07-095
Anti-PP2A-methylesterase/PME-1 Antibody
Upstate®, from rabbit
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About This Item
Recommended Products
biological source
rabbit
Quality Level
antibody form
purified immunoglobulin
antibody product type
primary antibodies
clone
polyclonal
species reactivity
human, rat, mouse
manufacturer/tradename
Upstate®
technique(s)
western blot: suitable
isotype
IgG
NCBI accession no.
UniProt accession no.
shipped in
dry ice
target post-translational modification
unmodified
Gene Information
human ... PPME1(51400)
Specificity
Protein Phosphatase Methylesterase-1
Immunogen
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.
Quality
routinely evaluated by immunoblot on RIPA lysates from mouse 3T3 fibroblasts
Target description
44kDa
Physical form
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
Storage and Stability
2 years at -20°C
Analysis Note
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.
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.
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Storage Class Code
10 - Combustible liquids
WGK
WGK 1
Certificates of Analysis (COA)
Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.
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Single-pot enzymatic synthesis of Dicer-substrate siRNAs.
Nucleic Acids Research null
PloS one, 12(12), e0189413-e0189413 (2017-12-19)
Soluble forms of oligomeric beta-amyloid (Aβ) are thought to play a central role in Alzheimer's disease (AD). Transgenic manipulation of methylation of the serine/threonine protein phosphatase, PP2A, was recently shown to alter the sensitivity of mice to AD-related impairments resulting
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
The Journal of neuroscience : the official journal of the Society for Neuroscience, 40(23), 4596-4608 (2020-04-29)
Beta-amyloid (Aβ) is thought to play a critical role in Alzheimer's disease (AD), and application of soluble oligomeric forms of Aβ produces AD-like impairments in cognition and synaptic plasticity in experimental systems. We found previously that transgenic overexpression of the
The Journal of biological chemistry, 274(20), 14382-14391 (1999-05-13)
Carboxymethylation of proteins is a highly conserved means of regulation in eukaryotic cells. The protein phosphatase 2A (PP2A) catalytic (C) subunit is reversibly methylated at its carboxyl terminus by specific methyltransferase and methylesterase enzymes which have been purified, but not
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