Cathepsin S (CTSS) is a lysosomal cysteine endopeptidase of the papain family or C1 family. It is produced as an inactive preproenzyme which is then converted into the active form in lysosomes and late endosomes.
Cathepsin S (CTSS) is a lysosomal cysteine endopeptidase of the papain family or C1 family. It is produced as an inactive preproenzyme which is then converted into the active form in lysosomes and late endosomes.
Cathepsin S (CTSS) is a lysosomal cysteine endopeptidase of the papain family or C1 family. It is produced as an inactive preproenzyme which is then converted into the active form in lysosomes and late endosomes.
Cathepsin B (CTSB) also known as APP secretase (APPS) and CPSB, is an enzymatic protein belonging to the peptidase C1 family. Cathepsin B / CTSB is synthesized as a preproenzyme. Following removal of the signal peptide, the inactive proenzyme undergo
Cathepsin L (CTSL1) also known as major excreted protein (MEP), is a member of the peptidase C1 family, is a dimer composed of disulfide-linked heavy and light chains linked by disulfide bonds. CTSL1 is a lysosomal cysteine proteinase that plays a ma
CD147, also known as Basigin (BSG), or extracellular matrix metalloproteinase inducer (EMMPRIN). The human basigin protein contains 269 amino acids that form two heavily glycosylated C2 type immunoglobulin-like domains at the N-terminal extracellular
Cell Adhesion Molecules (CAMs) are proteins located on the cell surface involved with the binding with other cells or with the extracellular matrix (ECM) in the process called cell adhesion. Cell adhesion molecule 1 is a single-pass type I membrane p
Members of the Dickkopf-related protein family (DKK-1, -2, -3, and -4) are secreted proteins with two cysteine-rich domains separated by a linker region. And DKK3 has been proposed as tumor suppressor gene and a marker for tumor blood vessels. DKK3 i