D-Val-Leu-Lys-pNA acetate
Based on 1 Customer Validation
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.
For research use only. We do not sell to patients.
- Purity: 99.74%
- Formula: C23H38N6O5·xC2HF3O2
- Molecular Weight:478.59 (free base)
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Storage:
Sealed storage, away from moisture and light.
Powder -80°C, 2 years , -20°C, 1 year* In solvent : -80°C, 6 months; -20°C, 1 month (sealed storage, away from moisture and light)
Biological Activity
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 Km of 0.2 mM, Vmax of 133 mmol/min, and Vmax/Km ratio of 665[2].
MedChemExpress (MCE) has not independently confirmed the accuracy of these methods. They are for reference only.
Chemical Information
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Appearance Solid
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Molecular Weight 478.59 (free base)
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Formula C23H38N6O5·xC2HF3O2
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Color White to off-white
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Synonyms
S-2251 acetate
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Sequence
D-Val-Leu-Lys-pNA
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Sequence Shortening
D-Val-LK-pNA
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Shipping
Room temperature in continental US; may vary elsewhere.
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Storage
Sealed storage, away from moisture and light
Powder -80°C 2 years -20°C 1 year * In solvent : -80°C, 6 months; -20°C, 1 month (sealed storage, away from moisture and light)
Solvent & Solubility
DMSO : 100 mg/mL (Need ultrasonic; Hygroscopic DMSO has a significant impact on the solubility of product, please use newly opened DMSO)
Purity & Documentation
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Data Sheet (273 KB)
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SDS (254 KB)
- English - EN (254 KB)
- Français - FR (254 KB)
- Deutsch - DE (254 KB)
- Norwegian - NO (254 KB)
- Español - ES (254 KB)
- Swedish - SV (254 KB)
- Italian - IT (254 KB)
- Korean - KR (254 KB)
- Portuguese - PT (254 KB)
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Handling Instructions (2659 KB)
References
[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. [Content Brief]
[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. [Content Brief]
Calculators
Concentration (start) × Volume (start) = Concentration (final) × Volume (final)