Recombinant Mouse Carboxypeptidase M/CPM Protein (His Tag)(Active) | PKSM040403

Recombinant Mouse Carboxypeptidase M/CPM Protein (His Tag)(Active) | PKSM040403 | Gentaur US, UK & Europe Disrtribition

Synonyms: Carboxypeptidase M;CPM

Active Protein: Active protein

Activity: A DNA sequence encoding the extracellular domain of mouse CPM isoform 1 (Q80V42-1) (Met 1-His 422), without the propeptide, was fused with a C-terminal polyhistidine tag.

Protein Construction: A DNA sequence encoding the extracellular domain of mouse CPM isoform 1 (Q80V42-1) (Met 1-His 422), without the propeptide, was fused with a C-terminal polyhistidine tag.

Fusion Tag: C-His

Species: Mouse

Expressed Host: HEK293 Cells

Shipping: This product is provided as lyophilized powder which is shipped with ice packs.

Purity: > 97 % as determined by reducing SDS-PAGE.

Endotoxin: < 1.0 EU per μg of the protein as determined by the LAL method.

Stability and Storage: Generally, lyophilized proteins are stable for up to 12 months when stored at -20 to -80℃. Reconstituted protein solution can be stored at 4-8℃ for 2-7 days. Aliquots of reconstituted samples are stable at < -20℃ for 3 months.

Molecular Mass: 47.8 kDa

Formulation: Lyophilized from sterile PBS, pH 7.4

Reconstitution: Please refer to the printed manual for detailed information.

Background: Carboxypeptidase M, also known as CPM, is a membrane-bound arginine/lysine carboxypeptidase which is a member of the carboxypeptidases family. These enzymes remove C-terminal amino acids from peptides and proteins and exert roles in the physiological processes of blood coagulation/fibrinolysis, inflammation, food digestion and pro-hormone and neuropeptide processing. Among the carboxypeptidases CPM is of particular importance because of its constitutive expression in an active form at the surface of specialized cells and tissues in the human body. CPM in the brain appears to be membrane-bound via a phosphatidylinositol glycan anchor. CPM is widely distributed in a variety of tissues and cells. 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.

Research Area: N/A