AMPM1 rabbit pAb - 100 μL

Catalytic activity: Release of N-terminal amino acids, preferentially methionine, from peptides and arylamides. Cofactor: Binds 1 sodium ion per subunit. The sodium ion has a structural role. Cofactor: Binds 2 cobalt ions per subunit. Cofactor: Binds 2 cobalt ions per subunit. The true nature of the physiological cofactor is under debate. The enzyme is also active with zinc, manganese or divalent iron ions. function: Removes the amino-terminal methionine from nascent proteins. function: Removes the amino-terminal methionine from nascent proteins. Required for normal progression through the cell cycle. similarity: Belongs to the peptidase M24A family.