Anti-PRKAG2 Antibody detects endogenous levels of total PRKAG2 protein.
PRKAG2 (protein kinase, AMP-activated, γ2 non-catalytic subunit) is a non-catalytic regulatory subunit of heterotrimeric AMP-activated protein kinase (AMPK), involved in the energy metabolism. It is predominantly present in all subcellular fractions, including the nuclei.
Immunogen
The antiserum was produced against synthesized peptide derived from human PRKAG2.
Immunogen Range: 1-50
Application
Anti-PRKAG2, N-Terminal antibody produced in rabbit is suitable for immunohistochemistry and indirect immunofluorescence.
Biochem/physiol Actions
PRKAG2 (protein kinase, AMP-activated, γ2 non-catalytic subunit) acts as a sensor of cellular energy status that is controlled by AMP (positively) and ATP (negatively). In normal state CBS domains from AMP-activated protein kinase can bind AMP, ATP, or S-adenosyl methionine. But in mutated condition, it cannot bind. As a result, it leads to hereditary diseases. Its major activity is involved in the regulation of energy homeostasis. It plays an important role in correcting of cell division and chromosome segregation during mitosis. Mutation in PRKAG2 causes Wolff-Parkinson-White (WPW) syndrome, a rare autosomal dominant inheritance disease.
Features and Benefits
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Physical form
Rabbit IgG in phosphate buffered saline (without Mg2+ and Ca2+), pH 7.4, 150mM NaCl, 0.02% sodium azide and 50% glycerol.
AMP-activated protein kinase has been shown to be a key regulator of energy homeostasis; it has also been identified as a tumor suppressor and is required for correct cell division and chromosome segregation during mitosis. The enzyme is a heterotrimer
The Journal of biological chemistry, 284(36), 23902-23911 (2009-07-03)
Ultrasensitivity, hysteresis (a form of biochemical memory), and all-or-none (digital) responses are important signaling properties for the control of irreversible processes and are well characterized in the c-Jun N-terminal kinase (JNK) system using Xenopus oocytes. Our aim was to study
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