Arg-C Ultra, Mass Spec Grade
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
Catalog Number:
Size
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)
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.
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:
What's in the box?
| Item | Part # | Size | Concentration |
|---|---|---|---|
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.Storage Conditions
What's in the box?
| Item | Part # | Size | Concentration |
|---|---|---|---|
Arg-C Ultra, Mass Spec Grade |
VA183B | 1 × 20μg | 0.2μg/μl |
SDS
Search for SDSCertificate of Analysis
Use Restrictions
For Research Use Only. Not for Use in Diagnostic Procedures.Storage Conditions
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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