Anti-AMPM1

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., Protein function: Cotranslationally removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met- Ala-, Cys, Gly, Pro, Ser, Thr, or Val). Required for normal progression through the cell cycle. [The UniProt Consortium] Recommended dilutions: WB 1:500-2000 ELISA 1:5000-20000. Cellular localization: Cytoplasm .