ACP5. also known as tartrate-resistant acid phosphatase (TRAP), is a metalloenzyme encoded by the ACP5 gene. It belongs to the acid phosphatase family and is characterized by its resistance to inhibition by tartrate. Structurally, it contains two iron-binding sites and a manganese-binding site critical for its enzymatic activity. ACP5 is primarily expressed in osteoclasts, immune cells (macrophages, dendritic cells), and certain cancer cells. In bone biology, ACP5 plays a key role in osteoclast-mediated bone resorption, facilitating the degradation of bone matrix during remodeling. Dysregulation of ACP5 is linked to pathological conditions, including osteoporosis, rheumatoid arthritis, and bone metastases in cancers.
ACP5 antibodies are immunological tools used to detect and quantify this enzyme in research and diagnostics. They enable the study of osteoclast differentiation, bone metabolism disorders, and tumor microenvironment interactions. In cancer research, ACP5 antibodies help investigate its role in promoting tumor cell invasion and metastasis. Clinically, elevated serum ACP5 levels, detected via antibody-based assays, serve as a biomarker for bone turnover diseases. Recent studies also explore ACP5's involvement in immune regulation, particularly in dendritic cell function and inflammatory responses. These antibodies are pivotal in elucidating ACP5's dual roles in physiological remodeling and disease progression, with potential therapeutic implications.