Active • Host: Insect cells • AA: 1-559, 1-270, and 1-331 for the α1, β1, and γ1 subunits • Tag: C-terminal His • MW: ~146 kDa
Technical Support & Resources

Visit our FAQ

Contact Us

Toll Free Phone (USA and Canada Only): (888) 526-5351
Direct Phone: (734) 975-3888

Request Technical Support

Technical Support Request

To streamline the process attach the appropriate questionnaire to your inquiry.

Download IHC QuestionnaireDownload WB Questionnaire

View Our Privacy Statement for details on how we use and protect your data. In addition, this site is protected by hCaptcha and its Privacy Policy and Terms of Service apply.

AMPK Complex (α1, β1, and γ1 subunits; human, recombinant)

Item No. 32557

Technical Information
Synonyms
  • AMPK Subunit α-1
  • MGC33776
  • MGC57364
  • PRKAA1
  • AMPK Subunit β-1
  • HAMPKb
  • MGC17785
  • PRKAB1
  • AMPK Subunit γ-1
  • AMPKG
  • MGC8666
  • PRKAG1
Purity
≥90% estimated by SDS-PAGE
Source
Active recombinant human C-terminal His-tagged AMPK complex (α1, β1, and γ1 subunits) expressed in insect cells
Amino Acids
α1: 1-559; β1: 1-270; γ1: 1-331
MW
~146 kDa complex (α1: 65 kDa; β1: 38 kDa; γ1: 31 kDa)
50 mM Sodium phosphate, pH 7.0, with 300 mM sodium chloride, 150 mM imidazole, 0.25 mM DTT, and 25% glycerol
Shipping & Storage Information
Storage
-80°C
Shipping
Dry ice in continental US; may vary elsewhere
Recommended Products

Certificates of Analysis & Batch Specific Data

Provide batch numbers separated by commas to download or request available product inserts, QC sheets, certificates of analysis, data packs, and GC-MS data.

    Add

    Lipid Resource Center
    Discover Products & Resources for Lipid Research
    • High-purity lipid standards
    • Lipid roles in biology
    • Lipids in health & disease
    • Lipids for pharmaceutical development
    • Protocols, advice, & resources
    EXPLORE NOW
    Product Description

    AMP-activated protein kinase (AMPK) is a heterotrimeric serine/threonine kinase.1 It is composed of an α subunit, two β subunits, and two γ subunits. The α and β subunits each have two isoforms, designated as α1, α2, β1, and β2, which differ at residues affected by post-translational modifications, and the γ subunit has γ1, γ2, and γ3 isoforms. The diversity of isoforms that can comprise the AMPK complex impart differing functions and subcellular localization.1,2 AMPK is ubiquitously expressed in eukaryotes, and AMPK complexes containing an α1 subunit are localized to the cytoplasm.2 AMPK is activated by phosphorylation of the α subunit by kinases and/or by AMP or ADP binding to the γ subunit, which occurs under low energy conditions with high ratios of AMP/ADP to ATP, or an increase in intracellular calcium levels.1,3 In this way, AMPK acts as a regulator of cellular energy homeostasis. It can also be activated under conditions of oxidative stress, where it functions as a redox sensor.2 Its activity is decreased under high energy conditions where ATP, glucose, fatty acids, and amino acids are plentiful.1 AMPK is involved via its downstream signaling pathways in lipid and glucose metabolism, protein synthesis, autophagy, and redox regulation, as well as inhibition of inflammatory processes.1,3 AMPK activation in vivo reduces adiposity in mice, as well as inhibits proliferation of cancer cells in vitro and reduces tumor growth in mouse xenograft models.2 Cayman's AMPK α1, β1, and γ1 Subunits (human, recombinant) protein can be used for enzyme activity assay applications. This protein consists of 1,160 amino acids and has a calculated molecular mass of approximately 146 kDa.

    WARNING This product is not for human or veterinary use.

    References & Product Citations
    Product Description References

    1. Jeon, S.-M. Regulation and function of AMPK in physiology and diseases. Exp. Mol. Med. 48(7), e245 (2016).

    2. Shirwany, N.A., and Zou, M.-H. AMPK: A cellular metabolic and redox sensor. A minireview. Front. Biosci. (Landmark Ed.) 19, 447-474 (2014).

    3. Hardie, D.G., Ross, F.A., and Hawley, S.A. AMPK: A nutrient and energy sensor that maintains energy homeostasis. Nat. Rev. Mol. Cell Biol. 13(4), 251-262 (2012).