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Documentos clave

14-595-M

Sigma-Aldrich

PP1α Protein, 10 µg

Recombinant, full length, human PP1α, for use in Phosphatase Assays.

Sinónimos:

PPP1C, Phosphoprotein phosphatase 1, Phosphorylase phosphatase

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About This Item

Código UNSPSC:
12352200
eCl@ss:
32160405
NACRES:
NA.32

origen biológico

human

Nivel de calidad

recombinante

expressed in E. coli

Formulario

solution

caducidad

6 mo.

mol peso

Mw 37.6 kDa

fabricante / nombre comercial

Upstate®

técnicas

activity assay: suitable (phosphatase)

solubilidad

water: soluble

Nº de acceso UniProt

temp. de almacenamiento

−20°C

Información sobre el gen

human ... PPP1CA(5499)

Descripción general

Research area: Neuroscience
Protein Phosphatase 1 (PP1) is one of the key serine/threonine-specific protein phosphatases.

Aplicación

Research Category
Inflammation & Immunology

Acciones bioquímicas o fisiológicas

Protein Target: PP1α Target Sub-Family: Ser/Thr phosphatase

Protein Phosphatase 1 (PP1) has been associated with a wide range of biological processes, including synaptic plasticity, cell cycle progression, dopaminergic neurotransmission, contraction, and glycogen metabolism, maintaining microtubule stability and the dephosphorylation of tau. Furthermore, PP-1 plays a vital role in synaptic development, plasticity, signaling, neurite outgrowth, synapse formation, ion channel function, and neurotransmission. Changes in PP-1 signaling within dendritic spines have been linked to various neurological and psychiatric disorders.

Envase

Also available in 250 µg size --call for pricing and availability and reference catalog number 14-595M when ordering the 250 µg size.

Calidad

routinely evaluated by dephosphorylation of 100μM DiFMUP

Forma física

Heparin agarose followed by Q agarose

Almacenamiento y estabilidad

6 months at -20°C from date of shipment

Otras notas

For Specific Activity data, refer to the Certificate of Analysis for individual lots of this enzyme

Información legal

UPSTATE is a registered trademark of Merck KGaA, Darmstadt, Germany

Cláusula de descargo de responsabilidad

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.

Pictogramas

Exclamation mark

Palabra de señalización

Warning

Frases de peligro

Clasificaciones de peligro

Skin Sens. 1

Código de clase de almacenamiento

12 - Non Combustible Liquids

Clase de riesgo para el agua (WGK)

WGK 1


Certificados de análisis (COA)

Busque Certificados de análisis (COA) introduciendo el número de lote del producto. Los números de lote se encuentran en la etiqueta del producto después de las palabras «Lot» o «Batch»

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Visite la Librería de documentos

Karl Foley et al.
The Journal of neuroscience : the official journal of the Society for Neuroscience, 41(14), 3040-3050 (2021-04-09)
Protein phosphatases, by counteracting protein kinases, regulate the reversible phosphorylation of many substrates involved in synaptic plasticity, a cellular model for learning and memory. A prominent phosphatase regulating synaptic plasticity and neurologic disorders is the serine/threonine protein phosphatase 1 (PP1).
Targeting phosphatases as the next generation of disease modifying therapeutics for Parkinson?s disease
Braithwaite SP, et al.
Neurochemistry International, 61, 899-906 (2012)
Alphonse Garcia et al.
Biochimie, 85(8), 721-726 (2003-10-31)
The reversible phosphorylation of proteins controlled by protein kinases and protein phosphatases is a major mechanism that regulates a wide variety of cellular processes. In contrast to C. elegans, recent studies in mammalian cells have highlighted a major role of
Modulation of dendritic spines by protein phosphatase-1
Advances in Pharmacology, 90.0, 117-144 (2021)
The role of protein phosphatase-1 in the modulation of synaptic and structural plasticity.
Munton, Richard P, et al.
Febs Letters, 567, 121-128 (2004)

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