07-095
Anti-PP2A-methylesterase/PME-1 Antibody
Upstate®, from rabbit
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A propos de cet article
Code UNSPSC :
12352203
eCl@ss :
32160702
Nomenclature NACRES :
NA.41
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Laissez-nous vous aiderSource biologique
rabbit
Niveau de qualité
Conjugué
unconjugated
Forme d'anticorps
purified immunoglobulin
Type de produit anticorps
primary antibodies
Clone
polyclonal
Espèces réactives
human, rat, mouse
Fabricant/nom de marque
Upstate®
Technique(s)
western blot: suitable
Isotype
IgG
Numéro d'accès NCBI
Numéro d'accès UniProt
Conditions d'expédition
dry ice
Modification post-traductionnelle de la cible
unmodified
Informations sur le gène
human ... PPME1(51400)
Description générale
44kDa
Immunogène
A mixture of two nickel agarose-purified, His6-tagged, bacterial expressed human Protein Phosphatase Methylesterase-1 (PME-1) fragments (residues 225-302 and 277-387). These two fragments represent the carboxyl-terminal portion of the protein.
Application
Research Category
Signaling
Neuroscience
Signaling
Neuroscience
Research Sub Category
Neurotransmitters & Receptors
Neurodegenerative Diseases
Neurotransmitters & Receptors
Neurodegenerative Diseases
This Anti-PP2A-methylesterase/PME-1 Antibody is validated for use in IP, WB for the detection of PP2A-methylesterase/PME-1.
Actions biochimiques/physiologiques
Protein Phosphatase Methylesterase-1
Forme physique
0.1M Tris-glycine, pH 7.4, 0.15M NaCl, 0.05% sodium azide before the addition of glycerol to 30%
Format: Purified
Protein A chromatography
Notes préparatoires
2 years at -20°C
Remarque sur l'analyse
Control
Positive Antigen Control: Catalog #12-305, 3T3/A31 lysate. Add 2.5 μL of 2-mercapto-ethanol/100 μL of lysate and boil for 5 minutes to reduce the preparation. Load 20 μg of reduced lysate per lane for minigels.
Positive Antigen Control: Catalog #12-305, 3T3/A31 lysate. Add 2.5 μL of 2-mercapto-ethanol/100 μL of lysate and boil for 5 minutes to reduce the preparation. Load 20 μg of reduced lysate per lane for minigels.
routinely evaluated by immunoblot on RIPA lysates from mouse 3T3 fibroblasts
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.
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Code de la classe de stockage
10 - Combustible liquids
Classe de danger pour l'eau (WGK)
WGK 1
Certificats d'analyse (COA)
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Single-pot enzymatic synthesis of Dicer-substrate siRNAs.
Guiley, KZ; Pratt, AJ; MacRae, IJ
Nucleic Acids Research null
Madhumathi Gnanaprakash et al.
Journal of Alzheimer's disease : JAD, 79(4), 1813-1829 (2021-01-19)
The serine/threonine protein phosphatase, PP2A, is thought to play a central role in the molecular pathogenesis of Alzheimer's disease (AD), and the activity and substrate specificity of PP2A is regulated, in part, through methylation and demethylation of its catalytic subunit.
Hye-Jin Park et al.
Annals of clinical and translational neurology, 3(10), 769-780 (2016-10-19)
Protein phosphatase 2A (PP2A) is a heterotrimeric holoenzyme composed of a catalytic C subunit, a structural A subunit, and one of several regulatory B subunits that confer substrate specificity. The assembly and activity of PP2A are regulated by reversible methylation
Christina Ising et al.
Nature, 575(7784), 669-673 (2019-11-22)
Alzheimer's disease is characterized by the accumulation of amyloid-beta in plaques, aggregation of hyperphosphorylated tau in neurofibrillary tangles and neuroinflammation, together resulting in neurodegeneration and cognitive decline1. The NLRP3 inflammasome assembles inside of microglia on activation, leading to increased cleavage
Ha Yin Lee et al.
Science signaling, 11(512) (2018-01-11)
Cancer cells increase glucose metabolism to support aerobic glycolysis. However, only some cancer cells are acutely sensitive to glucose withdrawal, and the underlying mechanism of this selective sensitivity is unclear. We showed that glucose deprivation initiates a cell death pathway
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