AdipoGen Life Sciences

Z-Leu-Leu-Leu-B(OH)2 [MG-262]

CHF 80.00
In stock
AG-CP3-0024-C200200 µgCHF 80.00
AG-CP3-0024-M0011 mgCHF 190.00
AG-CP3-0024-M0055 mgCHF 660.00
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Product Details
Synonyms Z-LLL-B(OH)2; Proteasome Inhibitor III
Product Type Chemical
Properties
Formula

C25H42BN3O6

MW 491.4
Sequence

Z-Leu-Leu-Leu-B(OH)2

CAS 179324-22-2
Purity Chemicals ≥95% (HPLC)
Appearance Solid lyophilized powder.
Solubility Soluble in DMSO.
InChi Key MWKOOGAFELWOCD-FKBYEOEOSA-N
Smiles CC(C)C[C@H](NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)OCC1=CC=CC=C1)B(O)O
Shipping and Handling
Shipping BLUE ICE
Short Term Storage +4°C
Long Term Storage -20°C
Handling Advice Avoid freeze/thaw cycles.
Use/Stability Stable for at least 1 year after receipt when stored at -20°C.
Documents
MSDS Download PDF
Product Specification Sheet
Datasheet Download PDF
Description
  • Highly potent and selective cell permeable inhibitor of the proteasome. Inhibits the chymotrypsin-like and caspase-like peptidase activity of the proteasome.
  • Calpain and cathepsin inhibitor.
  • Autophagy activator.
  • Similar structure as MG-132 (AG-CP3-0011) but much higher potency.
Product References
  1. Down-regulation of Flt-1 gene expression by the proteasome inhibitor MG262: J. Mezquita, et al.; J. Cell. Biochem. 89, 1138 (2003)
  2. Importance of the different proteolytic sites of the proteasome and the efficacy of inhibitors varies with the protein substrate: A.F. Kisselev, et al.; J. Biol. Chem. 281, 8582 (2006)
  3. Identification of the proteasome inhibitor MG262 as a potent ATP-dependent inhibitor of the Salmonella enterica serovar Typhimurium Lon protease: H. Frase, et al.; Biochemistry 45, 8264 (2006)
  4. Characterization of the Physiological Turnover of Native and Inactivated Cytochromes P450 3A in Cultured Rat Hepatocytes: A Role for the Cytosolic AAA ATPase p97?: S. Faouzi, et al.; Biochemistry 46, 7793 (2007)
  5. Proteasome activity and autophagosome content in liver are reciprocally regulated by ethanol treatment: P.G. Thomes, et al.; BBRC 417, 262 (2012)
  6. Staurosporine and venetoclax induce the caspase-dependent proteolysis of MEF2D-fusion proteins and apoptosis in MEF2D-fusion (+) ALL cells: N. Tange, et al.; Biomed. Pharmacother. 128,110330 (2020)
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