For Research Use Only. Not for use in diagnostic procedures.

Polyclonal

Rabbit

Small volumes of anti-PRKAG3 antibody vial(s) may occasionally become entrapped in the seal of the product vial during shipment and storage. If necessary, briefly centrifuge the vial on a tabletop centrifuge to dislodge any liquid in the container`s cap. Certain products may require to ship with dry ice and additional dry ice fee may apply.

Polyclonal

Western Blot (WB), Immunohistochemistry (IHC)

Immunohistochemistry of paraffin-embedded human kidney using PRKAG3 antibody at dilution of 1:100 (40x lens).

Immunofluorescence analysis of A549 cells using PRKAG3 antibody. Blue: DAPI for nuclear staining.

489

protein kinase, AMP-activated, gamma 3 non-catalytic subunit

5'-AMP-activated protein kinase subunit gamma-3; AMPK gamma3; AMPK gamma-3 chain; AMPK subunit gamma-3; 5'-AMP-activated protein kinase, gamma-3 subunit

5'-AMP-activated protein kinase subunit gamma-3

AMPKG3; AMPK gamma3; AMPK subunit gamma-3??[Similar Products]

AAKG3_HUMAN

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 is one of the gamma regulatory subunits of AMPK. It is dominantly expressed in skeletal muscle. Studies of the pig counterpart suggest that this subunit may play a key role in the regulation of energy metabolism in skeletal muscle. [provided by RefSeq, Jul 2008]

AMPKG3: AMP/ATP-binding 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. Gamma non-catalytic subunit mediates binding to AMP, ADP and ATP, leading to activate or inhibit AMPK: AMP-binding results in allosteric activation of alpha catalytic subunit (PRKAA1 or PRKAA2) both by inducing phosphorylation and preventing dephosphorylation of catalytic subunits. ADP also stimulates phosphorylation, without stimulating already phosphorylated catalytic subunit. ATP promotes dephosphorylation of catalytic subunit, rendering the AMPK enzyme inactive. AMPK is a heterotrimer of an alpha catalytic subunit (PRKAA1 or PRKAA2), a beta (PRKAB1 or PRKAB2) and a gamma non- catalytic subunits (PRKAG1, PRKAG2 or PRKAG3). Interacts with FNIP1 and FNIP2. Skeletal muscle, with weak expression in heart and pancreas. Belongs to the 5'-AMP-activated protein kinase gamma subunit family. 2 isoforms of the human protein are produced by alternative splicing.

Protein type: Protein kinase, regulatory subunit

Chromosomal Location of Human Ortholog: 2q35

Cellular Component: extracellular space; cytosol; AMP-activated protein kinase complex

Molecular Function: AMP-activated protein kinase activity; protein kinase binding; ATP binding

Biological Process: mitochondrion organization and biogenesis; glycogen biosynthetic process; organelle organization and biogenesis; insulin receptor signaling pathway; glucose transport; cell cycle arrest; protein amino acid phosphorylation; fatty acid biosynthetic process

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