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Fast, Efficient and Ultra-Specific Cysteine Protease for Use Alone or With Other Proteases for Bottom-Up Proteomics

  • Exclusively cleaves at the C-terminus of arginine residues including Arg-Pro sequence
  • Negligible cleavage at lysine residues, unlike standard Arg-C enzymes such as clostripain
  • Digests samples in as little as 30 minutes
  • Exhibits excellent cleavage activity in up to 6M urea
  • Robust digestion in a broad pH range from pH 5.0–9.0
  • Excellent use in combination with Lys-C to produce “tryptic” peptides

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$ 125.00

Catalog Number: VA1831

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$ 350.00

Catalog Number: VA1832

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Overview
Protocols
Specifications
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Arg-C Proteinase with Superior Cleavage Specificity and Efficiency for Mass Spec Analysis

The Arg-C Ultra protease is an endopeptidase that cleaves at the C-terminus of arginine residues, including the arginine amino acid next to the proline (Arg-Pro). This Mass Spec Grade enzyme can be used alone or in combination with other proteases for protein analysis by mass spectrometry and other applications. Arg-C Ultra has robust digestion activity with a pH range from pH 5.0–pH 9.0.

Applications

  • Protein Identification (ID)
  • Peptide mapping
  • De novo peptide sequencing
  • Characterization of post-translational modifications, particularly on lysines
  • Characterization and QA/QC of biotherapeutics (e.g., IgGs)
Bar graph showing that Arg-C Ultra offers superior specificity and efficiency over standard Arg-C and Trypsin proteases.

Arg-C Ultra offers superior specificity and efficiency over standard Arg-C and Trypsin proteases. Human K562 extract was digested overnight at 37°C with the indicated proteases using a 1:100 enzyme-to-substrate ratio. Peptides were analyzed by LC-MS/MS on an Orbitrap Exploris™ 240 (Thermo Fisher Scientific). Data analyses were conducted using Byonic software (Protein Metrics) with no enzyme specified.


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Effect of urea concentration on digestion efficiency of Arg-C Ultra, Mass Spec Grade, and Lys-C. Human K562 extract was digested with Arg-C Ultra, Mass Spec Grade, or native Lys-C at 1:100 for 2 hours at 37°C at a variety of urea concentrations. Peptides were analyzed by LC-MS/MS on an Orbitrap Exploris™ 240 (Thermo Fisher Scientific). Data analyses were conducted using Byonic software (Protein Metrics, Inc.) with no enzyme specified.


Bar graph showing the effect of pH on digestion efficiency of Arg-C Ultra, Mass Spec Grade.

Effect of pH on digestion efficiency of Arg-C Ultra, Mass Spec Grade. Human K562 extract was digested with Arg-C Ultra, Mass Spec Grade, at 1:100 for 2 hours at 37°C at different pH concentrations. Peptides were analyzed by LC-MS/MS on an Orbitrap Exploris™ 240 (Thermo Fisher Scientific). Data analyses were conducted using Byonic software (Protein Metrics, Inc.) with no enzyme specified.

Specifications

Catalog Number:

Contenido

Item Part # Presentación Concentración

Arg-C Ultra, Mass Spec Grade

VA183A 1 × 5μg 0.2μg/μl

Certificado de Análisis

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Use Restrictions

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

Condiciones de Almacenaje

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Contenido

Item Part # Presentación Concentración

Arg-C Ultra, Mass Spec Grade

VA183B 1 × 20μg 0.2μg/μl

Certificado de Análisis

Search by lot number

Use Restrictions

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

Condiciones de Almacenaje

BB

Resources

Characterization of a new ultra-selective, highly active Arginine-C protease for MS-based proteomics

Arg-C Ultra is successful in various applications, including characterization of bulk proteomes, hard-to-digest samples like muscle tissue, and post-translational modifications, particularly at lysine residues.

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