Recombinant Lysyl Endopeptidase is a serine protease of non-animal origin, which can specifically cleave the peptide bond at the carboxyl end of lysine residue. The optimum reaction pH is 9.0-9.5, and the isoelectric point is 6.9-7.0. The optimum reaction temperature is 30-37°C, and the stability decreases above 50°C. The biological activity is inhibited by DFP, PMSF and TLCK.
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Cat. No.: RLE-10 (for 10AU)
Cat. No.: RLE-100 (for 100AU)
Cat. No.: RLE-1k (for 1000AU)
Source: Escherichia coli
Appearance: White lyophilized powder
Activity: ≥ 1AU/mg
Purity (SDS-PAGE): Single major protein band
Specificity: Specific cleavage of lysine residues
Stability: After incubating in 4 mol/l urea or 0.2% SDS at 30°C for 6 h, the activity of the endopeptidase did not decrease.
Recommended Reaction System
System: 20-50 mM Tris-HCl (pH 8.5-9.5) to dissolve Recombinant Lysyl Endopeptidase
Enzyme: fusion protein = 1-100 AU: 1g (pH 9.0-10.0, temperature 25-37°C, reaction time 2-24h)
After dissolving, packed separately and store below -15°C.
It is suggested that the enzyme should be digested after desalination. If desalination is not possible, we recommend increasing the amount of enzyme and extend the digestion time.
The lyophilized powder of this product can be stored at -15°C for at least 24 months. No activity loss after repeated freezing and thawing at -20°C for 5 times when dissolved in Tris-HCl.
Only for research and not intended for treatment of humans or animals