Recombinant Human CPA3 protein

Carboxypeptidase A3 (CPA3), also known as mast cell carboxypeptidase A, is a zinc-dependent metalloprotease primarily expressed in mast cells. It belongs to the carboxypeptidase gene family, which plays roles in processing bioactive peptides by cleaving C-terminal amino acids. CPA3 is stored in mast cell secretory granules alongside other mediators like histamine and tryptase, and it is released during mast cell degranulation in response to allergic or inflammatory stimuli.

Originally identified as a mast cell-specific enzyme, CPA3 is encoded by the CPA3 gene in humans. Its precursor form requires proteolytic activation to become enzymatically active. Unlike other carboxypeptidases, CPA3 exhibits unique substrate specificity, preferentially cleaving aromatic or branched-chain aliphatic residues. This enzymatic activity contributes to the regulation of peptide hormones and inflammatory mediators, potentially influencing processes such as tissue remodeling, host defense, and anaphylaxis.

Recombinant CPA3 proteins are produced using biotechnological platforms (e.g., bacterial, insect, or mammalian expression systems) for research and therapeutic applications. These engineered proteins retain catalytic activity while enabling controlled production for functional studies. Current research focuses on CPA3's involvement in allergic diseases (asthma, anaphylaxis), mastocytosis, and cancer progression, where abnormal CPA3 levels correlate with disease severity. Its role in processing matrix proteins and bioactive peptides also suggests potential applications in biomarker development and targeted therapies. However, the complete physiological spectrum of CPA3 remains under investigation, particularly regarding its dual roles in protective immunity and pathological inflammation.