The CAPN7 antibody targets calpain-7 (CAPN7), a member of the calcium-dependent cysteine protease family, though its proteolytic activity remains less characterized compared to classical calpains. CAPN7. also known as paladin, is distinguished by its unique domain structure, featuring three N-terminal C2 domains and a C-terminal protease-like domain lacking critical catalytic residues, suggesting non-enzymatic roles. It is implicated in membrane trafficking, endocytosis, and lysosomal function, particularly through interactions with the endosomal sorting complex required for transport (ESCRT) machinery. Studies link CAPN7 to neural development, autophagy, and cancer progression, with altered expression observed in gliomas and breast cancers. The CAPN7 antibody is a critical tool for detecting the protein's expression, localization, and interaction partners in cellular and tissue contexts. Validated applications include Western blotting, immunofluorescence, and immunoprecipitation, aiding research into its regulatory mechanisms in vesicle dynamics and disease pathways. However, specificity validation is essential due to potential cross-reactivity with structurally similar proteins. Ongoing research aims to clarify CAPN7's precise biological functions and therapeutic relevance.