Ac-Leu-Leu-Nle-CHO - Enzo Life Sciences

BML-P120

Revised 05-Mar-10

Ac-Leu-Leu-Nle-CHO
SYNONYMS	ALLN Calpain inhibitor I Ac-LL-norleucinal
PRODUCT LINE	Signal Transduction
PRODUCT CATEGORY	Calpains / Related Products

Ordering Information

Product Numbers:	Format:	Size:	Unit Price:	Quantity:	Add To Cart
BML-P120-0005		5 mg	72.00 USD
BML-P120-0025		25 mg	286.00 USD
Replaces Prod. #: ALX-260-037

Product Specification

SEQUENCE:	N-Acetyl-Leu-Leu-Nle-CHO
FORMULA:	C₂₀H₃₇N₃O₄
MW:	383.54
CAS NUMBER:	110044-82-1
PURITY:	>95% (HPLC)
APPEARANCE:	White powder.
SOLUBILITY:	Soluble in DMSO (25 mg/ml), 100% ethanol and methanol.
SHIPPING:	SHIPPED ON BLUE ICE
LONG TERM STORAGE:	-20°C

Product Description

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.

Product Specific Literature References

Inhibition of the chymotrypsin-like activity of the pituitary multicatalytic proteinase complex.: A. Vinitsky et al.; Biochemistry 31, 9421 (1992) 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. Nat.l Acad. Sci. USA 90, 3353 (1993) Abstract
SREBP-1, a membrane-bound transcription factor released by sterol-regulated proteolysis.: X. Wang et al.; Cell 77, 53 (1994) 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
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
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
Fas aggregation does not correlate with Fas-mediated apoptosis.: Y. Lee & E. Shacter; J. Immunol. 167, 82 (2001) Abstract