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clasto-Lactacystin β-Lactone

Proteasome inhibitor
BML-PI108-0100 100 µg 315.00 USD
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Replaces Prod. #: ALX-270-280

Highly specific, cell permeable, and irreversible 20S proteasome inhibitor. Inhibits ubiquitin proteasome pathway in cell culture (IC50=1µM). It has been suggested that the natural product lactacystin acts as a precursor for clasto-lactacystin β-lactone and that the latter is the sole species that interacts with the proteasome. Inhibits cathepsin A. Leads to a reduction of adipogenesis. Induces neurite growth and inhibits cell cycle progression. 

Product Details

Alternative Name:Omuralide
Purity:≥95% (HPLC)
Appearance:White solid.
Solubility:Soluble in DMSO (25mg/ml) or acetonitrile.
Shipping:Ambient Temperature
Long Term Storage:-20°C
Use/Stability:Stable for at least 2 years after receipt when stored, as supplied, at -20°C. Stock solutions are stable for up to 1 month at -80°C.
Handling:Protect from light.
Regulatory Status:RUO - Research Use Only
BML-PI108 structure
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BML-PI108 structure

Product Literature References

Cytosolic PTEN-INDUCED PUTATIVE KINASE 1 is Stabilized By NF-κB Pathway and Promotes Non-Selective Mitophagy: G.G. Lim, et al.; J. Biol. Chem. 290, 16882 (2015), Abstract; Full Text
Protein carbonylation and aggregation precede neuronal apoptosis induced by partial glutathione depletion: A. Dasgupta, et al.; ASN Neuro 4, e00084 (2012), Abstract; Full Text
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), Abstract;
Inhibition of human preadipocyte proteasomal activity by HIV protease inhibitors or specific inhibitor lactacystin leads to a defect in adipogenesis, which involves matrix metalloproteinase-9: S. De Barros, et al.; J. Pharmacol. Exp. Ther. 320, 291 (2007), Abstract;
Lactacystin inhibits cathepsin A activity in melanoma cell lines: L. Kozlowski, et al.; Tumour Biol. 22, 211 (2001), Abstract;
Lactacystin, a proteasome inhibitor: discovery and its application in cell biology: H. Tomoda & S. Omura; Yakugaku Zasshi 120, 935 (2000), Review, Abstract;
Separation of cathepsin A-like enzyme and the proteasome: evidence that lactacystin/beta-lactone is not a specific inhibitor of the proteasome: H. Ostrowska, et al.; Int. J. Biochem. Cell Biol. 32, 747 (2000), Abstract;
Total synthesis and biological activity of lactacystin, omuralide and analogs: E.J. Corey & W.D. Li; Chem. Pharm. Bull. 47, 1 (1999), Abstract;
Lactacystin, proteasome function, and cell fate: G. Fenteany & S.L. Schreiber; J. Biol. Chem. 273, 8545 (1998), Abstract; Full Text
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, 13437 (1997), Abstract; Full Text
Mechanistic studies on the inactivation of the proteasome by lactacystin in cultured cells: L.R. Dick, et al.; J. Biol. Chem. 272, 182 (1997), Abstract; Full Text
Mechanistic studies on the inactivation of the proteasome by lactacystin: a central role for clasto-lactacystin beta-lactone: L.R. Dick, et al.; J. Biol. Chem. 271, 7273 (1996), Abstract;
Inhibition of proteasome activities and subunit-specific amino-terminal threonine modification by lactacystin: G. Fenteany, et al.; Science 268, 726 (1995), Abstract;
A beta-lactone related to lactacystin induces neurite outgrowth in a neuroblastoma cell line and inhibits cell cycle progression in an osteosarcoma cell line: G. Fenteany, et al.; Proc. Natl. Acad. Sci. USA 91, 3358 (1994), Abstract;

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