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Ac-Leu-Leu-Nle-CHO

BML-P120

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Cysteine protease inhibitor

Cell-permeable, peptide aldehyde inhibitor of calpain I (K_i=190nM), calpain II (K_i=150nM), cathepsin L (K_i=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.

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Product Details

Alternative Name	ALLN, Calpain inhibitor I, Ac-LL-norleucinal
Appearance	White powder.
CAS	110044-82-1
Formula	C₂₀H₃₇N₃O₄
MW	383.5
Purity	≥95% (HPLC)
Sequence	N-Acetyl-Leu-Leu-Nle-CHO
Solubility	Soluble in ethanol (5 mg/ml) or DMSO (10 mg/ml).
Source	Synthetic.

Handling & Storage

Use/Stability	As indicated on product label or CoA when stored as recommended.
Handling	Store dry and protect from light.
Long Term Storage	-20°C
Shipping	Blue Ice

Regulatory Status	RUO – Research Use Only

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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Ac-Leu-Leu-Nle-CHO

BML-P120

Product Details

Handling & Storage

Datasheet, Manuals, SDS & CofA

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