04685
Nε-Methyl-L-lysine hydrochloride
≥98.0% (TLC)
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About This Item
Fórmula empírica (notación de Hill):
C7H16N2O2 · HCl
Número de CAS:
Peso molecular:
196.68
EC Number:
MDL number:
UNSPSC Code:
12352202
PubChem Substance ID:
NACRES:
NA.32
assay:
≥98.0% (TLC)
Productos recomendados
Quality Level
assay
≥98.0% (TLC)
optical activity
[α]/D 20.5±1.5°, c = 0.1 in 1 M HCl
storage temp.
2-8°C
SMILES string
Cl.CNCCCC[C@H](N)C(O)=O
Cl.CNCCCC[C@H](N)C(O)=O
InChI
1S/C7H16N2O2.ClH/c1-9-5-3-2-4-6(8)7(10)11;/h6,9H,2-5,8H2,1H3,(H,10,11);1H/t6-;/m0./s1
InChI key
AQELUQTVJOFFBN-RGMNGODLSA-N
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Biochem/physiol Actions
N ε-methyl-L-lysine was identified as a lysine analog with inhibitory effects on the growth and sporulation of Penicillium chrysogenum and benzyl-penicillin formation by mycelia.
Packaging
Bottomless glass bottle. Contents are inside inserted fused cone.
Storage Class
11 - Combustible Solids
wgk_germany
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
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Los clientes también vieron
Agnes M Móricz et al.
Natural product communications, 6(5), 657-660 (2011-05-28)
The influence of monomethylated basic amino acids [NG-monomethyl-L-arginine (MMA) and Nepsilon-monomethyl-L-lysine (MML)] and ozone capturers (indigo carmine, d-limonene) on the antibacterial effect of the mycotoxins aflatoxins B1, B2, G1 and G2 was studied in BioArena, which is a complex bioautographic
C A Regenstreif et al.
Canadian journal of microbiology, 32(6), 522-524 (1986-06-01)
alpha-Methyl lysine was investigated as a potential inhibitor of lysine transport in Escherichia coli and Bacillus sphaericus. At equimolar concentrations, no inhibition was observed in either organism, but at 10X and 100X the lysine concentration, alpha-methyl lysine caused a 20-50%
Methylated lysines and 3-methylhistidine in myosin: tissue and developmental differences.
G Huszar
Methods in enzymology, 106, 287-295 (1984-01-01)
Duy P Nguyen et al.
Journal of the American Chemical Society, 131(40), 14194-14195 (2009-09-24)
Lysine methylation is an important post-translational modification of histone proteins that defines epigenetic status and controls heterochromatin formation, X-chromosome inactivation, genome imprinting, DNA repair, and transcriptional regulation. Despite considerable efforts by chemical biologists to synthesize modified histones for use in
B Maras et al.
European journal of biochemistry, 203(1-2), 81-87 (1992-01-15)
The complete amino acid sequence of glutamate dehydrogenase from the thermoacidophilic archaebacterium Sulfolobus solfataricus has been determined. The sequence was reconstructed by automated sequence analysis of peptides obtained after cleavage by trypsin, cyanogen bromide, Staphylococcus aureus V8 protease and pepsin.
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