Cathepsin-Z, also known as Cathepsin-X or Cathepsin-P, is a unique lysosomal cysteine protease. It is primarily expressed by antigen-presenting cells and has been associated with various physiological and pathological processes, including neuroinflammation . The antibody “Mouse Anti Human Cathepsin-Z” is specifically designed to detect human Cathepsin-Z in various applications, such as Western blotting, immunohistochemistry, and immunoprecipitation .
Cathepsin-Z is a member of the papain-like cysteine protease family. It is synthesized as an inactive proenzyme and activated in the acidic environment of lysosomes. The enzyme plays a crucial role in protein degradation and processing within the lysosome. Unlike other cathepsins, Cathepsin-Z has a unique C-terminal extension that may contribute to its specific functions .
Cathepsin-Z is predominantly expressed in antigen-presenting cells, such as macrophages and dendritic cells. It is also found in various tissues, including the liver, spleen, and lungs. The enzyme is localized in the lysosomes, where it participates in the degradation of intracellular and extracellular proteins .
Cathepsin-Z has been implicated in several diseases, particularly those involving inflammation and immune responses. For instance, its expression is upregulated in neuroinflammatory disorders, suggesting a role in mediating neuroinflammation . Additionally, Cathepsin-Z has been associated with cancer progression, where it may contribute to tumor invasion and metastasis.
The Mouse Anti Human Cathepsin-Z antibody is widely used in research to study the expression and function of Cathepsin-Z. Some of the key applications include: