**Background of Carboxypeptidase A1+A2+B Antibodies**
Carboxypeptidases are zinc-dependent exopeptidases that hydrolyze peptide bonds at the C-terminus of proteins, playing critical roles in protein maturation, digestion, and regulatory processes. Carboxypeptidase A (CPA) and B (CPB) are major pancreatic enzymes secreted as inactive zymogens (procarboxypeptidases) and activated by trypsin in the small intestine. CPA primarily cleaves hydrophobic or aromatic amino acids, while CPB targets basic residues (e.g., lysine, arginine). Mammalian CPA exists as two isoforms, CPA1 and CPA2. encoded by distinct genes. CPA1 is the predominant digestive form, whereas CPA2 exhibits narrower substrate specificity. CPB also has isoforms, including the pancreatic CPB1 and plasma CPB2 (TAFI).
Antibodies targeting CPA1. CPA2. and CPB are essential tools for studying their expression, localization, and function in physiology and disease. These antibodies help detect enzyme levels in tissues or fluids, aiding in diagnosing pancreatic disorders (e.g., pancreatitis, pancreatic insufficiency) or investigating pathological processes like inflammation and cancer. In research, they are used in immunoassays (e.g., Western blot, immunohistochemistry) to explore enzyme regulation, zymogen activation, or roles in metabolic pathways. Cross-reactivity studies are crucial, as CPA/CPB isoforms share structural homology. Commercial antibodies are often validated for specificity to avoid off-target binding. Understanding CPA/CPB biology via these antibodies contributes to therapeutic development, such as enzyme replacement therapies or inhibitors for conditions like fibrosis or thrombosis.