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A4021

Sigma-Aldrich

Nε-Acetyl-L-lysine

Nε-Acetyl-L-lysine

≥98% (TLC)

Synonym(s):

N6-acetyl-L-lysine

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$359.00

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1 G
$108.29
5 G
$359.00

About This Item

Linear Formula:
CH3CONH(CH2)4CH(NH2)CO2H
CAS Number:
692-04-6
Molecular Weight:
188.22
EC Number:
211-725-9
MDL number:
MFCD00002639
UNSPSC Code:
12352209
PubChem Substance ID:
24890737
NACRES:
NA.26

$108.29

List Price$119.00Save 9%
Web-Only Promotion

Available to ship onMay 01, 2025Details

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Product Name

Nε-Acetyl-L-lysine,

assay

≥98% (TLC)

form

powder

concentration

50 mg/mL in 80% acetic acid

color

colorless to white

mp

250 °C (dec.) (lit.)

storage temp.

−20°C

SMILES string

CC(=O)NCCCC[C@H](N)C(O)=O

InChI

1S/C8H16N2O3/c1-6(11)10-5-3-2-4-7(9)8(12)13/h7H,2-5,9H2,1H3,(H,10,11)(H,12,13)/t7-/m0/s1

InChI key

DTERQYGMUDWYAZ-ZETCQYMHSA-N

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Related Categories

Application


  • Nε-Acetyl L-α Lysine Improves Activity and Stability of α-Amylase at Acidic Conditions: A Comparative Study with other Osmolytes. This study highlights the use of Nε-Acetyl-ʟ-lysine in enhancing the functional stability and activity of α-amylase under acidic conditions, demonstrating its potential as a valuable additive in industrial enzyme applications (Joghee et al., 2020).

Biochem/physiol Actions

Nε-Acetyl-L-lysine (L-AcK) is an R-chain N-acetylated α amino acid used together with other lysine analogues to differentiate and characterized various aminoacylases and regulator 2 (Sir2) enzymes/sirtuins.

Storage Class

11 - Combustible Solids

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

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Certificates of Analysis (COA)

Lot/Batch Number
BCCM7176
BCCL9812
BCCK2331
BCCJ0164
BCCF1097

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S L Hazen et al.
The Journal of biological chemistry, 272(27), 16990-16998 (1997-07-04)
Activated human phagocytes employ the myeloperoxidase-H2O2-Cl- system to convert L-tyrosine to p-hydroxyphenylacetaldehyde (pHA). We have explored the possibility that pHA covalently reacts with proteins to form Schiff base adducts, which may play a role in modifying targets at sites of
C Crane-Robinson et al.
Methods (San Diego, Calif.), 12(1), 48-56 (1997-05-01)
Acetylation of specific lysine residues in the N-terminal domains of core histones is a biochemical marker of active genes. To determine the spatial and temporal distribution of this reversible posttranslational modification, affinity-purified polyclonal antibodies recognizing the epitope epsilon-acetyllysine have been
Brian E Schultz et al.
Biochemistry, 43(34), 11083-11091 (2004-08-25)
Histone deacetylase (HDAC) enzymes modulate gene expression through the deacetylation of acetylated lysine residues on histone proteins. They operate in biological systems as part of multiprotein corepressor complexes. To understand the reactivity of isolated HDACs and the contribution of cofactor
K Hoffmann et al.
Die Pharmazie, 55(8), 601-606 (2000-09-16)
Inhibitors of histone deacetylase (HD) are of great potential as new drugs due to their ability to influence transcriptional regulation and to induce apoptosis or differentiation in cancer cells. So far only radioactive enzyme activity assays or in-vivo assays with
T Henle et al.
Zeitschrift fur Lebensmittel-Untersuchung und -Forschung, 198(1), 66-67 (1994-01-01)
After heating N alpha-acetyllysine and glucose for 4 h at 90 degrees C in the dry state and subsequent acid hydrolysis with 7.8 N HCl, preparative fractionation of the dihydrochlorides of furosine and pyridosine was achieved by cation-exchange chromatography. The
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