赖氨酰肽链内切酶

可特异性切除赖氨酸C末端的多肽，用于Lys-X化合物的合成。冻干粉，易于溶于水和缓冲液。最佳pH值9.0-9.5，来源于细菌。抑制剂是DFP，PMSF和TLCK。

Lysyl Endopeptidase, originally isolated from the soil bacterium discovered by Masaki, et al. cleaves specifically the peptide bonds at the carboxy-terminal side of Lysine residues and S-aminoethylcysteine residues with a high degree of specificity, making it a valuable tool for protein sequence analysis and for enzymatic synthesis of Lys-X compounds. An added feature of Lysyl Endopeptidase is its ability to retain complete activity after incubation in 4M urea or in 0.1% SDS solution for up to 6 hours at 30 degrees C.

• Appearance: Lyophilized form containing ca. 10% Tris-HCl buffer, pH 8.
• Activity: Shown on each label
• Molecular Weight: 27,000 (gel filtration); 30,000 (SDS electrophoresis)
• Solubility: Soluble in water or buffer solution.
• Stability: Stable at 4 degrees C, when dissolved in buffer of pH 5~12. Stable at 30 degrees C in the range of pH 6~11, but unstable at 50 degrees C or higher.
• Optimal pH: 9.0 -9.5 (Amidase activity)
• Isoelectric point: 6.9~7.0
• Substrate specificity:
  Hydrolysable substrate ... Tos-Lys-Ome, Bz-Lys-NH₂, Bz-Lys-pNA, Lys-pNA
  Unhydrolysable substrate ... Bz-Arg-NH₂, Bz-Arg-pNa, Arg-pNA
• Inhibitors: DFP, PMSF, TLCK

Originally, the source of this product was indicated as "Achromobacter lyticus" based on the physiological and morphological properties of the bacteria. However, we confirmed that the 16SrDNA sequence was highly homologous to that of Lysobacter.