ER1905-48·Anti-Cathepsin B Ant

Cathepsin B is synthesized on the rough endoplasmic reticulum as a preproenzyme of 339 amino acid with a signal peptide of 17 amino acids. Procathepsin B of 43/46 kDa is then transported to the Golgi apparatus and cathepsin B is formed. Mature cathepsin B is composed of a heavy chain of 25-26 kDa and a light chain of 5kDa, which are linked by a dimer of disulfide. Cathepsin B may enhance the activity of other protease, including matrix metalloproteinase, urokinase (serine protease urokinase plasminogen activator), and cathepsin D, and thus it has an essential position for in the proteolysis of extracellular matrix components, intercellular communication disruption, and reduced protease inhibitor expression. It is also involved in autophagy and catabolism, which is advantageous in tumor malignancy and is possibly involved in specific immune resistance.