AdipoGen Life Sciences

Z-Leu-Leu-Leu-CHO [MG-132]

CHF 25.00
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AG-CP3-0011-M0011 mgCHF 25.00
AG-CP3-0011-M0055 mgCHF 65.00
AG-CP3-0011-M02525 mgCHF 195.00
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Product Details
Synonyms Z-LLL-CHO; Carbobenzoxy-L-leucyl-L-leucyl-L-leucinal; MG132
Product Type Chemical


MW 475.6


CAS 133407-82-6
RTECS OH2824610
Purity Chemicals ≥97% (HPLC)
Appearance White solid.
Solubility Soluble in DMSO or ethanol.
Smiles [H]C(=O)[C@]([H])(CC(C)C)NC(=O)[C@]([H])(CC(C)C)NC(=O)[C@]([H])(CC(C)C)NC(=O)OCC1=CC=CC=C1
Shipping and Handling
Shipping AMBIENT
Short Term Storage +4°C
Long Term Storage -20°C
Handling Advice Keep cool and dry.
Use/Stability Stable for at least 2 years after receipt when stored at -20°C.
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Product Specification Sheet
Datasheet Download PDF
  • Potent, cell permeable and selective, reversible proteasome inhibitor [2, 7].
  • Blocks degradation of short-lived proteins and induces a heat shock response [2, 6, 7].
  • NF-κB activation inhibitor through IκB degradation [3, 8].
  • Cell permeable, reversible peptide aldehyde inhibitor. Calpain and cathepsin inhibitor [4, 11].
  • Has anticancer properties by inducing cell cycle arrest and activating apoptosis in various cancer cell lines [8, 9, 12,13,15].
  • Has adjuvant/chemosensitizer potential [8].
  • Neurite outgrowth stimulator in PC12 cells [1].
  • Prevents β-secretase cleavage [5, 10].
  • Autophagy activator [12, 14].
Product References
  1. Isolation and characterization of possible target proteins responsible for neurite outgrowth induced by a tripeptide aldehyde in PC12H cells: Y. Saito, et al.; BBRC 184, 419 (1992)
  2. Inhibitors of the proteasome block the degradation of most cell proteins and the generation of peptides presented on MHC class I molecules: K.L. Rock, et al.; Cell 78, 761 (1994)
  3. The ubiquitin-proteasome pathway is required for processing the NF-kappa B1 precursor protein and the activation of NF-kappa B: V.J. Palombella, et al.; Cell 78, 773 (1994)
  4. Differential inhibition of calpain and proteasome activities by peptidyl aldehydes of di-leucine and tri-leucine: S. Tsubuki, et al.; J. Biochem. 119, 572 (1996)
  5. The carboxyl termini of beta-amyloid peptides 1-40 and 1-42 are generated by distinct gamma-secretase activities: H. Klafki, et al.; J. Biol. Chem. 271, 28655 (1996)
  6. Proteasome inhibition leads to a heat-shock response, induction of endoplasmic reticulum chaperones, and thermotolerance: K.T. Bush, et al.; J. Biol. Chem. 272, 9086 (1997)
  7. Proteasome inhibitors: valuable new tools for cell biologists: D.H. Lee & A.L. Goldberg; Trends Cell Biol. 8, 397 (1998)
  8. Inhibition of NF-kappaB sensitizes human pancreatic carcinoma cells to apoptosis induced by etoposide (VP16) or doxorubicin: A. Arlt, et al.; Oncogene 20, 859 (2001)
  9. Potential of the proteasomal inhibitor MG-132 as an anticancer agent, alone and in combination: D. Banerjee & A. Liefshitz; Anticancer Res. 21, 3941 (2001)
  10. The protease inhibitor, MG132, blocks maturation of the amyloid precursor protein Swedish mutant preventing cleavage by beta-Secretase: M.L. Steinhilb, et al.; J. Biol. Chem. 276, 4476 (2001)
  11. The proteasome inhibitor MG132 protects against acute pancreatitis: T. Letoha, et al.; Free Radic. Biol. Med. 39, 1142 (2005)
  12. Induction of autophagy by proteasome inhibitor is associated with proliferative arrest in colon cancer cells: W.K. Wu, et al.; BBRC 374, 258 (2008)
  13. Synthesis, radiosynthesis, and biological evaluation of new proteasome inhibitors in a tumor targeting approach: M. Vivier, et al.; J. Med. Chem. 51, 1043 (2008)
  14. Mechanisms of cross-talk between the ubiquitin-proteasome and autophagy-lysosome systems: V.I. Korolchuk, et al.; FEBS Lett. 584, 1393 (2010)
  15. MG132, a proteasome inhibitor, induces apoptosis in tumor cells: N. Guo & Z. Peng; Asia Pac. J. Clin. Oncol. 9, 6 (2013)
  16. AQP2 Abundance is Regulated by the E3-Ligase CHIP Via HSP70: M. Centrone, et al.; Cell Physiol. Biochem. 44, 515 (2017)
  17. Sal-like 4 protein levels in breast cancer cells are post-translationally down-regulated by tripartite motif containing 21: J. Itou, et al.; J. Biol. Chem. 293, 6556 (2018)
  18. Characterization of huntingtin interactomes and their dynamic responses in living cells by proximity proteomics: H. Xu, et al.; J. Neurochem. ahead of print (2022)
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