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A2010

Sigma-Aldrich

Nα-Acetyl-L-lysine

≥98% (TLC), suitable for ligand binding assays

Synonyme(s) :

N2-acetyl-L-lysine

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About This Item

Formule linéaire :
H2N(CH2)4CH(NHCOCH3)CO2H
Numéro CAS:
Poids moléculaire :
188.22
Numéro CE :
Numéro MDL:
Code UNSPSC :
12352209
eCl@ss :
32160406
ID de substance PubChem :
Nomenclature NACRES :
NA.26

product name

Nα-Acetyl-L-lysine,

Pureté

≥98% (TLC)

Forme

powder

Technique(s)

ligand binding assay: suitable

Couleur

colorless to white

Pf

256-258 °C (dec.) (lit.)

Température de stockage

−20°C

Chaîne SMILES 

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

InChI

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

Clé InChI

VEYYWZRYIYDQJM-ZETCQYMHSA-N

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Application

Nα-Acetyl-L-lysine has been used as a substrate for lysyl oxidase for synthesis of authentic α-aminoadipic semialdehyde (AAS)-p-aminobenzoic acid (ABA). It may be used in the synthesis of amino acid adducts of 4,4′-Methylenediphenyl diisocyanate (MDI).

Actions biochimiques/physiologiques

Nα-Acetyl-L-lysine is a biologically available N-terminal capped form of the proteinogenic α amino acid L-lysine. Nα-Acetyl-L-lysine is a substrate used to study and characterize lysyl oxidase(s).

Code de la classe de stockage

11 - Combustible Solids

Classe de danger pour l'eau (WGK)

WGK 3

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable

Équipement de protection individuelle

Eyeshields, Gloves, type N95 (US)


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Consulter la Bibliothèque de documents

Yael Belo et al.
Biochimica et biophysica acta. General subjects, 1863(9), 1343-1350 (2019-06-07)
The signal transducer and activator of transcription 3 (STAT3) protein is activated by phosphorylation of a specific tyrosine residue (Tyr705) in response to various extracellular signals. STAT3 activity was also found to be regulated by acetylation of Lys685. However, the
Jing Bi et al.
Emerging microbes & infections, 7(1), 108-108 (2018-06-15)
The DosR regulon is believed to be a key factor in latency adaptation of Mycobacterium tuberculosis and is strongly induced by multiple stresses, including hypoxia. Previous studies have revealed reversible acetylation of the conserved core DNA-binding lysine residue 182 (K182)
Wenhui Ren et al.
Scientific reports, 7, 39986-39986 (2017-01-04)
As members of bromodomain and extra-terminal motif protein family, bromodomain-containing proteins regulate a wide range of biological processes including protein scaffolding, mitosis, cell cycle progression and transcriptional regulation. The function of these bromodomain proteins (Brds) in innate immune response has
Heinz Neumann et al.
Molecular cell, 36(1), 153-163 (2009-10-13)
Lysine acetylation of histones defines the epigenetic status of human embryonic stem cells and orchestrates DNA replication, chromosome condensation, transcription, telomeric silencing, and DNA repair. A detailed mechanistic explanation of these phenomena is impeded by the limited availability of homogeneously
Yoshihiro Nakamura et al.
The Journal of biological chemistry, 282(6), 4193-4201 (2006-12-07)
The BET (bromodomains and extra terminal domain) family proteins recognize acetylated chromatin through their bromodomain and act as transcriptional activators. One of the BET proteins, BRD2, associates with the transcription factor E2F, the mediator components CDK8 and TRAP220, and RNA

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