D-Val-Leu-Lys-pNA acetate  (Synonyms: S-2251 acetate)

D-Val-Leu-Lys-pNA acetate (S-2251 acetate) is a chromogenic peptide substrate that serves as a characteristic substrate for plasmin and plasminogen. D-Val-Leu-Lys-pNA acetate acts as a sensitive substrate for the DFE27 serine protease derived from Bacillus subtilis DC27. Catalyzed by plasmin, D-Val-Leu-Lys-pNA acetate binds and hydrolyzes to release p-nitroaniline (pNA), which can be detected colorimetrically at 405 nm as a measure of fibrinolytic activity^[1][2].

D-Val-Leu-Lys-pNA (1 mM; 30 min at 37°C) acetate was the substrate against which purified DFE27 serine protease from Bacillus subtilis DC27 exhibits the highest amidolytic activity, with a hydrolysis rate of 225.291 mmol·min⁻¹·mL^−1[1].
D-Val-Leu-Lys-pNA (0.16 mM) acetate is hydrolyzed by Lys-gingipain from Porphyromonas gingivalis (strain H66) with a K_m of 0.2 mM, V_max of 133 mmol/min, and V_max/K_m ratio of 665^[2].

MedChemExpress (MCE) has not independently confirmed the accuracy of these methods. They are for reference only.

478.59 (free base)

C₂₃H₃₈N₆O₅·xC₂HF₃O₂

D-Val-Leu-Lys-pNA

D-Val-LK-pNA

Room temperature in continental US; may vary elsewhere.

Please store the product under the recommended conditions in the Certificate of Analysis.

• [1]. Hu Y, et al. Purification and characterization of a novel, highly potent fibrinolytic enzyme from Bacillus subtilis DC27 screened from Douchi, a traditional Chinese fermented soybean food. Sci Rep. 2019;9(1):9235. Published 2019 Jun 25.

  [2]. Pike R, et al. Lysine- and arginine-specific proteinases from Porphyromonas gingivalis. Isolation, characterization, and evidence for the existence of complexes with hemagglutinins. J Biol Chem. 1994 Jan 7;269(1):406-11.