|Cathepsin A/Lysosomal Carboxypeptidase A in Human Prostate. Cathepsin A/Lysosomal Carboxypeptidase A was detected in immersion fixed paraffin-embedded sections of human prostate using Goat Anti-Human Cathepsin A/Lysosomal Carboxypeptidase A Antigen Affinity-purified Polyclonal Antibody (Catalog # AF1049) at 3 µg/mL overnight at 4 °C. Before incubation with the primary antibody, tissue was subjected to heat-induced epitope retrieval using Antigen Retrieval Reagent-Basic (Catalog # CTS013). Tissue was stained using the Anti-Goat HRP-DAB Cell & Tissue Staining Kit (brown; Catalog # CTS008) and counterstained with hematoxylin (blue). Specific staining was localized to cytoplasm in epithelial cells. View our protocol for Chromogenic IHC Staining of Paraffin-embedded Tissue Sections.|
Cathepsin A/lyososomal carboxypeptidase A is a member of the serine carboxypeptidase family (1). Cathepsin A is a multifunctional enzyme that expresses deaminidase and esterase activities at neutral pH and carboxypeptidase activity at acidic pH. Also known as protective protein, its association with beta -galactosidase ( beta -gal) and neuraminidase is essential for beta -gal stability and neuraminidase activation in the lysosomes. Inherited deficiency of Cathepsin A causes the lysosomal storage disorder galactosialidosis, characterized by a combined secondary deficiency of beta -gal and neuraminidase. Cathepsin A is capable of hydrolyzing a variety of bioactive peptide hormones including tachykinins, indicating that extralysosomal Cathepsin A plays a role in regulation of functions of these molecules (2). Cathepsin A is synthesized as a single-chain precursor and processed into heavy (32 kDa) and light (20 kDa) chains, which are linked by disulfide bonds.
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