P6993
Protein Phosphatase 2A1 bovine
≥1500 units/mg protein
Synonym(e):
PPA2A1
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About This Item
Empfohlene Produkte
Biologische Quelle
bovine
Qualitätsniveau
Assay
≥90% (SDS-PAGE)
Form
solution
Spezifische Aktivität
≥1500 units/mg protein
Mol-Gew.
192 kDa
Verpackung
vial of 1 μg
Versandbedingung
dry ice
Lagertemp.
−70°C
Allgemeine Beschreibung
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.
Anwendung
Protein phosphatase 2A1 has been used to treat human fibroblast cells prior to western blot analysis.
Biochem./physiol. Wirkung
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.
Einheitendefinition
One unit will release 1.0 nanomole of phosphate from 32P-labeled phosphorylase A per minute at pH 7.0 at 30 °C.
Physikalische Form
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
Signalwort
Warning
H-Sätze
Gefahreneinstufungen
Skin Sens. 1
Lagerklassenschlüssel
10 - Combustible liquids
WGK
WGK 2
Flammpunkt (°F)
Not applicable
Flammpunkt (°C)
Not applicable
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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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