Cathepsin D is a lysosomal aspartyl protease encoded by the CTSD gene in humans . It is ubiquitously distributed in lysosomes and plays a crucial role in the degradation of proteins within the cell . Cathepsin D is involved in various physiological processes, including protein catabolism, hormone processing, and the activation of precursor proteins . It is also implicated in several pathological conditions, such as Alzheimer’s disease, cancer, and neurodegenerative disorders .
Cathepsin D is synthesized as an inactive precursor, known as preprocathepsin D, which undergoes proteolytic cleavage to form the active enzyme . The active enzyme consists of a protein dimer of disulfide-linked heavy and light chains . Cathepsin D functions optimally in the acidic environment of lysosomes and is involved in the degradation of various substrates, including amyloid-β protein (Aβ) and tau protein .
Cathepsin D has been extensively studied in the context of Alzheimer’s disease (AD). It degrades both the amyloid-β protein (Aβ) and the microtubule-associated protein tau, which accumulate pathognomonically in AD . Studies have shown that genetic deletion of Cathepsin D in mice leads to increased cerebral Aβ and tau pathology, suggesting a critical role for Cathepsin D in the proteostasis of these proteins . The enzyme’s activity is also influenced by Aβ42, which acts as a competitive inhibitor, further linking Cathepsin D to AD pathology .
Mouse anti-human Cathepsin D antibodies are commonly used in research to study the expression and function of Cathepsin D in various biological contexts. These antibodies are typically generated by immunizing mice with human Cathepsin D protein, followed by the isolation and purification of specific antibodies from the mouse serum. The antibodies can be used in various applications, including Western blotting, immunohistochemistry, and enzyme-linked immunosorbent assays (ELISA), to detect and quantify Cathepsin D in biological samples.