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V6258

Sigma-Aldrich

D-Val-Leu-Arg p-nitroanilide diacetate salt

≥95% (HPLC), suitable for ligand binding assays

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About This Item

Empirical Formula (Hill Notation):
C23H38N8O5 · 2 C2H4O2
CAS Number:
Molecular Weight:
626.70
MDL number:
UNSPSC Code:
12352209
PubChem Substance ID:
NACRES:
NA.26

product name

D-Val-Leu-Arg p-nitroanilide diacetate salt, ≥95% (HPLC)

Assay

≥95% (HPLC)

form

powder

composition

Peptide content, ~70%

technique(s)

ligand binding assay: suitable

color

white

storage temp.

−20°C

SMILES string

CC(O)=O.CC(O)=O.N[C@H](C(C)C)C(N[C@@H](CC(C)C)C(N[C@@H](CCCNC(N)=N)C(NC1=CC=C([N+]([O-])=O)C=C1)=O)=O)=O

InChI

1S/C23H38N8O5.2C2H4O2/c1-13(2)12-18(30-22(34)19(24)14(3)4)21(33)29-17(6-5-11-27-23(25)26)20(32)28-15-7-9-16(10-8-15)31(35)36;2*1-2(3)4/h7-10,13-14,17-19H,5-6,11-12,24H2,1-4H3,(H,28,32)(H,29,33)(H,30,34)(H4,25,26,27);2*1H3,(H,3,4)/t17-,18-,19+;;/m0../s1

InChI key

WGVZWNUZAXIGKU-HYKWBEMSSA-N

Amino Acid Sequence

Val-Leu-Arg-pNA

Application

D-Val-Leu-Arg p-nitroanilide diacetate salt has been used as a substrate to determine the amidolytic activity of the fibrinolytic enzyme from Bacillus subtilis DC33. It has also been used as a substrate to determine the activity of fibrinolytic enzymes from the earthworm Eisenia fetida.

Packaging

Bottomless glass bottle. Contents are inside inserted fused cone.

Quality

Salt content will vary.

Pictograms

Health hazard

Signal Word

Warning

Hazard Statements

Hazard Classifications

Repr. 2

Storage Class Code

11 - Combustible Solids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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T L Miranda et al.
Brazilian journal of medical and biological research = Revista brasileira de pesquisas medicas e biologicas, 28(5), 505-512 (1995-05-01)
Hydrolysis of D-valyl-L-leucyl-L-arginine p-nitroanilide (D-Val-Leu-Arg-Nan) at five different concentrations (10-20 microM) by human urinary kallikrein was studied in the absence and in the presence of increasing concentrations of basic pancreatic trypsin inhibitor (BPTI) (1.35-9.15 nM). The data indicate that the
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Hydrolysis of seven N alpha-substituted L-arginine 4-nitroanilides: benzoyl-arginine p-nitroanilide (Bz-Arg-Nan), tosyl-arginine p-nitroanilide (Tos-Arg-Nan), acetyl-leucyl-arginine p-nitroanilide (Ac-Leu-Arg-Nan), acetyl-phenylalanyl-arginine p-nitroanilide (Ac-Phe-Arg-Nan), benzoyl-phenylalanyl-arginine p-nitroanilide (Bz-Phe-Arg-Nan), tosyl-phenylalanyl-arginine p-nitroanilide (Tos-Phe-Arg-Nan), and D-valyl-leucyl-arginine p-nitroanilide (D-Val-Leu-Arg-Nan), and the N alpha-substituted L-arginine ester: benzoyl-arginine ethyl ester (Bz-Arg-OEt), by
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Mannose-binding lectin (MBL)-associated serine protease (MASP)-1 is an abundant component of the lectin pathway of complement. The related enzyme, MASP-2 is capable of activating the complement cascade alone. Though the concentration of MASP-1 far exceeds that of MASP-2, only a

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