A4021
Nε-Acetyl-L-lysine
≥98% (TLC)
Synonym(s):
N6-acetyl-L-lysine
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About This Item
Linear Formula:
CH3CONH(CH2)4CH(NH2)CO2H
CAS Number:
Molecular Weight:
188.22
EC Number:
MDL number:
UNSPSC Code:
12352209
PubChem Substance ID:
NACRES:
NA.26
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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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 Code
11 - Combustible Solids
WGK
WGK 3
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
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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
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
Yana Cen et al.
Journal of the American Chemical Society, 132(35), 12286-12298 (2010-08-20)
Sirtuins are protein-modifying enzymes distributed throughout all forms of life. These enzymes bind NAD(+), a universal metabolite, and react it with acetyllysine residues to effect deacetylation of protein side chains. This NAD(+)-dependent deacetylation reaction has been observed for sirtuin enzymes
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