Arg-C Ultra, Mass Spec Grade
Fast, Efficient and Ultra-Specific Cysteine Protease for Use Alone or With Other Proteases for Bottom-Up Proteomics
- Proteins cleaved exclusively at the C-terminus of arginine residues
- Minimal missed cleavages under optimal digestion conditions
- Complete digestion within 30 minutes to 2 hours
- Use with Lys-C or Trypsin to produce “tryptic” peptides
- Activity in 6M urea and from pH 5–9
- Broad enzyme-to-substrate ratio range enables cost efficiency based on sample and digestion conditions
Catalog Number:
Size
Catalog Number: VA1831
Catalog Number: VA1832
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
- Characterization of post-translational modifications, particularly on lysines
- Minimization of missed cleavages in trypsin workflows using Arg-C Ultra with Lys-C or Trypsin
- Peptide mapping of biotherapeutics
- De novo peptide sequencing
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 1:50 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.
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.
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.
Protocols
Complete Protocol
Specifications
Catalog Number:
Contenido
| Item | Part # | Presentación | Concentración |
|---|---|---|---|
Arg-C Ultra, Mass Spec Grade |
VA183A | 1 × 5μg | 0.2μg/μl |
SDS
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Use Restrictions
For Research Use Only. Not for Use in Diagnostic Procedures.Condiciones de Almacenaje
Contenido
| Item | Part # | Presentación | Concentración |
|---|---|---|---|
Arg-C Ultra, Mass Spec Grade |
VA183B | 1 × 20μg | 0.2μg/μl |
SDS
Search for SDSCertificado de Análisis
Use Restrictions
For Research Use Only. Not for Use in Diagnostic Procedures.Condiciones de Almacenaje
Resources
Featured Resource
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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Featured Article: Arg-C Ultra Simplifies Histone Preparation for LC-MS/MS
Using mammalian histone extract, the authors show that Arg-C Ultra facilitates histone preparation for LC-MS/MS.
