Modified Aspartic-N

3 x 5 µg

substance packed in 3 individually sealed vials

Highly purified modified Aspartic with extremely low autolysis and therefore greater control of protein fragmentation. Consistent Enzyme activity over long digestion periods. Characteristics: Endoproteinase Asp-N is a metallo enzyme isolated from a mutant of Pseudomonas fragi. The enzyme specifically hydrolyzes peptide bonds on the N-terminal side of aspartic and cysteic acids. Its optimum activity is at pH 6.5 – 8.0. The enzyme has a molecular weight of 27 kD. Chemical modification: Asp-N endoproteinase is subjected to extensive purification to remove contaminating proteases which could affect the specificity of the digestion process. The highly purified enzyme is subsequently modified chemically by a special process. As a result, the modified enzyme is more resistant to autolysis and has improved stability. The modified enzyme retains at least 80% of its activity after 6 hours incubation at 30°C in reaction buffer and at least 65% of its activity after 24 hours incubation under the same conditions.

Productnumber: S5443.0305

Deutsche Produktseite:
Modifiziertes Aspartin-N 3 x 5 µg  Proteins & Enzymes