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Trypsin Platinum, Mass Spectrometry Grade

va9000trypsinplatinummassspecgrad3

Trypsin for Most Accurate Biotherapeutic Protein Characterization and Specialized Proteomics Applications

  • Free of nonspecific cleavage activity commonly observed in proteomic and mass spec grade trypsins
  • Superior autoproteolytic resistance
  • Enhanced proteolytic efficiency
  • Excellent lot-to-lot reproducibility
  • Free of contaminating animal proteins

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Catalog number selected: VA9000

$ 140.00
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Trypsin Platinum, Mass Spectrometry Grade
100μg
$ 140.00
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Accurate Protein Characterization for Mass Spectrometry and RP-HPLC-UV

Trypsin Platinum, Mass Spectrometry Grade, is a recombinant protease designed for accurate protein characterization with mass spectrometry and reverse-phase high-performance liquid chromatography with UV detection (RP-HPLC-UV). It is free of any detectable nonspecific proteolytic activity. A novel chemical modification method assures maximal autoproteolytic resistance. Trypsin Platinum has high proteolytic efficiency and is free of contaminating proteins of animal origin.

Learn more about Trypsin Platinum and ask your questions in the Webinar "Biotherapeutic Protein Characterization: Overcoming the Challenges of Non-Specific Cleavage and Autoproteolysis",
Watch On Demand

Cleavage Specificity and Autoproteolytic Resistance

Commercially available proteomic and mass spec grade trypsin products contain nonspecific protease activity at a low but detectable level. Close analysis of this activity suggests it is chymotryptic in nature. The nonspecific, chymotryptic-like cleavage activity becomes evident if large amounts of trypsin are used in a digestion reaction (Figure 1, Panel A). These nonspecific cleavage activities compromise the quality of protein analysis. Our production procedure assures that Trypsin Platinum is free of any detectable traces of nonspecific cleavage activity (Figure 1, Panel B).

Autoproteolysis is another common negative side effect of trypsin digestion. To suppress trypsin autoproteolysis, trypsin used in protein mass spec sample preparation is chemically modified. Yet, a certain level of autoproteolysis is still observed (Figure 2, Panel A). The generated tryptic autoproteolytic peptides often compromise protein analysis, particularly if a large amount of trypsin is used in a digestion reaction. Our novel modification method further suppresses Trypsin Platinum autoproteolysis compared to the autoproteolysis observed in the currently available proteomic and mass spec grade trypsin products (Figure 2, Panel B), assuring that the level of autoproteolytic tryptic peptides remains negligibly low even if large quantities of Trypsin Platinum are used.

Trypsin Platinum Cleavage Specificity

RP-HPLC-UV data showing cleavage specificity of Trypsin Platinum.

Figure 1. Comparison of nonspecific proteolytic activity between Trypsin Platinum and trypsin from another supplier. Panitumumab (Vectibix®) was used as a model protein substrate. The digestion reactions used a 1:10 trypsin:protein ratio. Digested peptides were analyzed with RP-HPLC-UV. The peptide peaks were assigned with LC-MS to differentiate between specific and nonspecific peptides. Analysis showed that mass spec grade trypsin from vendor T (used for comparison) contains prominent nonspecific proteolytic activity (Panel A). Close analysis indicated a chymotryptic-like pattern of the generated nonspecific cleavages (data not shown). In contrast, Trypsin Platinum generated specific tryptic cleavages only (Panel B).

Trypsin Platinum Autoproteolytic Resistance

RP-HPLC-UV data showing autoproteolytic resistance of Trypsin Platinum.

Figure 2. Comparison of autoproteolytic activity between Trypsin Platinum and proteomic-grade trypsin from another supplier. Proteomic grade trypsin from vendor S (used for comparison) and Trypsin Platinum were incubated at conventional digestion conditions. Specifically, trypsin products were reconstituted in 100mM Tris-HCl (pH 8)/2mM CaCl2 and incubated overnight at 37°C. Autoproteolytic products were analyzed with RP-HPLC-UV. Fresh, nonincubated aliquots of either trypsin were analyzed as a control. Proteomic grade trypsin demonstrated prominent autoproteolysis, whereas autoproteolysis of Trypsin Platinum was reduced to a negligible level (compare Panels A and B).


Specifications

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Item Part # Size

Trypsin Platinum, Mass Spec Grade

VA900A 1 × 100μg

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Use Restrictions

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

Storage Conditions

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