CPZ
CPZ (carboxypeptidase Z) is a secreted metallocarboxypeptidase of the peptidase M14 family. It specifically removes C-terminal basic amino acids, particularly arginine, from substrates and peptides, and is linked to Wnt signalling and prohormone processing. Browse Assay Genie's current range of CPZ research reagents below, or read on for the biology behind the target.
CPZ cleaves substrates and peptides that carry C-terminal basic amino acids, with a particular preference for those ending in arginine. It is a member of the metallocarboxypeptidase family and displays carboxypeptidase activity towards basic C-terminal residues. The enzyme is most active at neutral pH and is inhibited by active site-directed inhibitors of metallocarboxypeptidases, which is useful to know when designing activity assays.
Beyond its basic catalytic role, CPZ is thought to modulate the Wnt signalling pathway, probably by cleaving a protein that has not yet been identified. It may also contribute to cleavage events during prohormone processing. These annotations are described as probable or possible, so the physiological substrates of CPZ remain an open question for researchers working on the CPZ protein.
The CPZ gene encodes carboxypeptidase Z, which belongs to the peptidase M14 family and the HGNC group of M14 carboxypeptidases. The protein is secreted into the extracellular space and is also found in the extracellular matrix. Alternative splicing in the coding region gives rise to multiple transcript variants that encode different isoforms. Orthologues of the gene are present in mouse and rat, both named Cpz, so the protein can be studied in common rodent models.
CPZ probably modulates the Wnt signalling pathway by cleaving a protein that is not yet defined, making it a candidate for pathway studies.
CPZ may take part in cleavage during prohormone processing, through its selectivity for C-terminal basic residues.
As an M14 metallocarboxypeptidase with preference for C-terminal arginine, CPZ is a model for studying substrate specificity and inhibition.
CPZ is secreted into the extracellular space and extracellular matrix, where it can act on peptides and protein substrates.
CPZ is a secreted metallocarboxypeptidase that specifically cleaves substrates and peptides with C-terminal basic amino acids, especially arginine. It probably modulates Wnt signalling by cleaving an undefined protein, and it may contribute to prohormone processing.
The approved name is carboxypeptidase Z, with the symbol CPZ. No aliases or previous symbols are recorded in HGNC. Alternative splicing in the coding region produces multiple transcript variants that encode different isoforms, so check the datasheet of any product for its validated reactivity.
Yes. Mouse and rat both have an orthologous gene named Cpz. The protein belongs to the peptidase M14 family, a group of metallocarboxypeptidases, so rodent models can be used to study CPZ biology. Check the datasheet of any product for its validated reactivity.
Other M14 carboxypeptidases and Wnt pathway targets with research reagents at Assay Genie.
Gene and protein annotations from HGNC, NCBI Gene and UniProt Q66K79; product specifications from Assay Genie datasheets.