Carboxypeptidase M Active Protein | CPM active protein

Carboxypeptidase M Protein, Human, Recombinant (His Tag)

Cat. Num. AAA8120751

• Purity: >98% as determined by SDS-PAGE
• Synonyms: Carboxypeptidase M; Carboxypeptidase M Protein; Human; Recombinant (His Tag); Human Carboxypeptidase M/CPM Protein (His Tag); carboxypeptidase M; CPM active protein

• Host: HEK293 Cells
• Purity/Purification: >98% as determined by SDS-PAGE
• Form/Format: Lyophilized from sterile PBS, pH7.4. Normally 5%-8% trehalose, mannitol and 0.01% Tween80 are added as protectants before lyophilization. Please refer to the specific buffer information in the hard copy of CoA.
• Sequence: Met1-His422

• Species: Human
• Activity: Measured by its ability to release Larginine from BenzoylAlaArg, with detection of the arginine amino group by ophthaldialdehyde. The specific activity is >40,000pmoles/min/ug.
• Endotoxin: <1.0EU per ug of the protein as determined by the LAL method
• Predicted N Terminal: Leu 18
• Tag: C-His
• Protein Construction: A DNA sequence encoding the human CPM (NP_938079.1) without the propeptide (Met 1-His 422) was expressed, fused with a polyhistidine tag at the C-terminus.
• Reconstitution: A hardcopy of COA with reconstitution instruction is sent along with the products. Please refer to it for detailed information.
• Preparation and Storage: Samples are stable for up to twelve months from date of receipt at -20 degree C to -80 degree C. Store it under sterile conditions at -20 degree C to -80 degree C. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.; In general, recombinant proteins are provided as lyophilized powder which are shipped at ambient temperature. Bulk packages of recombinant proteins are provided as frozen liquid.; They are shipped out with blue ice.

SDS-Page

Related Product Information for CPM active protein

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.

References

Deddish PA. et al., 1990, J Biol Chem. 265 (25): 15083-9. Nagae A. et al., 1992, J Neurochem. 59 (6): 2201-12. Skidgel RA. et al., 1996, Immunopharmacology. 32 (1-3): 48-52. Deiteren K. et al., 2009, Clin Chim Acta. 399 (1-2): 24-39.

NCBI and Uniprot Product Information

• NCBI GI #: 38327526
• NCBI GeneID: 1368
• NCBI Accession #: NP_938079.1
• NCBI GenBank Nucleotide #: NM_198320.3
• UniProt Accession #: P14384; Q9H2K9; B2R800
• Molecular Weight: 50,514 Da
• NCBI Official Full Name: carboxypeptidase M
• NCBI Official Synonym Full Names: carboxypeptidase M
• NCBI Official Symbol: CPM
• NCBI Protein Information: carboxypeptidase M
• UniProt Protein Name: Carboxypeptidase M
• Protein Family: Carboxypeptidase
• UniProt Gene Name: CPM
• UniProt Synonym Gene Names: CPM
• UniProt Entry Name: CBPM_HUMAN

NCBI Description

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. [provided by RefSeq, Jul 2008]

Uniprot Description

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. Belongs to the peptidase M14 family.

Protein type: Protease; Membrane protein, GPI anchor; EC 3.4.17.12

Chromosomal Location of Human Ortholog: 12q14.3

Cellular Component: cell surface; plasma membrane

Molecular Function: zinc ion binding; carboxypeptidase activity; metallocarboxypeptidase activity

Biological Process: anatomical structure morphogenesis; proteolysis