Recombinant protein phosphatase 1, catalytic subunit, gamma isoform
Aplicación
Anti-PPP1CC antibody produced in chicken is suitable for western blotting analysis at a dilution of 1:500, for tissue or cell staining at a dilution of 1:200.
Acciones bioquímicas o fisiológicas
Serine/threonine-protein phosphatase PP1-γ catalytic subunit is an enzyme encoded by the PPP1CC gene in humans. A novel phosphatidic acid (PA) binding region on PP1c-γ is identified that contains a unique loop-strand structural fold responsible for the interaction with PA. PP1c γ may function as a mediator of PA action in cells. There may be an existence of a specific high affinity PA-binding domain on the enzyme. Its overexpression promotes vascular smooth muscle cell survival by interfering with JNK1 and p53 phosphorylation cascades involved in apoptosis.
Forma física
Solution in phosphate buffered saline containing 0.02% sodium azide.
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.
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Phosphatidic acid (PA) has been recognized as a lipid second messenger, yet few cellular targets for PA have been identified. Previous work demonstrated PA as a potent and noncompetitive tight-binding inhibitor of the catalytic subunit (gamma isoform) of protein phosphatase-1
The Journal of biological chemistry, 283(32), 22193-22205 (2008-06-10)
The development of therapeutic strategies to inhibit reactive oxygen species (ROS)-mediated damage in blood vessels has been limited by a lack of specific targets for intervention. Targeting ROS-mediated events in the vessel wall is of interest, because ROS play important
The Journal of biological chemistry, 277(18), 15530-15538 (2002-02-22)
Phosphatidic acid (PA) has been identified as a bioactive lipid second messenger, yet despite extensive investigation, no cellular target has emerged as a mediator of its described biological effects. In this study, we identify the gamma isoform of the human
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