Proteases

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NEB offers several proteases with different recognition sites.

Trypsin-ultra, Mass Spectrometry Grade  (NEB #P8101) selectively cleaves peptide bonds C-terminal to lysine and arginine residues (1). Endoproteinase LysC (NEB #P8109) is a serine endoproteinase that cleaves peptide bonds at the carboxyl side of lysine. Endoproteinase AspN (NEB #P8104) and Endoproteinase GluC (NEB #P8100) selectively cleave peptide bonds N-terminal to aspartic acid residues and C-terminal to glutamic acid, respectively. These proteases are ideal for proteome analysis by mass spectrophotometry. Proteinase K (NEB # P8107) is a non-specific, subtilisin-related serine protease with a very high specific activity. Furin (NEB #P8077)  is a ubiquitous subtilisin-like proprotein convertase with a minimal cleavage site requirement of Arg-X-X-Arg'.

We also offer several proteases with unique, specific recognition sites. Enterokinase (NEB #P8070) is a specific protease that cleaves after lysine at its cleavage site Asp-Asp-Asp-Asp-Lys. Factor Xa (NEB #P8010) cleaves after the arginine residue in its preferred cleavage site Ile-(Glu or Asp)-Gly-Arg. This protease can be used with the pMAL™ protein fusion and purification system (NEB #E8200) during the purification step.

References

  1. Northrop, J.H. and Kunitz, M. (1931)  Science, 73, 262-263. PMID: 17755302
pMAL™ is a trademark of New England Biolabs, Inc.

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Protease Selection Chart