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The protein encoded by CPM is a membrane-bound arginine/lysine carboxypeptidase. 再加上，我们可以发Carboxypeptidase M 抗体 (77) 和 Carboxypeptidase M 试剂盒 (14)和数多这个蛋白质的别的产品。
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Low CPM expression is associated with colorectal cancer.
CPM binding to extracellular loop 2 of the B1R results in positive allosteric modulation of B1R signaling, and disruption of this interaction could provide a novel therapeutic approach to reduce pathological B1R signaling.
Carboxypeptidase M expression is lost in human renal cell carcinoma tumor cells, whereas it is abundant in tumor-associated foam cells and neovasculature.
novel marker and cellular player in lipid uptake and/or metabolism of activated macrophages by promoting foam cell formation
CPM and B1Rs on cell membranes form a critical complex that potentiates B1R 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 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.
Multiple transcription start sites in two regions ~30 kb apart are flanked by two unique functional promoters. Five major types of transcripts resulting from multiple transcription start sites and alternate splicing in the 5-prime region were identified.
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