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M0253 Sigma

L-Mimosine from Koa hoale seeds


Synonym: (S)-α-Amino-β-[1-(3-hydroxy-4-oxopyridine)]propionic acid, Leucenol




1 g in glass bottle

100, 500 mg in glass bottle

25 mg in poly bottle

Biochem/physiol Actions

L-Mimosine is a plant amino acid and potential inhibitor of the cell cycle giving rise to growth arrest in G1-phase. An iron chelator that inhibits DNA replication in mammalian cells. Has been shown to have apoptotic activity in xenotransplanted human pancreatic cancer. L-Mimosine is also used as a hypoxia-mimetic agent to stabilize Hypoxia Inducible Factor 1 (HIF-1). L-Mimosine stabilizes HIF-1 through the inhibition of Prolyl Hydroxylases (PHDs) which target HIF-1 through degradation. The mechanism of inhibition is likely through the chelation of Fe2+ bound to the active site of PHD which is required for enzymatic activity.

Features and Benefits

This compound is also offered as part of Sigma′s Library of Pharmacologically Active Compounds (LOPAC®1280), a biologically annotated collection of high-quality, ready-to-screen compounds. Click here to learn more.

Legal Information

LOPAC is a registered trademark of Sigma-Aldrich Co. LLC

Price and Availability

Flow Cytometry Instruments

All labs need water
Safety & Documentation

Safety Information

GHS07  GHS07
Signal word 
Hazard statements 
Precautionary statements 
Personal Protective Equipment 
NONH for all modes of transport
WGK Germany 


Certificate of Analysis

Certificate of Origin

Protocols & Articles


Oncogenes and Tumor Suppressors Reprogram Metabolism

Proliferating cells require the biosynthesis of structural components for biomass production and for genomic replication. This requires a reprogramming of the metabolic pathways to ensure nutrients s...
Keywords: Aerobic, Antitumor agents, Apoptosis, Biofiles, Cancer, Citric Acid Cycle, Degradations, Environmental, Events, Gene expression, Glycolysis, Growth factors, Metabolic Pathways, Metabolism, Metabolites, Nucleotide Synthesis, PAGE, Pentose phosphate pathway, Phosphorylations, Support

Peer-Reviewed Papers


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