Cathepsin B (human, recombinant)

Cathepsin B is a lysosomal cysteine protease and member of the papain family of peptidases that has endo- and exopeptidase activity. Cathepsin B is translated as an inactive preproprotein containing a signal peptide, precursor peptide, and catalytic domain. Following removal of the signal peptide, the precursor peptide is cleaved to release a single-chain polypeptide, which can be further cleaved and the pieces connected via disulfide bonds to form a double-chain form of the protein. Cathepsin B is ubiquitously expressed and localizes primarily to the lysosome where the acidic conditions are optimal for its dipeptidyl carboxypeptidase activity. It is involved in lysosomal protein degradation and maintenance of the intracellular proteome but is also found in the cytoplasm, mitochondria, or nucleus, at the plasma membrane, or secreted into the extracellular matrix and is involved in diverse functions, such as cell death, cell division, and degradation of structural proteins. In cancer cells, secreted cathepsin B cleaves and activates extracellular matrix proteins involved in invasion and metastasis. The expression or protein levels of cathepsin B are increased in a variety of cancers, including esophageal cancer, hepatocellular carcinoma, and prostate cancer. Cathepsin B has a complex role in Alzheimer's disease, where it degrades amyloid-beta but can also form pyroglutamic acid amyloid-beta peptide, which has increased neurotoxicity compared with full-length amyloid-beta (1-42). It is also involved in the binding of viruses to host cells via cleavage of the glycoproteins from Middle East respiratory syndrome coronavirus (MERS-CoV) and Ebola virus. Cayman's Cathepsin B (human, recombinant) protein can be used for enzyme activity assays. The proprotein consists of 332 amino acids, has a calculated molecular weight of 37.2 kDa, and a predicted N-terminus of Phe74 after signal and precursor peptide cleavage. By SDS-PAGE, under reducing conditions, the apparent molecular mass of the protein is 36 or 43 kDa for the pro- and mature forms, respectively, due to glycosylation.Synonyms: Amyloid Precursor Protein Secretase, APP Secretase, APPS, Cathepsin B1, CPSB, CTSB, Cysteine Protease. Purity: >97% estimated by SDS-PAGE. Endotoxin Testing: <1.0 EU/µg determined by the LAL endotoxin assay. Source: Active recombinant human C-terminal His-tagged cathepsin B expressed in HEK293 cells. Amino Acids: 74-339. MW: 37.2 kDa. Formulation: (Request formulation change), Lyophilized from sterile PBS, pH 7.4. Specific Activity: Batch specific. UniProt Accession #: P07858.