Analysis of Cathepsin B (total) (Human) by ELISA (CAT#: STEM-MB-0716-LGZ)

Introduction

Cathepsin, a papain-like cysteine or aspartic acid protease, is ubiquitously present in lysosome organelles, activated in an acidic environment, and cleaves various target proteins. According to their structure and substrate specificity, there are about ten kinds of members in the cathepsin family, including A, B, C, D, E, G, H, K, L, S and so on. Cathepsins play an important role in the turnover of intracellular and extracellular proteins through endocytosis, as well as an alternative mechanism for initiating and transmitting signals of apoptosis, as well as pathophysiological changes of tumor and inflammatory tissue damage.
Among them, hispsin B (EC 3.4.22.1), also known as CTSB, as the signature enzyme protein of lysosome, can transform β-amyloid precursor protein into β-amyloid protein spots, which play an important role in antigen processing, tumor metastasis, bone reabsorption, intracellular or secretory regulation of protein turnover, egg cell maturation, cell apoptosis, etc. Intercellular contact and extracellular matrix components affect the conversion of 43kd cathepsinogen L into mature proteins. Cathepsin B degrades collagen, connective tissue protein and beta-amyloid precursor protein. It interacts with cysteine protease inhibitors A and B, S100A10 and other proteins. Abnormal cathepsin B can lead to diseases such as Alzheimer's syndrome and esophageal tumors.