Zeta’s CPA1 rabbit recombinant antibody identifies a 419 amino acid-secreted monomeric protein highly expressed in pancreatic tissue. Human pancreatic procarboxypeptidase A (CPA) has three different active forms, two of which are designated carboxypeptidase A1 (CPA1) and carboxypeptidase A2 (CPA2). Functioning as a pancreatic exopeptidase, CPA1 uses zinc as a cofactor to catalyze the release of C-terminal amino acids from a variety of proteins, thereby playing a key role in protein digestion and degradation. Via its catalytic activity, CPA1 is also thought to be involved in zymogen (proenzyme) inhibition, probably functioning to block enzyme activation pathways.
Carboxypeptidase A1 (CPA1) immunohistochemistry provides a highly sensitive and specific method to identify Acinar Cell Carcinoma (ACC) of the pancreas. Abnormal levels of CPA1 are associated with pancreatic cancer, suggesting a possible role in either tumor progression or tumor suppression events.
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