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Cysteine protease inhibitor
BML-P120-0005 5 mg 116.00 USD
BML-P120-0025 25 mg 458.00 USD
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Replaces Prod. #: ALX-260-037

Cell-permeable, peptide aldehyde inhibitor of calpain I (Ki=190nM), calpain II (Ki=150nM), cathepsin L (Ki=0.5nM) and other neutral cysteine proteases. Inhibits cell cycle progression at G1/S and metaphase/anaphase in CHO cells by inhibiting cyclin B degradation. Also stimulates HMG-CoA synthase transcription by inhibiting degradation of active SREBP-1 (sterol regulatory element-binding protein 1). Protects against neuronal damage caused by hypoxia and ischemia. Inhibits apoptosis in thymocytes and metamyelocytes. Also prevents nitric oxide production by activated macrophages by interfering with the transcription of inducible nitric oxide synthase (iNOS; NOS II). Inhibits proteolytic degradation of IκBα and IκBß in RAW macrophages induced with LPS. It also prolong association of MHC class I molecules with the transporters associated with antigen processing.

Product Details

Alternative Name:ALLN, Calpain inhibitor I, Ac-LL-norleucinal
Purity:≥95% (HPLC)
Appearance:White powder.
Solubility:Soluble in ethanol (5 mg/ml) or DMSO (10 mg/ml).
Shipping:Blue Ice Not Frozen
Long Term Storage:-20°C
Handling:Store dry and protect from light.
Regulatory Status:RUO - Research Use Only

Product Literature References

Fas aggregation does not correlate with Fas-mediated apoptosis.: Y. Lee & E. Shacter; J. Immunol. 167, 82 (2001), Abstract;
N-acetyl-leucinyl-leucinyl-norleucinal inhibits lipopolysaccharide-induced NF-kappaB activation and prevents TNF and IL-6 synthesis in vivo.: S.R. Schow & A. Joly; Cell. Immunol. 175, 199 (1997), Abstract;
Inhibitors of the proteasome pathway interfere with induction of nitric oxide synthase in macrophages by blocking activation of transcription factor NF-kappa B.: J.M. Griscavage et al.; Proc. Natl. Acad. Sci. USA 93, 3308 (1996), Abstract;
The protease inhibitor, N-acetyl-L-leucyl-L-leucyl-leucyl-L-norleucinal, decreases the pool of major histocompatibility complex class I-binding peptides and inhibits peptide trimming in the endoplasmic reticulum.: E.A. Hughes et al.; J. Exp. Med. 183, 1569 (1996), Abstract;
Serine and cysteine proteinase inhibitors prevent nitric oxide production by activated macrophages by interfering with transcription of the inducible NO synthase gene.: J.M. Griscavage et al.; Biochem. Biophys. Res. Commun. 215, 721 (1995), Abstract;
SREBP-1, a membrane-bound transcription factor released by sterol-regulated proteolysis.: X. Wang et al.; Cell 77, 53 (1994), Abstract;
Evidence for the presence of five distinct proteolytic components in the pituitary multicatalytic proteinase complex. Properties of two components cleaving bonds on the carboxyl side of branched chain and small neutral amino acids.: M. Orlowski et al.; Biochemistry 32, 1563 (1993), Abstract;
In vivo inhibition of cyclin B degradation and induction of cell-cycle arrest in mammalian cells by the neutral cysteine protease inhibitor N-acetylleucylleucylnorleucinal.: S.W. Sherwood et al.; Proc. Natl. Acad. Sci. USA 90, 3353 (1993), Abstract;
Inhibition of the chymotrypsin-like activity of the pituitary multicatalytic proteinase complex.: A. Vinitsky et al.; Biochemistry 31, 9421 (1992), Abstract;

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