Rabbit PRKAA1 Polyclonal Antibody | anti-PRKAA1 antibody

Anti-PRKAA1 Antibody

Cat. Num. AAA419624

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

• Host: Rabbit
• Reactivity: Human, Mouse, Rat
• Clonality: Polyclonal
• Isotype: IgG
• Specificity: Western blot analysis of HeLa cell lysate using PRKAA1 antibody. Immunohistochemistry analysis of paraffin-embedded human prostate cancer, using PRKAA1 antibody. Immunofluorescence analysis of HeLa cell using PRKAA1 antibody.
• Purity/Purification: Affinity Purification
• Form/Format: Liquid
• Concentration: 1mg/ml (varies by lot)
• Sequence Length: 550

• Applicable Applications for anti-PRKAA1 antibody: Western Blot (WB), Immunohistochemistry (IHC), Immunofluorescence (IF), Immunoprecipitation (IP)
• Application Notes: WB: 1:500-1:2000; IHC: 1:50-1:200; IF: 1:50-1:200; IP: 1:20-1:100
• Immunogen: Recombinant protein of human PRKAA1
• Storage Buffer: PBS with 0.02% sodium azide,50% glycerol, pH7.3.
• Preparation and Storage: Store at -20 degree C (regular) and -80 degree C (long term). Avoid freeze / thaw cycles.

Western Blot (WB)

Immunohistochemistry (IHC)

Immunofluorescence (IF)

Related Product Information for anti-PRKAA1 antibody

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 +/- subunit and regulatory 2 and 3 subunits, each of which is encoded by two or three distinct genes (+/-1, 2; 21, 2; 31, 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+/- at Thr172 in the activation loop, and this phosphorylation is required for AMPK activation (3-5). AMPK+/- is also phosphorylated at Thr258 and Ser485 (for +/-1; Ser491 for +/-2). The upstream kinase and the biological significance of these phosphorylation events have yet to be elucidated (6). The 21 subunit is post-translationally modified by myristoylation and multi-site phosphorylation including Ser24/25, Ser96, Ser101, Ser108, and Ser182 (6, 7). Phosphorylation at Ser108 of the 21 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 AMPK3 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 (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).

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 catalytic subunit alpha 1
• NCBI Official Symbol: PRKAA1
• NCBI Official Synonym Symbols: AMPK; AMPKa1
• NCBI Protein Information: 5'-AMP-activated protein kinase catalytic subunit alpha-1
• UniProt Protein Name: 5'-AMP-activated protein kinase catalytic subunit alpha-1
• UniProt Gene Name: PRKAA1
• UniProt Synonym Gene Names: AMPK1; HMGCR kinase

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

Chromosomal Location of Human Ortholog: 5p13.1

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

Molecular Function: AMP-activated protein kinase activity; chromatin binding; histone serine kinase activity; protein binding; protein kinase activity

Biological Process: cell cycle arrest; cellular response to glucose starvation; cellular response to nutrient levels; fatty acid homeostasis; glucose homeostasis; lipid biosynthetic process; macroautophagy; negative regulation of apoptosis; negative regulation of lipid catabolic process; negative regulation of TOR signaling pathway; positive regulation of autophagy; positive regulation of glycolysis; protein amino acid phosphorylation; regulation of circadian rhythm; response to gamma radiation; signal transduction