Rabbit PRKAA1 Polyclonal Antibody | anti-PRKAA1 antibody

Rabbit Anti Human PRKAA1 PolyClonal Antibody

Cat. Num. AAA1488686

• Gene Names: PRKAA1; AMPK; AMPKa1
• Reactivity: Human, Mouse, Rat
• Applications: Western Blot, Immunohistochemistry, Immunoprecipitation
• Purity: Affinity Purification
• Synonyms: PRKAA1; Polyclonal Antibody; Rabbit Anti Human PRKAA1 PolyClonal Antibody; AMPK; AMPKa1; MGC33776; MGC57364AMPKalpha; anti-PRKAA1 antibody

• Host: Rabbit
• Reactivity: Human, Mouse, Rat
• Clonality: Polyclonal
• Isotype: IgG
• Purity/Purification: Affinity Purification
• Sequence Length: 550

• Applicable Applications for anti-PRKAA1 antibody: Western Blot (WB), Immunohistochemistry (IHC), Immunoprecipitation (IP)
• Immunogen: A synthetic peptide of human PRKAA1
• Relevance: 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. 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; beta1, 2; gamma1, 2, 3). The kinase is activated by an elevated AMP/ATP ratio due to cellular and environmental stress, such as heat shock, hypoxia, and ischemia. The tumor suppressor LKB1, in association with accessory proteins STRAD and MO25, phosphorylates AMPKalpha at Thr172 in the activation loop, and this phosphorylation is required for AMPK activation. AMPKalpha 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. The beta1 subunit is post-translationally modified by myristoylation and multi-site phosphorylation including Ser24/25, Ser96, Ser101, Ser108, and Ser182. 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. Several mutations in AMPKgamma subunits have been identified, most of which are located in the putative AMP/ATP binding sites (CBS or Bateman domains). Mutations at these sites lead to reduction of AMPK activity and cause glycogen accumulation in heart or skeletal muscle. 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.
• Storage Buffer: Store at -20 degree C or -80 degree C. Avoid freeze / thaw cycles. Buffer: PBS with 0.02% sodium azide, 50% glycerol, pH7.3.

NCBI and Uniprot Product Information

• NCBI GI #: 27469582
• NCBI GeneID: 5562
• Molecular Weight: 65,523 Da
• NCBI Official Full Name: PRKAA1 protein
• NCBI Official Synonym Full Names: protein kinase, AMP-activated, alpha 1 catalytic subunit
• NCBI Official Symbol: PRKAA1
• NCBI Official Synonym Symbols: AMPK; AMPKa1
• NCBI Protein Information: 5'-AMP-activated protein kinase catalytic subunit alpha-1; ACACA kinase; AMPK alpha 1; HMGCR kinase; AMPK subunit alpha-1; tau-protein kinase PRKAA1; acetyl-CoA carboxylase kinase; AMP -activate kinase alpha 1 subunit; hydroxymethylglutaryl-CoA reductase kinase; AMP-activated protein kinase, catalytic, alpha-1; 5'-AMP-activated protein kinase, catalytic alpha-1 chain
• UniProt Protein Name: 5'-AMP-activated protein kinase catalytic subunit alpha-1
• UniProt Gene Name: PRKAA1
• UniProt Synonym Gene Names: AMPK1; AMPK subunit alpha-1; ACACA kinase; HMGCR kinase
• UniProt Entry Name: AAPK1_HUMAN

NCBI Description

The protein encoded by this gene belongs to the ser/thr protein kinase family. It is the catalytic subunit of the 5'-prime-AMP-activated protein kinase (AMPK). AMPK is a cellular energy sensor conserved in all eukaryotic cells. The kinase activity of AMPK is activated by the stimuli that increase the cellular AMP/ATP ratio. AMPK regulates the activities of a number of key metabolic enzymes through phosphorylation. It protects cells from stresses that cause ATP depletion by switching off ATP-consuming biosynthetic pathways. Alternatively spliced transcript variants encoding distinct isoforms have been observed. [provided by RefSeq, Jul 2008]

Uniprot Description

AMPKA1: 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 a number of metabolic enzymes and transcription regulators. 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. Two isoforms of the human protein are produced by alternative splicing.

Protein type: Protein kinase, CAMK; EC 2.7.11.26; Autophagy; EC 2.7.11.31; Kinase, protein; EC 2.7.11.1; Protein kinase, Ser/Thr (non-receptor); EC 2.7.11.27; CAMK group; CAMKL family; AMPK subfamily

Chromosomal Location of Human Ortholog: 5p12

Cellular Component: nucleoplasm; cytoplasm; apical plasma membrane; intracellular; cytosol; nucleus; AMP-activated protein kinase complex

Molecular Function: AMP-activated protein kinase activity; protein C-terminus binding; cAMP-dependent protein kinase activity; metal ion binding; [acetyl-CoA carboxylase] kinase activity; histone serine kinase activity; protein kinase activity; protein binding; tau-protein kinase activity; chromatin binding; kinase binding; ATP binding; [hydroxymethylglutaryl-CoA reductase (NADPH)] kinase activity

Biological Process: protein heterooligomerization; activation of MAPK activity; lipid biosynthetic process; rhythmic process; positive regulation of cholesterol biosynthetic process; signal transduction; glucose homeostasis; protein amino acid phosphorylation; response to caffeine; cellular response to glucose starvation; cellular response to nutrient levels; negative regulation of lipid catabolic process; regulation of transcription, DNA-dependent; positive regulation of cell proliferation; response to gamma radiation; negative regulation of glucosylceramide biosynthetic process; cell cycle arrest; fatty acid biosynthetic process; positive regulation of autophagy; response to UV; negative regulation of TOR signaling pathway; Wnt receptor signaling pathway; transcription, DNA-dependent; glucose metabolic process; regulation of circadian rhythm; cholesterol biosynthetic process; fatty acid homeostasis; cold acclimation; positive regulation of glycolysis; insulin receptor signaling pathway; response to hypoxia; autophagy; fatty acid oxidation; response to activity; negative regulation of apoptosis