Recombinant Asp-N Protease, MS Grade

Recombinant Asp-N protease (MS grade) is a recombinant endoprotease that specifically hydrolyzes peptide bonds N-terminal to aspartic acid residues. It is a highly active protease cloned from Stenotrophomonas maltophilia and purified from Escherichia coli, suitable for proteomic analysis of complex mixtures.

rAsp-N protease, MS grade; Recombinant Asp-N endopeptidase, MS grade; Recombinant asparagine-specific endopeptidase, MS grade; MS grade recombinant Asp-N protease; Mass spec grade recombinant Asp-N

25 kDa

Min. 90%

According to HPLC analysis, when Cecropin A is incubated with rAsp-N at 30°C for 15 minutes using an enzyme-to-substrate ratio of 1:1,000, at least 90% of Cecropin A is digested.

Mass spectrometry

Lyophilized powder

Store at -20°C for long term storage.

Recombinant Asp-N protease (MS grade) is an endonuclease specifically used for proteomics research, which can specifically cleave peptide bonds at the N-terminus of aspartic acid residues. Due to its high specificity and reliable enzymatic cleavage efficiency, it has a wide range of applications in protein digestion, peptide fingerprint analysis and mass spectrometry detection. The use of mass spectrometry grade Asp-N protease can generate peptides suitable for high-sensitivity mass spectrometry analysis, which helps to accurately identify protein sequences, locate post-translational modifications, and deeply analyze complex protein samples, thus playing an important role in biomedical research and new drug development.