Carboxypeptidase E/CPE Protein, Human (428a.a, HEK293, His)

Carboxypeptidase E (CPE), which cleaves C-terminal amino acid residues and is involved in neuropeptide processing, is itself subject to intracellular processing Carboxypeptidase E (CPE) is an enkephalin-convertase that cleaved a C-terminal basic residue from enkephalin precursors to generate enkephalin^[1].
CPE is a glycoprotein, which is synthesized as a larger inactive precursor. It is exclusively synthesized by membrane-bound polyribosomes in the brain^[1][2].
There exists two forms of CPE, soluble and membrane-bound in most tissues with CPE activity. These two forms differ slightly in molecular weight, but have identical enzymatic properties. Both forms arise from the same precursor, which is encoded by a single gene. This gene is a member of a carboxypeptidase gene family that includes CPA and CPB^[2].

Human

HEK293

C-His

P16870-1/NP_001864.1 (E26-S453)

1363

Partial

Approximately 53 kDa, based on SDS-PAGE under reducing conditions, due to the glycosylation.

Greater than 90% as determined by reducing SDS-PAGE.

<1 EU/μg, determined by LAL method.