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M3529

Sigma-Aldrich

L-Methionine p-nitroanilide

≥98% (TLC), suitable for ligand binding assays

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About This Item

Empirical Formula (Hill Notation):
C11H15N3O3S
CAS Number:
6042-04-2
Molecular Weight:
269.32
MDL number:
MFCD00063424
UNSPSC Code:
12352209
PubChem Substance ID:
24896851
NACRES:
NA.26

product name

L-Methionine p-nitroanilide,

Assay

≥98% (TLC)

form

powder

technique(s)

ligand binding assay: suitable

color

white to faint yellow

storage temp.

−20°C

SMILES string

CSCC[C@H](N)C(=O)Nc1ccc(cc1)[N+]([O-])=O

InChI

1S/C11H15N3O3S/c1-18-7-6-10(12)11(15)13-8-2-4-9(5-3-8)14(16)17/h2-5,10H,6-7,12H2,1H3,(H,13,15)/t10-/m0/s1

InChI key

PLBWRAWSHVJPTL-JTQLQIEISA-N

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Biochem/physiol Actions

L-Methionine p-nitroanilide is a hMetAP2 substrate.

Storage Class Code

11 - Combustible Solids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

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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Sanghamitra Mitra et al.
Analytical biochemistry, 357(1), 43-49 (2006-07-18)
A direct and convenient spectrophotometric assay has been developed for methionine aminopeptidases (MetAPs). The method employs the hydrolysis of a substrate that is a methionyl analogue of p-nitroaniline (L-Met-p-NA), which releases the chromogenic product p-nitroaniline. This chromogenic product can be
R A Cowman et al.
Journal of dental research, 70(12), 1508-1515 (1991-12-01)
Intact cells of Streptococcus sanguis ATCC 10556 possessed arylaminopeptidases exhibiting activity toward the nitroanilide (NA) derivatives of leucine, alanine, methionine, arginine, or lysine. Weak hydrolytic activity was observed in assays with the NA derivatives of valine, proline, glycine, or glutamic
G Yang et al.
Biochemistry, 40(35), 10645-10654 (2001-08-29)
The steady-state kinetics of a full-length and truncated form of the type 2 human methionine aminopeptidase (hMetAP2) were analyzed by continuous monitoring of the amide bond cleavage of various peptide substrates and methionyl analogues of 7-amido-4-methylcoumarin (AMC) and p-nitroaniline (pNA)

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