Anti -AMP Activated Protein Kinase 1, phosphorylated (AMPK)

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

Chromosome: 1; NC_000001.10 (57110990..57181008). Location: 1p31

Monoclonal

7H5

Rabbit

Detects endogenous levels of AMPK alpha1 only when phosphorylated at Ser485. The antibody does not cross-react with phosphorylated AMPK alpha2 or other related proteins. Species Crossreactivity: human, hamster, monkey, mouse and rat.

Supernatant
Supernatant

Supplied as a liquid in 10mM sodium HEPES, 150mM sodium chloride 0.1mg/ml BSA, <0.02% sodium azide, 50% glycerol.

May be stored at 4 degree C for short-term only. For long-term storage, store at -20 degree C. Aliquots are stable for at least 12 months at -20 degree C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Further dilutions can be made in assay buffer.

Small volumes of anti-PRKAA2 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.

AMP-activated protein kinase (AMPK) is highly conserved from yeast to plants and animals and plays a key role in the regulation of energy homeostasis (1). AMPK is a heterotrimeric complex composed of a catalytic alpha subunit and regulatory beta and gamma subunits, each of which is encoded by two or three distinct genes (alpha1, 2; beta 1, 2; gamma1, 2, 3) (2). The kinase is activated by an elevated AMP/ATP ratio due to cellular and environmental stress, such as heat shock, hypoxia and ischemia (1). The tumor suppressor LKB1, in association with accessory proteins STRAD and MO25, phosphorylates AMPK alpha at Thr172 in the activation loop and this phosphorylation is required for AMPK activation (3-5). AMPK alpha is also phosphorylated at Thr258 and Ser485 (for alpha1; Ser491 for alpha2). The upstream kinase and the biological significance of these phosphorylation events have yet to be elucidated (6). The beta1 subunit is post-translationally modified by myristoylation and multisite phosphorylation including Ser24/25, Ser96, Ser101, Ser108 and Ser182 (6,7). Phosphorylation at Ser108 of the beta1 subunit seems to be required for the activation of AMPK enzyme, while phosphorylation at Ser24/25 and Ser182 affects AMPK localization (7). Several mutations in AMPK gamma subunits have been identified, most of which are located in the putative AMP/ATP s (CBS or Bateman domains). Mutations at these sites lead to reduction of AMPK activity and cause glycogen accumulation in heart or skeletal muscle (1,2). Accumulating evidence indicates that AMPK not only regulates the metabolism of fatty acids and glycogen, but also modulates protein synthesis and cell growth through EF2 and TSC2/mTOR pathways, as well as blood flow via eNOS/nNOS (1).

Antibodies; Abs to Protein Kinases

Western Blot (WB)

Suitable for use in Western Blot
Dilution: Western Blot: 1:1000

62,320 Da[Similar Products]

protein kinase, AMP-activated, alpha 2 catalytic subunit

5'-AMP-activated protein kinase catalytic subunit alpha-2; AMPK-alpha-2 chain; OTTHUMP00000009993; AMPK subunit alpha-2; 5'-AMP-activated protein kinase, catalytic alpha-2 chain

5'-AMP-activated protein kinase catalytic subunit alpha-2

AMPK; AMPK2??[Similar Products]

AAPK2_HUMAN

The protein encoded by this gene is a catalytic 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. Studies of the mouse counterpart suggest that this catalytic subunit may control whole-body insulin sensitivity and is necessary for maintaining myocardial energy homeostasis during ischemia. [provided by RefSeq]

AMPKA2: a catalytic subunit of AMP-activated protein kinase (AMPK). Acts as an energy sensor, playing a key role in regulating cellular energy metabolism. A protein kinase of the CAMKL family whose activation is regulated by the balance between ADP/AMP/ATP, and intracellular Ca(2+) levels. Acts as a metabolic stress-sensing protein kinase switching off biosynthetic pathways when cellular ATP levels are depleted and when 5'-ADP and -AMP rise in response to fuel limitation and/or hypoxia. Activates energy-producing pathways and inhibits energy-consuming processes. Restores ATP levels in cells by switching off anabolic and switching on catabolic pathways. Activated primarily by rising ADP levels and not, as previously thought, solely by AMP. AMPK resembles an adenylate charge regulatory system in which anabolic and catabolic pathways are regulated by adenine nucleotide ratios. Acts via direct phosphorylation of metabolic enzymes and transcription regulators. Regulates fatty acid synthesis by phosphorylating acetyl-CoA carboxylase. Regulates cholesterol synthesis by phosphorylating and inactivating hormone-sensitive lipase and hydroxymethylglutaryl-CoA reductase. Activated by at least two distinct upstream kinases: the tumor suppressor LKB1 and CaMKK2. Also acts as a regulator of cellular polarity by remodeling the actin cytoskeleton, probably by indirectly activating myosin. AMPK is a heterotrimer of an alpha catalytic subunit (AMPKA1 or -2), a beta (AMPKB1 or -2) and a gamma non-catalytic subunit (AMPKG1, -2 or -3). Different possible combinations of subunits give rise to 12 different holoenzymes. Binding of ADP or AMP to non-catalytic gamma subunit (PRKAG1, -2 or -3) results in allosteric activation. AMPK is activated by antihyperglycemic drug metformin, a drug prescribed to patients with type 2 diabetes: in vivo, metformin seems to mainly inhibit liver gluconeogenesis. However, metformin can be used to activate AMPK in muscle and other cells in culture or ex vivo. Selectively inhibited by compound C (6-[4-(2-Piperidin-1-yl-ethoxy)-phenyl)]-3-pyridin-4-yl-pyyrazolo[1,5-a] pyrimidine. Activated by resveratrol, a natural polyphenol present in red wine, and S17834, a synthetic polyphenol. Salicylate/aspirin directly activates kinase activity. Studies in the mouse suggest that AMPK2 may control whole-body insulin sensitivity and is necessary for maintaining myocardial energy homeostasis during ischemia.

Protein type: Autophagy; EC 2.7.11.1; EC 2.7.11.31; Protein kinase, CAMK; EC 2.7.11.27; Kinase, protein; Protein kinase, Ser/Thr (non-receptor); CAMK group; CAMKL family; AMPK subfamily

Chromosomal Location of Human Ortholog: 1p31

Cellular Component: nucleoplasm; cytosol

Molecular Function: AMP-activated protein kinase activity; protein serine/threonine kinase activity; protein binding; metal ion binding; protein serine/threonine/tyrosine kinase activity; [acetyl-CoA carboxylase] kinase activity; chromatin binding; histone serine kinase activity; ATP binding; [hydroxymethylglutaryl-CoA reductase (NADPH)] kinase activity; protein kinase activity

Biological Process: lipid biosynthetic process; rhythmic process; cellular lipid metabolic process; carnitine shuttle; signal transduction; glucose homeostasis; protein amino acid phosphorylation; cellular response to glucose starvation; cellular response to nutrient levels; regulation of fatty acid biosynthetic process; regulation of transcription, DNA-dependent; response to stress; cell cycle arrest; fatty acid biosynthetic process; positive regulation of autophagy; mitochondrion organization and biogenesis; negative regulation of TOR signaling pathway; Wnt receptor signaling pathway; transcription, DNA-dependent; organelle organization and biogenesis; regulation of circadian rhythm; cholesterol biosynthetic process; fatty acid homeostasis; positive regulation of glycolysis; energy reserve metabolic process; insulin receptor signaling pathway; autophagy; negative regulation of apoptosis

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