CPE Human

CPE is a single-chain peptidase with an optimal pH range between 5.0 and 6.0 . The enzyme is initially synthesized as an inactive precursor, which is then processed into its active form primarily within secretory vesicles . The active form of CPE cleaves C-terminal amino acid residues, facilitating the maturation of various peptide hormones and neurotransmitters, including insulin and enkephalin .

CPE is essential for the proper functioning of the endocrine and nervous systems. It is involved in the processing of numerous peptide hormones and neurotransmitters, which are critical for maintaining physiological homeostasis . For instance, CPE knockout mice exhibit obesity due to impaired glucose clearance and insulin resistance, highlighting its role in metabolic regulation .

Recombinant human CPE is produced using advanced biotechnological methods. It is typically expressed in host cells such as HEK293 or mouse myeloma cell lines . The recombinant protein is purified to high levels of purity (>90% or >95%) and is often tagged with a polyhistidine tag for ease of purification .

The activity of recombinant human CPE is measured by its ability to cleave a peptide substrate, benzoyl-AR-OH, resulting in the formation of a fluorescent molecule . This specific activity is a key indicator of the enzyme’s functionality and is typically greater than 12,000 pmol/min/µg .

Recombinant human CPE is widely used in research to study the processing and maturation of peptide hormones and neurotransmitters. It is also utilized in various biochemical assays to investigate enzyme kinetics and substrate specificity .

Recombinant human CPE is supplied as a lyophilized powder or a filtered solution and should be stored at -20°C to -70°C to maintain its stability . It is important to avoid repeated freeze-thaw cycles to preserve the enzyme’s activity.