RelevanceA member of the metalloproteinase family M16, nardilysin is most similar to insulin degrading enzyme, and the bacterial peptidase pitrilysin. It cleaves peptide substrates on the N terminus of arginine residues in dibasic pairs. Nardilysin was first described as a processing enzyme of somatostatin 1-28, which is cleaved at the Arg-Lys paired amino acid location. Nardilysin was named N arginine dibasic convertase (NRD convertase) to reflect this cleavage, although it was later shown that the activity was due to aminopeptidase B acting as a heterodimer with nardilysin. In addition to somatostatin 1-28, nardilysin cleaves dynorphin A and a-neoendorphin. Nardilysin was first detected in the brain and testis, and later in the heart, skeletal muscle, and in lesser amounts in most tissues and cell lines.
Recombinant Human Nardilysin protein images
SDS-PAGE - Nardilysin protein (Tagged-His Tag) (ab92081)
The image shows an electrophoretic assay performed using an Agilent 5100 ALP. In some images coloured control bands can be seen at 15 kDa (green) and/or 240 kDa (purple). The protein-specific band is blue.
References for Recombinant Human Nardilysin protein (ab92081)
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