Aminopeptidase N, Rat

Native aminopeptidase N purified from rat renal brush-border membranes and cleaved with papain to produce soluble enzyme. A single-chain, integral membrane protease that functions to remove N-terminal amino acids from peptides with broad specificity. Aminopeptidase N is believed to play a role in angiogenesis and elevated levels of aminopeptidase N have been reported in patients with various types of cancer and have been correlated with tumor load. Also involved in the final stages of digestion of small peptides in the intestinal brush border.

Native aminopeptidase N purified from rat renal brush-border membranes and cleaved with papain to produce soluble enzyme. A single-chain, integral membrane protease that, functions with broad specificity to remove N-terminal amino acids from peptides. It has been reported that levels of aminopeptidase N are elevated in cancer subjects and correlate with tumor load, and thus, the enzyme is believed to play a role in angiogenesis.

Please refer to vial label for lot-specific concentration.

Toxicity: Standard Handling (A)

One unit is defined as the amount of enzyme that will hydrolyze 1.0 µmol L-Leu-pNA per min at 37°C, pH 7.2

In 200 mM NaCl, 50 mM Tris-HCl, pH 8.0.

Bhagwat, S.V., et al. 2003. Blood101, 1818.
van Hensbergen, Y., et al. 2002. Clin. Cancer Res.8, 3747.
Ishii, K., et al. 2001. Biol. Pharm. Bull.24, 226.

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