Carboxypeptidase E Mouse, Unlabeled, Clone: 35, Bd, Mouse Monoclonal Antibody, Each

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Carboxypeptidase e (cpe), also known as carboxypeptidase h and enkephalin convertase, is found as both a membrane-bound and a soluble glycoprotein in neuroendocrine tissues and adrenal-gland chromaffin granules. The c-terminus forms an amphiphilic α-helix, suggesting that this region is responsible for the membrane-bound form. Evidence suggests the active form of cpe is located in the secretory vesicles. Cpe appears to have several functions. It is an exopeptidase that cleaves neuropeptides with c-terminal basic amino acids, producing an active form of the peptide. It has also been proposed that membrane-bound cpe is a sorting receptor for regulated secretory pathway (rsp) proteins in the tgn pituitary golgi and secretory granule membranes. Rsp proteins primarily consist of hormones and neuropeptides. Mice that carry a mutation in the cpe gene cpe[fat] display endocrine disorders such as obesity, infertility, and hyperproinsulinemia. Furthermore, the same endocrine disorders are observed in cpe[fat] mice where the cpe gene has been effaced by antisense rna.Immunofluorescence, immunohistochemistry, immunoprecipitation, western blotting