Product Description
APPLICATION
- Biological medicine production (such as insulin, GLP-1 drugs)
FEATURES
- Patented technology products;
- High purity and high catalytic efficiency;
- Specific activity ≥ 2.5AU/mg pro.
AI Product Description
*The following content is generated by AI and is for reference only.
Recombinant Lysyl Endopeptidase, also known as Lys-C or Lysyl endopeptidase, is a highly purified serine protease produced through recombinant DNA technology in *Escherichia coli*. This enzyme exhibits exceptional specificity for cleaving peptide bonds on the carboxyl side of lysine residues within polypeptide chains. Unlike its microbial counterpart, the recombinant version offers superior consistency, higher specific activity, and minimal contamination with other proteolytic activities, making it an ideal choice for biochemical research requiring high precision.
The molecular formula of the mature protein varies slightly depending on the specific construct and purification tags, but the catalytic domain typically corresponds to a mass of approximately 34 kDa. While a single universal CAS number may not exist for every commercial batch due to proprietary production methods, this enzyme is generally cataloged under CAS numbers associated with *Aspergillus* species derivatives or specific recombinant identifiers provided by manufacturers like Wako or Thermo Fisher. Its biochemical grade designation ensures suitability for sensitive applications where purity is paramount.
The primary application of Recombinant Lysyl Endopeptidase lies in protein sequencing and mass spectrometry-based proteomics. It serves as a powerful alternative to trypsin for digesting proteins into peptides. Because it generates longer peptide fragments compared to trypsin, it is particularly effective for analyzing proteins containing extensive disulfide bridges or those that are difficult to solubilize. Furthermore, its unique cleavage pattern complements trypsin digestion, allowing researchers to achieve more comprehensive sequence coverage when used in tandem. The enzyme remains active in various denaturing conditions, including in the presence of urea and SDS, which facilitates the digestion of complex or aggregated samples without the need for prior reduction and alkylation steps in some protocols.
In addition to proteomics, this reagent is utilized in peptide synthesis, structural biology studies, and the generation of specific epitopes for antibody development. Its stability and reliability have made it a standard tool in modern laboratories dedicated to understanding protein structure, function, and interactions. Researchers appreciate its ability to produce reproducible results across different experimental setups, thereby accelerating discovery in fields ranging from drug development to biomarker identification.