Lys-C
Lysyl endopeptidases (Lys-C) cleave specifically at the C-terminus of Lysine residues. Our recombinant sequencing grade Lys-C is produced in Escherichia coli to high purity, compatible for mass spectrometry-based proteomics analysis. Originally identified in Achromobacter lyticus, our Lys-C outperforms all alternatives by consistently delivering precision in peptide cleavage and minimizing missed cleavages. This superior cleavage efficiency ensures reproducibility and accurate results across experiments. With our Lys-C, researchers can confidently push the boundaries of discovery, unlocking a deeper understanding of complex proteomes with unprecedented reliability.
Product Details
Our Lys-C [KPL0033] is available as a liquid or lyophilized formulation. It is compatible with different sample preparation protocols and digestion buffers such as Tris-HCl and HEPES. The recommended pH range for our Lys-C is between pH 7-9. Our Lys-C retains high activity under high denaturing conditions up to 8M Urea and 2M Guanidine Chloride. We perform stringent quality control on our Lys-C with experimental conditions representative of typical proteomics experiments to guarantee consistent results across batches
Experimental conditions: Digestion of HeLa protein extract. Lys-C to protein ratio of 1:100 in 50mM HEPES pH 8.5 buffer. Sample digested overnight at 37°C and analyzed using LC/MS.
Technical Specifications
Formulation
Liquid or lyophilized
Compatible Buffers
Tris-HCl, HEPES
pH Range
7-9
High Activity Conditions
Up to 4M Urea and 2M Guanidine Chloride
Quality Control
Stringent testing under typical proteomics experimental conditions
More Technical Specifications
| Property | Specification |
|---|---|
| Product Name | Lys-C |
| Specificity | Cleaves at the C-terminus of Lysine residues |
| Formulations | Liquid, Lyophilized |
| Optimal pH Range | 7 - 9 |
| Buffer Compatibility | Tris-HCl, HEPES, Ammonium Bicarbonate, TEAB, PBS |
| Denaturing Conditions | Retains activity in up to 8M Urea and 2M Guanidine Chloride |
| Enzyme-to-Protein Ratio | 1:100 (as per experimental conditions provided) |
| Quality Control | Stringent QC under typical proteomics experimental conditions |
| Source | Recombinantly produced in Escherichia coli |
| Applications | Mass spectrometry-based proteomic analysis, various sample preparation protocols |
| Safety Data Sheet |
Quality Control
Each batch of Lys-C [KPL0033] undergoes stringent quality control under experimental conditions representative of typical proteomics experiments. This guarantees consistent results across different batches and applications.
Key Benefits of Using Lys-C
Superior Precision in Peptide Cleavage
Our Lys-C consistently delivers precision in peptide cleavage, ensuring accurate experimental results.
Minimizes Missed Cleavages
With superior cleavage efficiency, our Lys-C minimizes missed cleavages, providing more reliable data.
Ensures Reproducibility and Accurate Results
Stringent quality control ensures that Lys-C offers reproducibility and accuracy across all experiments.
Compatibility with Mass Spectrometry-Based Proteomics
Lys-C is specifically designed to be compatible with mass spectrometry-based proteomics, enhancing research outcomes.
High Activity Under Denaturing Conditions
Our Lys-C retains high activity even under high denaturing conditions, making it versatile for various experimental setups.
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Order more to save more! Our Lys-C [KPL0033] is available in different volume and weight ranges for your needs.
Frequently Asked Questions (FAQ)
1. What is Lys-C?
Lys-C is a lysyl endopeptidase that cleaves specifically at the C-terminus of lysine residues. It's widely used in proteomics for protein digestion prior to mass spectrometry analysis.
2. Where does your Lys-C sequence originate?
Our Lys-C is based on the enzyme originally identified in Achromobacter lyticus, produced recombinantly in Escherichia coli to ensure high purity and batch-to-batch consistency.
3. What formulations are available?
Lys-C [KPL0033] is available in both liquid and lyophilized formulations to suit different laboratory workflows and storage preferences.
4. What buffers are compatible with Lys-C?
Lys-C is compatible with common proteomics buffers including Tris-HCl and HEPES. The recommended pH range is 7–9.
