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ProAlanase and ProAlanase Plus (Mass Spec Grade)

Site-Specific Endoprotease that Targets Proline and Alanine

  • Available in two concentrations
  • ProAlanase, Mass Spec Grade: 5µg, frozen at 0.2µg/µl
  • ProAlanase Plus, Mass Spec Grade: 15µg, frozen at 0.5µg/µl
  • Early access material; please contact us for more information

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This product is discontinued
ProAlanase and ProAlanase Plus (Mass Spec Grade)

ProAlanase, the Newest Alternative to Trypsin for Proteomic Research

ProAlanase is an endoprotease that preferentially cleaves proteins on the C-terminal side of proline and, to a lesser extent, alanine amino acids. Isolated and purified from the fungus Aspergillus niger, ProAlanase is also known as An-PEP or EndoPro. Peptides derived from protein digestion with ProAlanase are suitable for identification and characterization by mass spectrometry.

Digestion with trypsin often provides incomplete sequence coverage or missed identification of post-translational modifications. Like Trypsin, alternative proteases such as Lys-C, Asp-N, Glu-C and Arg-C also cleave at charged residues, introducing bias to regions within proteins that are digested. The newest solution is ProAlanase, which cleaves at unique, non-charged sites in the proteome.

C-terminal cleavage specificity of ProAlanase.

Figure 1. C-terminal cleavage specificity of ProAlanase. Human K562 extract was digested with ProAlanase at pH 1.5 for 2 hours at 37°C using a 1:100 enzyme:substrate ratio. Peptides were analyzed by LC-MS/MS on a Q-Exactive Plus. Data were searched using Byonic™ software with no enzyme specified. Cleavage occurs predominantly on the C-terminal side of proline and alanine

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