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T1660

Sigma-Aldrich

Nε,Nε,Nε-Trimethyllysine hydrochloride

≥97% (TLC)

Synonym(s):

1-Pentanaminium, 5-amino-5-carboxy-N,N,N-trimethyl-, chloride (1:1), (5S)-

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About This Item

Empirical Formula (Hill Notation):
C9H20N2O2 · HCl
CAS Number:
Molecular Weight:
224.73
MDL number:
UNSPSC Code:
12352202
PubChem Substance ID:
NACRES:
NA.26

Assay

≥97% (TLC)

form

powder

contains

salts and water as balance

composition

Amino acid content, ~75%

technique(s)

LC/MS: suitable

color

white

storage temp.

−20°C

SMILES string

[Cl-].C[N+](C)(C)CCCC[C@H](N)C(O)=O

InChI

1S/C9H20N2O2.ClH/c1-11(2,3)7-5-4-6-8(10)9(12)13;/h8H,4-7,10H2,1-3H3;1H/t8-;/m0./s1

InChI key

ZKIJKCHCMFGMCM-QRPNPIFTSA-N

Storage Class Code

11 - Combustible Solids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

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Sara P Gaucher et al.
Journal of proteome research, 7(6), 2320-2331 (2008-04-18)
Recent developments in shotgun proteomics have enabled high-throughput studies of a variety of microorganisms at a proteome level and provide experimental validation for predicted open reading frames in the corresponding genome. More importantly, advances in mass spectrometric data analysis now
Andrew J Bannister et al.
The Journal of biological chemistry, 280(18), 17732-17736 (2005-03-12)
Methylation of lysine 4 of histone H3 (K4/H3) is linked to transcriptional activity, whereas methylation of K9/H3 is tightly associated with gene inactivity. These are well characterized sites of methylation within histones, but there are numerous other, less characterized, sites
Lynnette M A Dirk et al.
Biochemistry, 46(12), 3905-3915 (2007-03-07)
Processive versus distributive methyl group transfer was assessed for pea Rubisco large subunit methyltransferase, a SET domain protein lysine methyltransferase catalyzing the formation of trimethyllysine-14 in the large subunit of Rubisco. Catalytically competent complexes between an immobilized form of des(methyl)
Naomi van Vlies et al.
Analytical biochemistry, 354(1), 132-139 (2006-05-19)
Although the mouse frequently is used to study metabolism and deficiencies therein, little is known about carnitine biosynthesis in this animal. To this point, only laborious procedures have been described to measure the activity of carnitine biosynthesis enzymes using subcellular
Naomi van Vlies et al.
The FEBS journal, 274(22), 5845-5851 (2007-10-20)
The first enzyme of carnitine biosynthesis is the mitochondrial 6-N-trimethyllysine dioxygenase, which converts 6-N-trimethyllysine to 3-hydroxy-6-N-trimethyllysine. Using progressive membrane solubilization with digitonin and protease protection experiments, we show that this enzyme is localized in the mitochondrial matrix. Latency experiments with

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