ALLN (110044-82-1) is a cell-permeable, peptide aldehyde inhibitor of calpain I (Ki=190 nM), calpain II (Ki=150 nM), cathepsin L (Ki=0.5 nM) and other neutral cysteine proteases.1 Inhibits cell cycle progression at G1/S and metaphase/anaphase in CHO cells by inhibiting cyclin B degradation.2 Inhibits proteolytic degradation of IκBα and IκBβ in RAW macrophages induced with LPS.3 Blocks AIF-mediated necroptosis.4 Cell permeable.
1) Sasaki et al. (1990), Inhibitory effect of di- and tripeptidyl aldehydes on calpains and cathepsins; J. Enzyme Inhib. 3 195
2) Sherwood et al. (1993) In vivo inhibition of cyclin B degradation and induction of cell-cycle arrest in mammalian cells by the neutral cysteine protease inhibitor N-acetylleucylleucylnorleucinal; Proc. Natl. Acad. Sci USA 90 3353
3) Schow and Joly (1997), N-acetyl-leucinyl-leucinyl-norleucinal inhibits lipopolysaccharide-induced NF-kappaB activation and prevents TNF and IL-6 synthesis in vivo; Cell Immunol. 175 199
4) Shang et al. (2014) Calpain: a molecule to induce AIF-mediated necroptosis in RGC-5 following elevated hydrostatic pressure; BMC Neurosci. 15 63