Key features and details
- Rabbit polyclonal to AMPK alpha 2 (phospho S173)
- Suitable for: WB, ELISA
- Reacts with: Recombinant fragment
- Isotype: IgG
Product nameAnti-AMPK alpha 2 (phospho S173) antibody
See all AMPK alpha 2 primary antibodies
DescriptionRabbit polyclonal to AMPK alpha 2 (phospho S173)
Tested applicationsSuitable for: WB, ELISAmore details
Species reactivityReacts with: Recombinant fragment
Predicted to work with: Human
Synthetic phospho-peptide corresponding to N-terminal residues (phospho site at 173 Serine) of human AMPK alpha 2 protein
Storage instructionsShipped at 4°C. Upon delivery aliquot and store at -20°C. Avoid freeze / thaw cycles.
Storage bufferPreservative: 0.01% Sodium azide
Constituents: 50% Glycerol, PBS
Concentration information loading...
PurityImmunogen affinity purified
- Pathways and Processes
- Metabolic signaling pathways
- Lipid and lipoprotein metabolism
- Fatty acids
- Pathways and Processes
- Metabolic signaling pathways
- Energy transfer pathways
- Integration of energy
Our Abpromise guarantee covers the use of ab55886 in the following tested applications.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
|WB||Use a concentration of 1 µg/ml. Predicted molecular weight: 62 kDa. This antibody has been tested in Western blot against the recombinant peptide used as an immunogen. We have no data on detection of endogenous protein.|
|ELISA||Use at an assay dependent dilution.|
FunctionCatalytic 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. Regulates lipid synthesis by phosphorylating and inactivating lipid metabolic enzymes such as ACACA, ACACB, GYS1, HMGCR and LIPE; regulates fatty acid and cholesterol synthesis by phosphorylating acetyl-CoA carboxylase (ACACA and ACACB) and hormone-sensitive lipase (LIPE) enzymes, respectively. Regulates insulin-signaling and glycolysis by phosphorylating IRS1, PFKFB2 and PFKFB3. Involved in insulin receptor/INSR internalization (PubMed:25687571). AMPK stimulates glucose uptake in muscle by increasing the translocation of the glucose transporter SLC2A4/GLUT4 to the plasma membrane, possibly by mediating phosphorylation of TBC1D4/AS160. Regulates transcription and chromatin structure by phosphorylating transcription regulators involved in energy metabolism such as CRTC2/TORC2, FOXO3, histone H2B, HDAC5, MEF2C, MLXIPL/ChREBP, EP300, HNF4A, p53/TP53, SREBF1, SREBF2 and PPARGC1A. Acts as a key regulator of glucose homeostasis in liver by phosphorylating CRTC2/TORC2, leading to CRTC2/TORC2 sequestration in the cytoplasm. In response to stress, phosphorylates 'Ser-36' of histone H2B (H2BS36ph), leading to promote transcription. Acts as a key regulator of cell growth and proliferation by phosphorylating TSC2, RPTOR and ATG1/ULK1: in response to nutrient limitation, negatively regulates the mTORC1 complex by phosphorylating RPTOR component of the mTORC1 complex and by phosphorylating and activating TSC2. In response to nutrient limitation, promotes autophagy by phosphorylating and activating ATG1/ULK1. AMPK also acts as a regulator of circadian rhythm by mediating phosphorylation of CRY1, leading to destabilize it. May regulate the Wnt signaling pathway by phosphorylating CTNNB1, leading to stabilize it. Also phosphorylates CFTR, EEF2K, KLC1, NOS3 and SLC12A1. Plays an important role in the differential regulation of pro-autophagy (composed of PIK3C3, BECN1, PIK3R4 and UVRAG or ATG14) and non-autophagy (composed of PIK3C3, BECN1 and PIK3R4) complexes, in response to glucose starvation. Can inhibit the non-autophagy complex by phosphorylating PIK3C3 and can activate the pro-autophagy complex by phosphorylating BECN1.
Sequence similaritiesBelongs to the protein kinase superfamily. CAMK Ser/Thr protein kinase family. SNF1 subfamily.
Contains 1 protein kinase domain.
DomainThe AIS (autoinhibitory sequence) region shows some sequence similarity with the ubiquitin-associated domains and represses kinase activity.
Phosphorylated at Thr-172 by STK11/LKB1 in complex with STE20-related adapter-alpha (STRADA) pseudo kinase and CAB39. Also phosphorylated at Thr-172 by CAMKK2; triggered by a rise in intracellular calcium ions, without detectable changes in the AMP/ATP ratio. CAMKK1 can also phosphorylate Thr-172, but at much lower level. Dephosphorylated by protein phosphatase 2A and 2C (PP2A and PP2C). Phosphorylated by ULK1; leading to negatively regulate AMPK activity and suggesting the existence of a regulatory feedback loop between ULK1 and AMPK. Dephosphorylated by PPM1A and PPM1B at Thr-172 (mediated by STK11/LKB1).
Cellular localizationCytoplasm. Nucleus. In response to stress, recruited by p53/TP53 to specific promoters.
- Information by UniProt
- 5'-AMP-activated protein kinase catalytic subunit alpha-2 antibody
- AAPK2_HUMAN antibody
- ACACA kinase antibody
ab55886 has been referenced in 1 publication.
- Kari S et al. PKA Activates AMPK Through LKB1 Signaling in Follicular Thyroid Cancer. Front Endocrinol (Lausanne) 10:769 (2019). PubMed: 31798532