Render Target: STATIC
Render Timestamp: 2024-11-21T13:51:04.947Z
Commit: 5c4accf06eb7154018ba3f54329c7590f97f534a
XML generation date: 2024-11-14 19:01:13.122
Product last modified at: 2024-10-18T07:01:10.167Z
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PDP - Template Name: Matched Antibody Pair
PDP - Template ID: *******446e1e7

Total AMPKα Matched Antibody Pair #74094

Filter:
  • ELISA

    Supporting Data

    REACTIVITY H M R Hm Mk
    Application Key:
    • ELISA-ELISA 
    Species Cross-Reactivity Key:
    • H-Human 
    • M-Mouse 
    • R-Rat 
    • Hm-Hamster 
    • Mk-Monkey 

    Product Information

    Product Usage Information

    Matched Antibody Pairs include capture and detection antibodies to non-overlapping epitopes. Optimal dilutions/concentrations should be determined by the end user.

    Formulation

    Supplied in 1X PBS (10 mM Na2HPO4, 3 mM KCl, 2 mM KH2PO4, and 140 mM NaCl (pH 7.8)). BSA and Azide Free.

    Storage

    Store at -20ºC. This product will freeze at -20ºC so it is recommended to aliquot into single-use vials to avoid multiple freeze/thaw cycles. A slight precipitate may be present and can be dissolved by gently vortexing. This will not interfere with antibody performance.

    Product Description

    The Total AMPKα Matched Antibody Pair is ideal for use with immunoassay technologies and high-throughput ELISA platforms requiring antibody pairs with specialized or custom antibody labeling. Labels include fluorophores, lanthanides, biotin, and beads. Platforms requiring conjugated Matched Antibody Pairs include MSD, Quanterix Simoa, Alpha Technology (AlphaScreen, AlphaLISA, LANCE, HTRF), and Luminex.

    Learn how Matched Antibody Pairs move your projects forward, faster at cst-science.com/matched-antibody-pairs.

    Background

    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 α subunit and regulatory β and γ subunits, each of which is encoded by two or three distinct genes (α1, 2; β1, 2; γ1, 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 AMPKα at Thr172 in the activation loop, and this phosphorylation is required for AMPK activation (3-5). AMPKα is also phosphorylated at Thr258 and Ser485 (for α1; Ser491 for α2). The upstream kinase and the biological significance of these phosphorylation events have yet to be elucidated (6). The β1 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 β1 subunit seems to be required for AMPK activation, while phosphorylation at Ser24/25 and Ser182 affects AMPK localization (7). Several mutations in AMPKγ 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).
    For Research Use Only. Not For Use In Diagnostic Procedures.
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