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trypsin, mass spec, in-gel digestion, in-solution digestion, protein interactions, protein modifications, 2-D gels, proteases, phosphorylation, glycosylation , v195

Pepsin preferentially cleaves at the C-terminus of phenylalanine, leucine, tyrosine and tryptophan. Pepsin can be used alone or with other proteases for protein analysis by mass spectrometry and other applications. Activity is optimal at pH 1.0-3.0.

Pepsin preferentially cleaves at the C-terminus of phenylalanine, leucine, tyrosine and tryptophan. This protease can be used alone or in combination with other proteases for protein analysis by mass spectrometry and other applications. Pepsin activity is optimal at pH 1.0-3.0.