|Application ||WB, E|
|Calculated MW||30302 Da|
|Antigen Region||3-33 aa|
|Other Names||5'-AMP-activated protein kinase subunit beta-2, AMPK subunit beta-2, PRKAB2|
|Target/Specificity||This AMPK beta2 (PRKAB2) antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 3-33 amino acids from the N-terminal region of human AMPK beta2 (PRKAB2).|
|Format||Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is purified through a protein A column, followed by peptide affinity purification.|
|Storage||Maintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.|
|Precautions||AMPK beta2 (PRKAB2) Antibody (N-term) is for research use only and not for use in diagnostic or therapeutic procedures.|
|Function||Non-catalytic subunit of AMP-activated protein kinase (AMPK), an energy sensor protein kinase that plays a key role in regulating cellular energy metabolism. In response to reduction of intracellular ATP levels, AMPK activates energy-producing pathways and inhibits energy-consuming processes: inhibits protein, carbohydrate and lipid biosynthesis, as well as cell growth and proliferation. AMPK acts via direct phosphorylation of metabolic enzymes, and by longer-term effects via phosphorylation of transcription regulators. Also acts as a regulator of cellular polarity by remodeling the actin cytoskeleton; probably by indirectly activating myosin. Beta non-catalytic subunit acts as a scaffold on which the AMPK complex assembles, via its C-terminus that bridges alpha (PRKAA1 or PRKAA2) and gamma subunits (PRKAG1, PRKAG2 or PRKAG3).|
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Provided below are standard protocols that you may find useful for product applications.
The protein encoded by this gene is a regulatory subunit of the AMP-activated protein kinase (AMPK). AMPK is a heterotrimer consisting of an alpha catalytic subunit, and non-catalytic beta and gamma subunits. AMPK is an important energy-sensing enzyme that monitors cellular energy status. In response to cellular metabolic stresses, AMPK is activated, and thus phosphorylates and inactivates acetyl-CoA carboxylase (ACC) and beta-hydroxy beta-methylglutaryl-CoA reductase (HMGCR), key enzymes involved in regulating de novo biosynthesis of fatty acid and cholesterol. This subunit may be a positive regulator of AMPK activity. The myristoylation and phosphorylation of this subunit have been shown to affect the enzyme activity and cellular localization of AMPK. This subunit may also serve as an adaptor molecule mediating the association of the AMPK complex.
Minokoshi, Y., et al., Nature 428(6982):569-574 (2004).
Prochazka, M., et al., Mol. Cell. Probes 16(6):421-427 (2002).
Park, S.H., et al., J. Appl. Physiol. 93(6):2081-2088 (2002).
Xu, X.R., et al., Proc. Natl. Acad. Sci. U.S.A. 98(26):15089-15094 (2001).
Thornton, C., et al., J. Biol. Chem. 273(20):12443-12450 (1998).
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