CLIK-148

CLIK-148 is a highly selective, irreversible and orally active cysteine protease inhibitor, primarily targeting Cathepsin L. CLIK-148 effectively inhibits the Cathepsin L-dependent degradation of HMG-CoA reductase in the endoplasmic reticulum (ER) membrane. CLIK-148 inhibits the processing of proCCK by Cathepsin L, thereby reducing the production of CCK8 (HY-P0093) . CLIK-148 inhibits the degradation of type I collagen by osteoclasts' secreted Cathepsin L, reducing tumor-induced bone metastasis and malignant hypercalcemia. CLIK-148 can be used for the studies of bone metabolism disorders and regulation of neuropeptide processing[1][2][3][4].

Product Specifications

CAS Number

[215098-90-1]

UNSPSC

12352005

Target

Cathepsin; Cholecystokinin Receptor

Related Pathways

GPCR/G Protein; Metabolic Enzyme/Protease; Neuronal Signaling

Applications

Metabolism-protein/nucleotide metabolism

Field of Research

Cancer; Metabolic Disease; Neurological Disease

Smiles

CN(C)C([C@H](CC1=CC=CC=C1)NC([C@@H]2[C@H](O2)C(NCCC3=CC=CC=N3)=O)=O)=O

Molecular Formula

C22H26N4O4

Molecular Weight

410.47

References & Citations

[1]Katunuma N, et al. Structure based development of novel specific inhibitors for cathepsin L and cathepsin S in vitro and in vivo. FEBS Lett. 1999 Sep 10;458 (1) :6-10. |[2]Beinfeld MC, et al. Cathepsin L plays a major role in cholecystokinin production in mouse brain cortex and in pituitary AtT-20 cells: protease gene knockout and inhibitor studies. Peptides. 2009 Oct;30 (10) :1882-91.|[3]Katunuma N, et al. Structure-based design of specific cathepsin inhibitors and their application to protection of bone metastases of cancer cells. Arch Biochem Biophys. 2002 Jan 15;397 (2) :305-11. |[4]Moriyama T, et al. 3-hydroxy-3-methylglutaryl coenzyme A reductase is sterol-dependently cleaved by cathepsin L-type cysteine protease in the isolated endoplasmic reticulum. Arch Biochem Biophys. 2001 Feb 15;386 (2) :205-12.