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D7254

DNP-L-alanine

Name: DNP-<SC>L</SC>-alanine
Brand: SIGMA

Synonym(s):

N-(2,4-Dinitrophenyl)-L-alanine

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About This Item

Empirical Formula (Hill Notation):

C₉H₉N₃O₆

CAS Number:

1655-52-3

Molecular Weight:

255.18

UNSPSC Code:

12352200

PubChem Substance ID:

24894094

EC Number:

216-739-9

MDL number:

MFCD00038106

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storage temp.

−20°C

SMILES string

CC(Nc1ccc(cc1N(=O)=O)N(=O)=O)C(O)=O

Storage Class

13 - Non Combustible Solids

wgk

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)

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Certificates of Analysis (COA)

Lot/Batch Number

091K1573

066H3290

049F0784

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N-acetylmuramoyl-L-alanine amidase assay based on specific radioactive labeling of muropeptide L-alanine: quantitation of the enzyme activity in the autolysin deficient Bacillus subtilis 168, flaD strain.

P Margot et al.

Analytical biochemistry, 198(1), 15-18 (1991-10-01)

A sensitive and highly reproducible assay for N-acetylmuramoyl-L-alanine amidase (EC 3.5.1.28) was devised, based on specific and homogeneous L-[14C]alanine labeling of the substrate, the peptidoglycan. The method involves partial purification of both the enzyme and the substrate and monitoring the

A novel chiral microenvironmental probe at the active site of trypsin. Extrinsic cotton effects of acyl-trypsin possessing an enantiomeric pair of chromophores.

H Nakayama et al.

European journal of biochemistry, 112(2), 403-409 (1980-11-01)

p-Amidinophenyl esters of an enantiomeric pair of N-(2,4-dinitrophenyl)alanine (N2Ph-Ala) were both efficiently hydrolyzed by trypsin. The acylation and deacylation rate constants for the D-isomer are 1/2.5 of those for the L-isomer. Slow rates of deacylation of the two substrates made

Ligand binding by antibody IgE Lb4: assessment of binding site preferences using microcalorimetry, docking, and free energy simulations.

C A Sotriffer et al.

Biophysical journal, 76(6), 2966-2977 (1999-06-04)

Antibody IgE Lb4 interacts favorably with a large number of different compounds. To improve the current understanding of the structural basis of this vast cross-reactivity, the binding of three dinitrophenyl (DNP) amino acids (DNP-alanine, DNP-glycine, and DNP-serine) is investigated in

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