AG-CN2-0442-C100100 µgCHF 350.00
|Purity Chemicals||≥95% (HPLC)|
|Appearance||White to off-white solid.|
|Solubility||Soluble in DMSO or acetonitrile. Undergoes hydrolysis in aqueous buffers.|
|Other Product Data||In vitro lactacystin does not react with the proteasome. It rather undergoes a spontaneous conversion (lactonization) to the active metabolite clasto-lactacystin β-lactone.|
|Shipping and Handling|
|Short Term Storage||+4°C|
|Long Term Storage||-20°C|
|Handling Advice||Protect from light.|
Stable for at least 1 year after receipt when stored at -20°C.
Store solutions at -20°C in the dark.
|Product Specification Sheet|
- Potent and selective irreversible and cell permeable proteasome inhibitor. Inhibits the chymotrypsin-like, trypsin-like and caspase-like peptidase activity of the proteasome.
- The active metabolite of lactacystin (Prod. No. AG-CN2-0104) with higher potency since it does not require hydrolysis in order to become cell permeable.
- Calpain and cathepsin inhibitor.
- Apoptosis inducer.
- Anticancer compound. Induces differentiation and inhibits cell cycle progression in several tumor cell lines.
- Induces neuritogenesis.
- Autophagy inducer.
- Inhibition of proteasome activities and subunit-specific amino-terminal threonine modification by lactacystin: G. Fenteany, et al.; Science 268, 726 (1995)
- Lactacystin and clasto-lactacystin beta-lactone modify multiple proteasome beta-subunits and inhibit intracellular protein degradation and major histocompatibility complex class I antigen presentation: A. Craiu, et al.; J. Biol. Chem. 272, 56 (1997)
- Mechanistic studies on the inactivation of the proteasome by lactacystin in cultured cells: L.R. Dick, et al.; J. Biol. Chem. 272, 182 (1997)
- Lactacystin, proteasome function, and cell fate: G. Fenteany & S.L. Schreiber; J. Biol. Chem. 273, 8545 (1998) (Review)
- Prediction of the mechanism of action of omuralide (clasto-lactacystin beta-lactone) on human cathepsin A based on a structural model of the yeast proteasome beta5/PRE2-subunit/omuralide complex: S. Aikawa, et al.; Biochim. Biophys. Acta 1764, 1372 (2006)
- 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)
- Effect of proteasome inhibitor clasto-lactacystin-beta-lactone on the proteome of the haloarchaeon Haloferax volcanii: P.A. Kirkland, et al.; Microbiology 153, 2271 (2007)