pureté
≥90% (SDS-PAGE)
Forme
solution
Activité spécifique
≥1500 units/mg protein
Poids mol.
192 kDa
Conditionnement
vial of 1 μg
Conditions d'expédition
dry ice
Température de stockage
−70°C
Description générale
Protein Phosphatase 2A1 (PP2A1) belongs to the PP2A family and comprises trimeric A, B and C subunits. PPA2 enzymes are serine/threonine phosphatases and exist as several isoforms.
Application
Protein phosphatase 2A1 has been used to treat human fibroblast cells prior to western blot analysis.
Actions biochimiques/physiologiques
Protein Phosphatase 2A is a cytoplasmic protein, which colocalizes with microtubule proteins and is involved in the dephosphorylation of the tau protein and oncoprotein 18. Protein Phosphatase 2A1 (PP2A1) binds to polymerized microtubule proteins and may be targeted by tubulin in modulating phosphatase activity. PP2A1 is implicated as a growth suppressor and is associated with dysregulation in cancer. It also regulates cell cycle, RNA splicing differentiation, and signal transduction. PP2A dysfunction is correlated to the tau protein deregulation in Alzheimer′s disease pathophysiology. Protein Phosphatase 2A1 is a divalent cation-dependent protein serine/threonine phosphatase implicated as a growth suppressor and is associated with dysregulation in cancer.
Définition de l'unité
One unit will release 1.0 nanomole of phosphate from 32P-labeled phosphorylase A per minute at pH 7.0 at 30 °C.
Forme physique
Solution in 50 mM Tris-HCl, pH 7.0, containing 14 mM 2-mercaptoethanol, 1 mM benzamidine, 0.1 mM PMSF, 1 mM EDTA, and 50% glycerol
Mention d'avertissement
Warning
Mentions de danger
Conseils de prudence
Classification des risques
Skin Sens. 1
Code de la classe de stockage
10 - Combustible liquids
Classe de danger pour l'eau (WGK)
WGK 2
Point d'éclair (°F)
Not applicable
Point d'éclair (°C)
Not applicable
Certificats d'analyse (COA)
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K Webley et al.
Molecular and cellular biology, 20(8), 2803-2808 (2000-03-25)
Replicative senescence in human fibroblasts is absolutely dependent on the function of the phosphoprotein p53 and correlates with activation of p53-dependent transcription. However, no evidence for posttranslational modification of p53 in senescence has been presented, raising the possibility that changes
A Hiraga et al.
The Biochemical journal, 346 Pt 2, 433-439 (2000-03-24)
Protein phosphatase (PP) 2A1, a trimer composed of A-, B- and C-subunits in the PP2A family, has been regarded as a principal form localizing at microtubules (MT), but PP2A2, the dimer of A- and C-subunits, has not. Substantiating the claim
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