62354-43-2
Chemical Structure
D-Val-Leu-Lys-pNA dihydrochloride
Synonym(s): D-Val-Leu-Lys-p-itoailide dihydrochloride; D-VLK-pNA dihydrochloride; S 2251 dihydrochloride
- CAS No.: 62354-43-2
- Formula:C23H40Cl2N6O5
- Molecular Weight:551.51
IUPAC Name: (S)-6-amino-2-((S)-2-((R)-2-amino-3-methylbutanamido)-4-methylpentanamido)-N-(4-nitrophenyl)hexanamide dihydrochloride
InChIKey: VESQMNNSPPEOSZ-ZLARAOTRSA-N
SMILES: CC(C)[C@@H](N)C(N[C@@H](CC(C)C)C(N[C@@H](CCCCN)C(NC1=CC=C(C=C1)[N+]([O-])=O)=O)=O)=O.Cl.Cl
Biological Activity: D-Val-Leu-Lys-pNA (D-Val-Leu-Lys-p-nitroanilide) dihydrochloride is a chromogenic peptide substrate that serves as a characteristic substrate for plasmin and plasminogen. D-Val-Leu-Lys-pNA dihydrochloride acts as a sensitive substrate for the DFE27 serine protease derived from Bacillus subtilis DC27. Catalyzed by plasmin, D-Val-Leu-Lys-pNA dihydrochloride binds and hydrolyzes to release p-nitroaniline (pNA), which can be detected colorimetrically at 405 nm as a measure of fibrinolytic activity[1][2].
| Cat. No. | Product Name | Purity | Description | Pricing | |||||||||||||||||||
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D-Val-Leu-Lys-pNA dihydrochloride | 99.92% | D-Val-Leu-Lys-pNA (D-Val-Leu-Lys-p-nitroanilide) dihydrochloride is a chromogenic peptide substrate that serves as a characteristic substrate for plasmin and plasminogen. D-Val-Leu-Lys-pNA dihydrochloride acts as a sensitive substrate for the DFE27 serine protease derived from Bacillus subtilis DC27. Catalyzed by plasmin, D-Val-Leu-Lys-pNA dihydrochloride binds and hydrolyzes to release p-nitroaniline (pNA), which can be detected colorimetrically at 405 nm as a measure of fibrinolytic activity. | ||||||||||||||||||||
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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]
