Product introduction
Lysyl endonuclease, also known as lysyl endopeptidase, Lys-C endonuclease, is a serine protease originally discovered and isolated from soil bacteria by Masaki et al. The enzyme is highly specific and specifically cleaves peptide bonds at the carboxy terminus of lysine residues and S-aminoethyl cysteine residues. It has also been reported to have a small amount of non-specific cleavage.
This enzyme is a very valuable tool enzyme for protein sequence analysis and bioproduct production. The enzyme can be used alone or in combination with other proteases, and the digested protein can be used for peptide mapping and preparation of the protein of interest. The product is a recombinant lysyl endonuclease powder which is isolated and purified from recombinant E. coli and then freeze-dried.This product is a biochemical-grade genetically engineered enzyme. It does not contain enzyme inhibitors such as DFP, PMSF and TLCK. It has the same activity and specificity as natural lysyl endo enzyme and can be used in biological products such as insulin and GLP-1.
Product FeatureAppearances: White or off-white powder.
Specific activity: ≥1.0AU/mg pro. (Check COA).
MW: 36kD±3.6kD.
Purity: Single main band (SDS-PAGE) with a molecular weight of 27.7 kD ± 2.8 kD(SDS-PAGE).
Optimum pH: 8.5~9.5
Solubility: Soluble in buffer
Enzyme activity definition: At 30 °C, pH 9.5, the amount of enzyme that produces 1 μmol of p-nitroaniline per minute for the catalytic substrate is 1 AU.
Notice and Disclaimera. The product may self-digest when the temperature exceeds 37°C. Most of the viability is retained in 1M urea or 0.1% SDS.b. The product has moisture absorption and should be taken after room temperature balance.c. The product is for research use only and should not be used for diagnosis or treatment of animals or humans.