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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:
55528-53-5
Molecular Weight:
224.73
MDL number:
MFCD06795777
UNSPSC Code:
12352202
PubChem Substance ID:
24899984
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

Related Categories

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

Certificates of Analysis (COA)

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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
C J Rebouche et al.
The Journal of nutrition, 116(5), 751-759 (1986-05-01)
Rates of carnitine biosynthesis in mammals depend on the availability of substrates and the activity of enzymes subserving the pathway. This study was undertaken to test the hypothesis that the availability of epsilon-N-trimethyllysine is rate-limiting for synthesis of carnitine in
Jean-François Couture et al.
The Journal of biological chemistry, 281(28), 19280-19287 (2006-05-10)
SET domain enzymes represent a distinct family of protein lysine methyltransferases in eukaryotes. Recent studies have yielded significant insights into the structural basis of substrate recognition and the product specificities of these enzymes. However, the mechanism by which SET domain
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)
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