||Recombinant Human CPE MS Standard Protein, C13 and N15-labeled (CPE, Heavy Labeled) Glu 26 - Ser 453 (Accession # NP_001864.1) was produced in human 293 cells (HEK293).
||Carboxypeptidase E (CPE), also known as Carboxypeptidase H or enkephalin convertase. Carboxypeptidase E cleaves C-terminal amino acid residues and is involved in neuropeptide processing. It is a peripheral membrane protein. CPE specifically binds regulated secretory pathway proteins, including prohormones, but not constitutively secreted proteins. Carboxypeptidase E appears to have several functions. The active form of carboxypeptidase E was shown to be in secretory vesicles, where it acts as an exopeptidase to activate neuropeptides, It does that by cleaving off basic C-terminal amino acids, producing the active form of the peptide. Products of carboxypeptidase E include insulin, enkephalin, and most other neuroendocrine peptides.It has also been proposed that membrane-associated carboxypeptidase E acts as a sorting signal for regulated secretory proteins in the trans-Golgi network of the pituitary and in secretory granules; regulated secretory proteins are mostly hormones and neuropeptides. Mice with mutant carboxypeptidase E Cpe, display endocrine disorders like obesity and infertility.[1-3]
||Lyophilized from 0.22 μm filtered solution in PBS, pH7.4. Normally Mannitol or Trehalose are added as protectants before lyophilization.
||CPE, Heavy Labeled, fused with 6×His tag at the C-terminus, has a calculated MW of 49 kDa. The predicted N-terminus is Glu 26. DTT-reduced Protein migrates as 53 kDa.
||Less than 1.0 EU per μg of the CPE, Heavy Labeled by the LAL method.
||>95% as determined by SDS-PAGE.
||Avoid repeated freeze-thaw cycles.No activity loss was observed after storage at:In lyophilized state for 1 year (4oC-8oC); After reconstitution under sterile conditions for 1 month (4oC-8oC) or 3 months (-20oC to -70oC).