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The protein encoded by CPM is a membrane-bound arginine/lysine carboxypeptidase. Additionally we are shipping Carboxypeptidase M Antibodies (64) and Carboxypeptidase M Proteins (14) and many more products for this protein.
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spatial proximity between angiotensin-converting enzyme (show ACE ELISA Kits) and the endogenous CPM enables an angiotensin-converting enzyme (show ACE ELISA Kits) evoked release of CPM
of the 33 transcripts from the CPM locus, four were evaluated with one showing expression patterns that differed considerably from the other ones and from the mouse CPM gene, suggesting that there may be more than one transcriptional unit in this locus
CPM binding to extracellular loop 2 of the B1R (show BDKRB1 ELISA Kits) results in positive allosteric modulation of B1R (show BDKRB1 ELISA Kits) signaling, and disruption of this interaction could provide a novel therapeutic approach to reduce pathological B1R (show BDKRB1 ELISA Kits) signaling.
Carboxypeptidase M expression is lost in human renal cell carcinoma tumor cells, whereas it is abundant in tumor-associated foam cells and neovasculature.
CPM and B1Rs on cell membranes form a critical complex that potentiates B1R (show BDKRB1 ELISA Kits) signaling.
CPM amplification could be used as an alternative diagnostic tool for the diagnosis of well-differentiated liposarcoma/atypical lipomatous tumors.
Results report the crystallization of human carboxypeptidase M and its 3.0 angstrom crystal structure.
Carboxypeptidase M and kinin B1 (show BDKRB1 ELISA Kits) receptors interact to facilitate efficient b1 signaling from B2 agonists
Cleavage of the C-terminal lysine residue of SDF-1alpha by CPM leads to attenuated chemotactic responses.
CPM is membrane-bound via attachment of glycosylphosphatidylinositol at Ser406. Glu264 is a critical catalytic residue, whereas Glu260 affects stability and substrate kinetics.
The protein encoded by this gene is a membrane-bound arginine/lysine carboxypeptidase. Its expression is associated with monocyte to macrophage differentiation. This encoded protein contains hydrophobic regions at the amino and carboxy termini and has 6 potential asparagine-linked glycosylation sites. The active site residues of carboxypeptidases A and B are conserved in this protein. Three alternatively spliced transcript variants encoding the same protein have been described for this gene.
, carboxypeptidase m
, renal carboxypeptidase
, urinary carboxypeptidase B
, carboxypeptidase D