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Key Documents

Ursprungszeugnis (CoO)/Analysenzertifikate (CoA)

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A4021

N_ε-Acetyl-L-lysin

Name: <I>N</I><SUB>ε</SUB>-Acetyl-<SC>L</SC>-lysin
Brand: SIGMA

≥98% (TLC)

Synonym(e):

N⁶-acetyl-L-lysine

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About This Item

Lineare Formel:

CH₃CONH(CH₂)₄CH(NH₂)CO₂H

CAS-Nummer:

692-04-6

Molekulargewicht:

188.22

EG-Nummer:

211-725-9

MDL-Nummer:

MFCD00002639

UNSPSC-Code:

12352209

PubChem Substanz-ID:

24890737

NACRES:

NA.26

Empfohlene Produkte

Slide 1 of 10

1 of 10

Sigma-Aldrich

A2010

N_α-Acetyl-L-lysin

Sigma-Aldrich

A9125

N_α-Acetyl-L-glutamin

Sigma-Aldrich

L5501

L-Lysin

Sigma-Aldrich

855642

N-Acetyl-L-glutaminsäure

S460184

N-ACETYL-L-GLUTAMINE

Sigma-Aldrich

T1660

Nε,Nε,Nε-Trimethyllysine hydrochloride

Sigma-Aldrich

A3133

N_α-Acetyl-L-arginin

Sigma-Aldrich

A3626

N_α-Acetyl-L-ornithin

Sigma-Aldrich

T0625

Taurin

Sigma-Aldrich

359688

Boc-Lys-OH

product name

N_ε-Acetyl-L-lysin,

Assay

≥98% (TLC)

Form

powder

Konzentration

50 mg/mL in 80% acetic acid

Farbe

colorless to white

mp (Schmelzpunkt)

250 °C (dec.) (lit.)

Lagertemp.

−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

InChIKey

DTERQYGMUDWYAZ-ZETCQYMHSA-N

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Anwendung

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. Wirkung

Nε-Acetyl-L-lysin (L-AcK) ist eine R-Ketten-N-acetylierte α-Aminosäure, die zusammen mit anderen Lysinanaloga zum Differenzieren und Charakterisieren von verschiedenen Aminoacylasen sowie Regulator-2-Enzymen (Sir2)/Sirtuinen eingesetzt wird.

Lagerklassenschlüssel

11 - Combustible Solids

WGK

WGK 3

Flammpunkt (°F)

Not applicable

Flammpunkt (°C)

Not applicable

Analysenzertifikate (COA)

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Slide 1 of 4

1 of 4

Sigma-Aldrich

A3133

N_α-Acetyl-L-arginin

Sigma-Aldrich

D4268

N^G,N^G-Dimethylarginine dihydrochloride

Sigma-Aldrich

A4625

N-Acetyl-L-alanine

Sigma-Aldrich

M7033

N_ω-Methyl-L-arginin -acetat (Salz)

Transition state of ADP-ribosylation of acetyllysine catalyzed by Archaeoglobus fulgidus Sir2 determined by kinetic isotope effects and computational approaches.

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

Chemical characterization of a protein-4-hydroxy-2-nonenal cross-link: immunochemical detection in mitochondria exposed to oxidative stress.

J A Cohn et al.

Archives of biochemistry and biophysics, 328(1), 158-164 (1996-04-01)

We have previously shown that incubation of the model protein glucose-6-phosphate dehydrogenase (Glu-6-PDH) from the bacterium Leuconostoc mesenteroides with 4-hydroxy-2-nonenal (HNE), a major product of lipid peroxidation, results in the formation of cross-linked protein. HNE-modified protein is resistant to proteolytic

Plasmodium falciparum Sir2 is an NAD+-dependent deacetylase and an acetyllysine-dependent and acetyllysine-independent NAD+ glycohydrolase.

Jarrod B French et al.

Biochemistry, 47(38), 10227-10239 (2008-08-30)

Sirtuins are NAD (+)-dependent enzymes that deacetylate a variety of cellular proteins and in some cases catalyze protein ADP-ribosyl transfer. The catalytic mechanism of deacetylation is proposed to involve an ADPR-peptidylimidate, whereas the mechanism of ADP-ribosyl transfer to proteins is

Human neutrophils employ the myeloperoxidase-hydrogen peroxide-chloride system to oxidize alpha-amino acids to a family of reactive aldehydes. Mechanistic studies identifying labile intermediates along the reaction pathway.

S L Hazen et al.

The Journal of biological chemistry, 273(9), 4997-5005 (1998-03-28)

We have recently demonstrated that neutrophils oxidize nearly all of the amino acids commonly found in plasma to a corresponding family of aldehydes in high yield. The reaction is mediated by hypochlorous acid (HOCl), the major oxidant generated by the

Generation of antibodies to Di- and trichloroacetylated proteins and immunochemical detection of protein adducts in rats treated with perchloroethene.

A Pähler et al.

Chemical research in toxicology, 11(9), 995-1004 (1998-10-07)

Antibodies directed against chemical specific protein modifications are valuable tools to detect and comparatively quantify protein modifications. Both Nepsilon-(dichloroacetyl)-L-lysine and Nepsilon-(trichloroacety)l-L-lysine have been detected as modified amino acids in liver and kidneys of rats treated with perchloroethene (PER) after proteolysis.

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Key Documents

N_ε-Acetyl-L-lysin

≥98% (TLC)

About This Item

Empfohlene Produkte

Eigenschaften

product name

Assay

Form

Konzentration

Farbe

mp (Schmelzpunkt)

Lagertemp.

SMILES String

InChI

InChIKey

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Beschreibung

Anwendung

Biochem./physiol. Wirkung

Sicherheitshinweise

Lagerklassenschlüssel

WGK

Flammpunkt (°F)

Flammpunkt (°C)

Dokumentation

Analysenzertifikate (COA)

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