金山科研平台，产品价格货期咨询微信：jinshanbio Source:E. coli-derived, Ser38-Pro704, with an N-terminal Met and 6-His tag Accession #:Q9BYT8 N-terminal Sequence Analysis:Met Purity:>95%, by SDS-PAGE under reducing conditions and visualized by silver stain. Endotoxin Level: Predicted Molecular Mass:77 kDa SDS-PAGE:73 kDa, reducing conditions Activity:Measured by its ability to cleave a fluorogenic peptide substrate, (7-methoxycoumarin-4-yl)acetyl-Pro-Leu-Gly-Pro-D-Lys(2,4-dinitrophenyl)-OH or Mca-PLGPK(Dnp)-OH.The specific activity is >70 pmol/min/µg, as measuredunder the describedconditions. Formulation:Supplied as a 0.2 µm filtered solution in Tris, NaCl and Glycerol.See Certificate of Analysis for details. Molecule Information: Neurolysin Aliases: AGTBP; Neurotensin Endopeptidase; NLN; Oligopeptidase M Entrez Gene IDs: 57486 (Human); 75805 (Mouse); 117041 (Rat) Background: Neurolysin Neurolysin, also known as Oligopeptidase M (mitochondrial peptidase), soluble angiotensin II-binding protein and endopeptidase EC 3.4.24.16, is a homologue of Thimet Ologopeptidase (THOP1), a zinc peptidase of the M3 family that also includes mitochondrial intermediate peptidase. Neurolysin expresses in two forms with the difference of an N-terminal transit peptide that targets the localization to mitochondria. The shorter form of Neurolysin exists in cytosol. Like THOP1, Neurolysin is capable of cleaving a number of vasoactive peptides such as bradykinin and neurotensin. All known substrates of THOP1 and Neurolysin contain 17 or fewer amino acids.