Render Target: STATIC
Render Timestamp: 2024-12-09T12:17:13.450Z
Commit: 224419269841c11382c4555dbee545259bf6c379
XML generation date: 2024-08-01 15:24:29.941
Product last modified at: 2024-08-20T12:15:16.158Z
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PDP - Template Name: Polyclonal Antibody
PDP - Template ID: *******59c6464

PKM1/2 Antibody #3186

Filter:
  • WB

    Supporting Data

    REACTIVITY H M R
    SENSITIVITY Endogenous
    MW (kDa) 60
    SOURCE Rabbit
    Application Key:
    • WB-Western Blotting 
    Species Cross-Reactivity Key:
    • H-Human 
    • M-Mouse 
    • R-Rat 

    Product Information

    Product Usage Information

    Application Dilution
    Western Blotting 1:1000

    Storage

    Supplied in 10 mM sodium HEPES (pH 7.5), 150 mM NaCl, 100 µg/ml BSA and 50% glycerol. Store at –20°C. Do not aliquot the antibody.

    Protocol

    Specificity / Sensitivity

    PKM1/2 Antibody detects endogenous levels of total PKM (including M1 and M2) protein.

    Species Reactivity:

    Human, Mouse, Rat

    The antigen sequence used to produce this antibody shares 100% sequence homology with the species listed here, but reactivity has not been tested or confirmed to work by CST. Use of this product with these species is not covered under our Product Performance Guarantee.

    Species predicted to react based on 100% sequence homology:

    Chicken, Xenopus

    Source / Purification

    Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to the sequence of human PKM2. Antibodies are purified by protein A and peptide affinity chromatography.

    Background

    Pyruvate kinase is a glycolytic enzyme that catalyses the conversion of phosphoenolpyruvate to pyruvate. In mammals, the M1 isoform (PKM1) is expressed in most adult tissues (1). The M2 isoform (PKM2) is an alternatively spliced variant of M1 that is expressed during embryonic development (1). Research studies found that cancer cells exclusively express PKM2 (1-3). PKM2 is shown to be essential for aerobic glycolysis in tumors, known as the Warburg effect (1). When cancer cells switch from the M2 isoform to the M1 isoform, aerobic glycolysis is reduced and oxidative phosphorylation is increased (1). These cells also show decreased tumorigenicity in mouse xenografts (1). Recent studies showed that PKM2 is not essential for all tumor cells (4). In the tumor model studied, PKM2 was found to be active in the non-proliferative tumor cell population and inactive in the proliferative tumor cell population (4).
    For Research Use Only. Not For Use In Diagnostic Procedures.
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