CPM
CPM (carboxypeptidase M) is a membrane-bound arginine/lysine carboxypeptidase that removes C-terminal basic residues from peptides and proteins. It belongs to the peptidase M14 family and acts at the cell surface. Browse Assay Genie's current range of CPM research reagents below, or read on for the biology behind the target.
CPM is a carboxypeptidase that specifically removes C-terminal basic residues, arginine or lysine, from peptides and proteins. It is believed to play important roles in controlling the activity of peptide hormones and growth factors at the cell surface, and in the membrane-localised degradation of extracellular proteins. Because it acts on substrates at the plasma membrane, CPM is a useful focus for studies of how cell-surface proteolysis shapes peptide signalling.
The CPM gene encodes a membrane-bound arginine/lysine carboxypeptidase classified by HGNC in the M14 carboxypeptidases gene group, and by UniProt in the peptidase M14 family. The protein carries hydrophobic regions at its amino and carboxy termini and has six potential asparagine-linked glycosylation sites. The active site residues of carboxypeptidases A and B are conserved in this protein. Three alternatively spliced transcript variants have been described, and all encode the same protein. The mouse ortholog is Cpm.
According to the NCBI Gene summary, CPM expression is associated with monocyte to macrophage differentiation, which makes it a point of interest in myeloid cell biology. Researchers studying the CPM protein or CPM gene often do so in the context of cell-surface peptide processing and the regulation of growth factor activity.
CPM is believed to control peptide hormone activity at the cell surface by removing C-terminal arginine or lysine residues.
Cell-surface trimming of C-terminal basic residues is proposed to modulate growth factor activity, making CPM relevant to signalling studies.
CPM expression is associated with monocyte to macrophage differentiation, so it is studied as a marker in myeloid cell biology.
CPM contributes to membrane-localised degradation of extracellular proteins, an area relevant to cell-surface proteolysis research.
CPM specifically removes C-terminal basic residues, arginine or lysine, from peptides and proteins. It is believed to control the activity of peptide hormones and growth factors at the cell surface and to take part in membrane-localised degradation of extracellular proteins.
CPM stands for carboxypeptidase M, and no alternative gene symbols are recorded by HGNC. Three alternatively spliced transcript variants have been described for the gene, but all of them encode the same protein, so no distinct protein isoforms are reported.
CPM expression is associated with monocyte to macrophage differentiation. The gene has a mouse ortholog, Cpm, and the active site residues of carboxypeptidases A and B are conserved in the protein. Check the datasheet of any product for its validated reactivity.
Other M14 carboxypeptidases and related peptidases with products at Assay Genie.
Gene and protein annotations from HGNC, NCBI Gene and UniProt P14384; product specifications from Assay Genie datasheets.