Carboxypeptidase E
Carboxypeptidase E (CPE), also known as prohormone-processing carboxypeptidase, is a metallocarboxypeptidase central to the maturation of peptide hormones and neuropeptides in the regulated secretory pathway. The enzyme removes C-terminal lysine and arginine residues exposed after endoprotease cleavage of prohormone precursors, acting on substrates such as proinsulin, proopiomelanocortin, and numerous neuropeptides. Beyond catalysis, CPE functions as a sorting receptor that directs cargo proteins into regulated secretory granules. The famous fat mutation, which inactivates CPE in mice, causes obesity and hyperproinsulinemia, demonstrating the enzyme's physiological importance, and reduced CPE activity has been linked to defective glucose homeostasis and altered neuroendocrine function in animal models.
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Carboxypeptidase E Recombinant Proteins (2)
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Recombinant Protein Expression Service
- Codon Optimization
- Gene Synthesis
- Construction of Expression Vector
- Strain Screening
- Protein Expression
- Purification & QC
- Protein Delivery
- Formel: Human
- Molecular Weight: Sf9 insect cells
The EpCAM/TROP1 protein serves as an important homogeneous interacting molecule that promotes direct contact between intestinal epithelial cells (IEC) and intraepithelial lymphocytes (IEL) in the mucosal epithelium. This feature helps establish an immune barrier against mucosal infections. EpCAM/TROP1 Protein, Human (His-SUMO) is the recombinant human-derived EpCAM/TROP1 protein, expressed by E. coli , with N-6*His, N-SUMO labeled tag.
