Trypsin Gold, Mass Spectrometry Grade

by Promega
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V5280

Description

  • Overview
  • Protocols
  • Specifications
  • Resources
  • Trypsin is a serine protease that specifically cleaves at the carboxylic side of lysine and arginine residues. The stringent specificity of trypsin is essential for protein identification. Native trypsin is subject to autolysis, generating pseudotrypsin, which exhibits a broadened specificity including a chymotrypsin-like activity. Such autolysis products, present in a trypsin preparation, would result in additional peptide fragments that could interfere with database analysis of the mass of fragments detected by mass spectrometry. Trypsin Gold, Mass Spectrometry Grade, is manufactured to provide maximum specificity. Lysine residues in the porcine trypsin have been modified by reductive methylation, yielding a highly active and stable molecule that is extremely resistant to autolytic digestion. The specificity of the purified trypsin is further improved by TPCK treatment, which inactivates chymotrypsin. The treated trypsin is then purified by affinity chromatography and lyophilized to yield Trypsin Gold, Mass Spectrometry Grade. It is resistant to mild denaturing conditions such as 0.1% SDS, 1M urea or 10% acetonitrile and retains 50% of its activity in 2M guanidine HCl. The activity of trypsin is decreased when acidic residues are present on either side of a susceptible bond. If proline is at the carboxylic side of lysine or arginine, the bond is almost completely resistant to cleavage.

    Each lot of quality-tested Trypsin Gold, Mass Spectrometry Grade, is qualified for use with in-gel digestion and mass spectrometric analysis. For more information, see the Protein Purification and Analysis chapter of the Protocols and Applications Guide.

    Learn more about our custom options for this product at: www.promega.com/custom/

    Applications
    • Trypsin digestion of proteins from 1 or 2-D gels.
    • Tryptic digestion of proteins in-solution.

     

    Spectrogram of bovine carbonic anhydrase II digested by Trypsin Gold, Mass Spectrometry Grade.
    Spectrogram of bovine carbonic anhydrase II digested by Trypsin Gold, Mass Spectrometry Grade.
    Cut sites for Arg-C, Sequencing Grade; Glu-C, Sequencing Grade; Asp-N, Sequencing Grade; Trypsin Gold, Mass Spectrometry Grade; Sequencing Grade Modified Trypsin; Immobilized Trypsin; Chymotrypsin, Sequencing Grade; Endoproteinase Lys-C, Sequencing Grade; rLys-C, Mass Spec Grade.
    Cut sites for Arg-C, Sequencing Grade; Glu-C, Sequencing Grade; Asp-N, Sequencing Grade; Trypsin Gold, Mass Spectrometry Grade; Sequencing Grade Modified Trypsin; Immobilized Trypsin; Chymotrypsin, Sequencing Grade; Endoproteinase Lys-C, Sequencing Grade; rLys-C, Mass Spec Grade.
  • Protocols

    Complete Protocol

    Download PDF

    Trypsin Gold, Mass Spectrometry Grade Technical Bulletin

    PDF (354 KB)

    Video Protocols

    trypsin01-fallback
  • Certificate of Analysis

    Lookup Certificate of Analysis

    Storage Conditions

    -30C TO -10C

    Use Restrictions

    For Research Use Only. Not for Use in Diagnostic Procedures.

  • Resources

    Citations

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