carboxypeptidase M Protein (recombinant mouse)

Activity: Measured by its ability to release Larginine from BenzoylAlaArg, with detection of the arginine amino group by ophthaldialdehyde.The specific activity is >40,000 pmoles/min/µg. Protein Construction: Recombinant Mouse carboxypeptidase M is produced by our Mammalian expression system and the target gene encoding Leu18-Ser423 is expressed with a 6His tag at the C-terminus. Sequence: Leu18-Ser423. Fusion tag: C-6His Endotoxin: < 1.0 EU per µg as determined by the LAL method. Apparent Molecular Mass: 56kDa. Protein function: Carboxypeptidase M (CPM) belongs to the peptidase M14 family, and exists in cell membrane. The protein binds 1 zinc ion per subunit, and cleavage of C-terminal arginine or lysine residues from polypeptides. CPM specifically removes C-terminal basic residues (Arg or Lys) from peptides and proteins. It is believed to play important roles in the control of peptide hormone and growth factor activity at the cell surface, and in the membrane-localized degradation of extracellular proteins. Protein function: Specifically removes C-terminal basic residues (Arg or Lys) from peptides and proteins. It is believed to play important roles in the control of peptide hormone and growth factor activity at the cell surface, and in the membrane-localized degradation of extracellular proteins. [The UniProt Consortium]