Cat.No. : |
CPE-210H |
Product Overview : |
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) with fully chemically defined cell culture medium to obtain >99% incorporation efficien |
Description : |
Carboxypeptidase E (CPE) is 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. |
Source : |
HEK293 |
Species : |
Human |
Tag : |
His |
Form : |
Lyophilized from 0.22 μm filtered solution in PBS, pH7.4. Normally Mannitol or Trehalose are added as protectants before lyophilization. |
Molecular Mass : |
CPE, Heavy Labeled is fused with polyhistidine tag at the C-terminus, and has a calculated MW of 49 kDa. The predicted N-terminus is Glu 26. DTT-reduced Protein migrates as 53 kDa in SDS-PAGE .CPE, Heavy Labeled is labeled with [U- 13C6, 15N4]-L-Arginine |
Endotoxin : |
Less than 1.0 EU per μg of the CPE, Heavy Labeled by the LAL method. |
Purity : |
>95% 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. |