| Description : |
Carboxypeptidase M (CPM) belongs to the peptidase M14 family. CPM specifically removes C-terminal basic residues (Arg or Lys) from peptides and proteins, and the activity is inhibited by O-phenanthroline and MGTA and activated by cobalt. The amino acid sequence of CPM indicated that the C-terminal hydrophobic region might be a signal for membrane attachment via a glycosylphosphatidylinositol (GPI) anchor. CPM is involved in peptide metabolism on both the cell surface and in extracellular fluids. CPM functions not only as a protease but also as a binding partner in cell-surface protein-protein interactions. |
| Source : |
HEK293 |
| Species : |
Human |
| Tag : |
His |
| Form : |
Lyophilized from 0.22 μm filtered solution in 50 mM MES, pH 6.5 with 100 mM NaCl. Normally Mannitol or Trehalose are added as protectants before lyophilization. |
| Bio-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. |
| Molecular Mass : |
rh CPM /Carboxypeptidase M is fused with a polyhistidine tag at the C-terminus, and has a calculated MW of 47.1 kDa. The predicted N-terminus is Leu 18. DTT-reduced Protein migrates as 49 kDa in SDS-PAGE due to glycosylation. |
| Endotoxin : |
Less than 1.0 EU per μg of the rh CPM /Carboxypeptidase M by the LAL method. |
| Purity : |
>90% as determined by SDS-PAGE. |
| Storage : |
Avoid repeated freeze-thaw cycles.No activity loss was observed after storage at:In lyophilized state for 1 year (4oC); After reconstitution under sterile conditions for 3 months (-70oC). |
| Reconstitution : |
See Certificate of Analysis for reconstitution instructions and specific concentrations. |
