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April 1, 2012 (Vol. 32 , No. 7)


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Four new proteases—Pepsin, Elastase, Sequencing Grade Arg-C, and Thermolysin—are provided in a lyophilized format, enabling resuspension in any buffer. Pepsin preferentially cleaves at the C-terminus of phenylalanine, leucine, tyrosine, and tryptophan. Elastase is a serine protease that can digest elastin, preferentially cleaving at the C-terminus of alanine, valine, serine, glycine, leucine, or isoleucine. Arg-C (clostripain) is a sequencing grade endopeptidase that cleaves at the C-terminus of arginine residues, including sites next to proline. Thermolysin is a thermostable metalloproteinase with an optimal digestion temperature range of 65–85°C. It preferentially cleaves at the N-terminus of the hydrophobic residues leucine, phenylalanine, valine, isoleucine, alanine, and methionine.

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