Recombinant Asp-N from Yinjia Bio is of microbial origin and expressed in an Escherichia coli system. As a metalloprotease, it requires zinc ions as a cofactor. It specifically cleaves the peptide bonds at the N-terminus of aspartic acid and cysteine in phosphate, acetate, or Tris buffers at pH 6.0–8.5. If cysteine is reduced or alkylated, only the peptide bond at the N-terminus of aspartic acid is cleaved.
Product images are for reference only.
Applications
(1)Protein structure analysis.
(2)Protein sequence analysis.
Advantages
(1)High purity: free from other protease contamination, with no endo- or exoglycosidase activities.
(2)High specificity: strict cleavage site specificity.
(3)High efficiency: when used in combination with recombinant trypsin, it improves protein digestion.
Information
Asp-N, Liquid
(1)Product Name: Recombinant Asp-N
(2)Catalog No. : YJ-O-320
(3)Size: 5 µg / 10 µg / 20 µg / 50 µg
(4)Storage temperature: -20 °C
Asp-N, Lyophilized
(1)Product Name: Recombinant Asp-N, Lyophilized
(2)Catalog No. : YJ-O-340
(3)Size: 2 µg / 5 µg
(4)Storage temperature: 2–8 °C
