Protein Modifying Tools

Proteinase K is a subtilisin-related serine protease that hydrolyzes a variety of peptide bonds and is frequently used to cleanup enzymatic reactions or cell lysates.

• Highly characterized for more consistent performance
• Optimal activity and stability for up to 24 months
• Active in a wide range of temperatures and buffers with optimal activity between 20 and 60°C and a pH between 7.5 and 12.0.
• No detectable endonuclease, exonuclease, DNase or RNase contaminating activities

This standard is a complex mixture of peptides produced by the tryptic digest of reduced and alkylated Bovine Serum Albumin (BSA).

• Used to standardize MALDI-TOF or ESI mass spectrometers (TOF, Q-TOF, Ion Trap, or Orbitrap)
• Standardization range of 500-2400 Da
• Free of salts, glycerol and detergents
• Supplied lyophilized
• Optimal stability for up to 24 months

Trypsin-ultra, Mass Spectrometry Grade is a serine endopeptidase, which selectively cleaves peptide bonds C-terminal to lysine and arginine residues.  Trypsin-ultra cleaves at Lys-Pro and Arg-Pro bonds at a much slower rate than when Lys and Arg are N-terminal to other residues.

• Analyze complex proteomes with minimal autolysis
• Compatible for simultaneous co-digestion with PNGase F (NEB# P0709)
• Compatible for simultaneous co-digestion with Endoproteinase LysC (NEB# P8109)
• Suitable for both in-gel and solution digests
• Supplied lyophilized
• Optimal activity and stability for up to 12 months