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| Product Name | Mass-Spectrometry-Grade Recombinant Lys-C |
| Catalog No. | IVDRM-0304 |
| Description | A recombinant lysyl endopeptidase (Lys-C) produced in E. coli that reproduces the specificity of the natural Achromobacter enzyme: it hydrolyses amide, ester and peptide bonds on the carboxyl side of lysine. The preparation is free of contaminating proteases such as Lys-N or Arg-C, shows a single major band on electrophoresis, and is frequently combined with trypsin to lower the proportion of missed lysine sites in shotgun proteomics. |
| Intended Use | Protein identification by mass spectrometry, alone or in parallel digestion with mass-grade trypsin. |
| Principle / Technology | Cleaves peptide bonds specifically at the carboxyl side of lysine residues, generating longer peptides than trypsin at lysine-dense regions. |
| Detection Method | Peptide bonds C-terminal to lysine |
| Sample Type | Denatured or urea-treated protein extracts; the enzyme retains activity in strongly denaturing buffers commonly used before digestion |
| Performance Range / Specifications | Specific activity of at least 3.0 AU/mg; single major band on SDS-PAGE; molecular mass 29 +/- 3 kDa |
| Specificity | Highly specific for lysine carboxyl-side amide, ester and peptide bonds; free of Lys-N, Arg-C and other contaminating serine proteases |
| Reaction Conditions / Protocol | Dissolve or dilute the enzyme in the recommended buffer, combine with the denatured substrate and incubate; for complex digests, pair with trypsin to reduce missed lysine cleavages. |
| Components / Formulation | Supplied as a concentrated solution in sodium acetate/EDTA buffer |
| Storage Conditions | -25 to -15 °C |
| Shelf Life | 12 months from the release date |
| Package Specifications | 20 microgram and 5 x 20 microgram packs |
| Product Form | Sterile-filtered solution, 1.0 mg/mL |
| Quality Control | Verified by electrophoresis (single main band) with activity assigned against a chromogenic lysine substrate |
| Key Features | E. coli expression with no animal-derived content; specificity identical to the natural enzyme; clean single-band purity; effective companion enzyme to trypsin for lowering missed-cleavage rates |
| Purity | At least 95% |
| Concentration | 1.0 mg/mL |
| Activity / Unit Definition | At least 3.0 AU/mg; one AU is the enzyme amount that generates 1 micromol of AC-Lys-pNA per minute at 37 °C in 25 mmol/L Tris-HCl, pH 9.0 |
| Molecular Weight | 29 +/- 3 kDa |
| Source / Origin | Recombinant expression in Escherichia coli |
| pH Range / Optimal pH | pH 5.5 in the storage formulation |
| Shipping Conditions | Cold pack |
| Expiration Date / Stability | One year at -25 to -15 °C |
| Regulatory / Compliance | Research-grade raw material |
| Compatibility | Compatible with urea and other denaturants used in proteomic sample preparation; activity defined in Tris buffer at alkaline pH |
| Recommended Buffer System | 5 mM sodium acetate, 10 mM EDTA, pH 5.5 |
| Application Notes / Precautions | Avoid repeated freeze-thaw; keep EDTA-containing formulation intact; when sequencing digestion conditions, confirm buffer compatibility with the downstream MS platform. |
| Batch-to-Batch Consistency | Lot-controlled; lot number on the vial label |
| Model Type | Recombinant lysyl endopeptidase, mass-spectrometry grade |
| Starting Material / Tissue Site | Denatured protein extracts prepared for peptide mass fingerprinting or LC-MS/MS |
| Delivery Standard | Supplied frozen in single-use or multi-use packs |
| Readouts / Downstream Assays | Peptide yield and lysine-site coverage by LC-MS/MS |
For in vitro diagnostic use.
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