5. Can Lys-C be used under denaturing conditions?
Yes. Our Lys-C retains high activity in up to 8M urea and 2M guanidine chloride, making it ideal for digesting proteins that require strong denaturants for solubilization.
6. What enzyme-to-protein ratio do you recommend?
We recommend a 1:100 (w/w) enzyme-to-protein ratio for overnight digestion at 37°C, though this can be adjusted based on your specific workflow.
7. Can I use Lys-C with Trypsin?
Yes! Lys-C and Trypsin are commonly used together in a sequential digestion protocol, where Lys-C is added first under denaturing conditions followed by Trypsin after dilution. However, our data suggests that Lys-C can be added simultaneously with Trypsin while delivering the same benefits thus simplifying your workflow without sacrificing digestion efficiency or peptide coverage.
8. Is Lys-C compatible with LC-MS workflows?
Yes. Our Lys-C is produced to sequencing-grade purity and is fully compatible with mass spectrometry-based proteomics analysis.
9. How should I store Lys-C?
Store lyophilized Lys-C at -20°C. Once reconstituted, aliquot and store at -20°C to avoid repeated freeze-thaw cycles.
10. How do you ensure batch-to-batch consistency?
Each batch undergoes stringent quality control under experimental conditions representative of typical proteomics workflows, guaranteeing consistent performance across batches.
References
1. van der Hoeven LR, Lechner M, Hernandez-Rollan C, Batth TS, Olsen JV. Comparative Analysis of Lysine-Specific Peptidases for Optimizing Proteomics Workflows. Journal of Proteome Research 2025. DOI: 10.1021/acs.jproteome.5c00872 https://pubs.acs.org/doi/10.1021/acs.jproteome.5c00872
A comprehensive comparison of lysine-specific peptidases for proteomics applications, providing guidance on enzyme selection for optimal workflow performance.
2. Glatter T, Ludwig C, Ahrné E, Aebersold R, Heck AJR, Schmidt A. Large-scale quantitative assessment of different in-solution protein digestion protocols reveals superior cleavage efficiency of tandem Lys-C/trypsin proteolysis over trypsin digestion. Journal of Proteome Research 2012; 11:5145–5156. https://pubs.acs.org/doi/10.1021/pr300273g
A systematic comparison showing that tandem Lys-C/trypsin digestion yields more fully cleaved peptides and reduces missed cleavages compared to trypsin alone.
3. Poulsen JW, Madsen CT, Young C, Poulsen FM, Nielsen ML. Using guanidine-hydrochloride for fast and efficient protein digestion and single-step affinity-purification mass spectrometry. Journal of Proteome Research 2013; 12:1020–1030. https://pubs.acs.org/doi/10.1021/pr300883y
Demonstrates that Lys-C digestion in guanidine-HCl can be completed in 30 minutes without introducing chemical artifacts, enabling fast and efficient proteomics workflows.
4. Navarrete-Perea J, Yu Q, Gygi SP, Paulo JA. Streamlined tandem mass tag (SL-TMT) protocol: an efficient strategy for quantitative (phospho)proteome profiling using tandem mass tag-synchronous precursor selection-MS3. Journal of Proteome Research 2018; 17:2226–2236. https://pmc.ncbi.nlm.nih.gov/articles/PMC5994137/
Describes a streamlined Lys-C/trypsin digestion protocol for TMT-based quantitative proteomics and phosphoproteomics, enabling deep proteome coverage with integrated phosphopeptide enrichment.
5. Wu Z, Huang J, Huang J, Li Q, Zhang X. Lys-C/Arg-C, a more specific and efficient digestion approach for proteomics studies. Analytical Chemistry 2018; 90:9700–9707. https://pubs.acs.org/doi/10.1021/acs.analchem.8b02448
Evaluates Lys-C in combination with Arg-C as an alternative to Trypsin digestion, demonstrating improved specificity and digestion efficiency for both qualitative and quantitative proteomics.
6. Masaki T, Tanabe M, Nakamura K, Soejima M. Studies on a new proteolytic enzyme from Achromobacter lyticus M497-1. Biochimica et Biophysica Acta 1981; 660:51–55.
The original characterization of lysyl endopeptidase from Achromobacter lyticus, describing its strict lysine specificity and high activity under denaturing conditions.
Protocols
Coming soon!