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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

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Quality Level

200

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

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This Item
14580C320542602
Nε,Nε,Nε-Trimethyllysine hydrochloride ≥97% (TLC)

Sigma-Aldrich

T1660

Nε,Nε,Nε-Trimethyllysine hydrochloride

Nα,Nα-Bis(carboxymethyl)-L-lysine hydrate ≥97.0% (TLC)

Sigma-Aldrich

14580

Nα,Nα-Bis(carboxymethyl)-L-lysine hydrate

Nα,Nα-Bis(carboxymethyl)-L-lysine trifluoroacetate salt ≥95% (TLC)

Sigma-Aldrich

C3205

Nα,Nα-Bis(carboxymethyl)-L-lysine trifluoroacetate salt

Propionyl-L-carnitine ≥94.0% (HPLC)

Sigma-Aldrich

42602

Propionyl-L-carnitine

form

powder

form

powder

form

powder

form

powder or crystals

technique(s)

LC/MS: suitable

technique(s)

-

technique(s)

-

technique(s)

LC/MS: suitable

assay

≥97% (TLC)

assay

≥97.0% (TLC)

assay

≥95% (TLC)

assay

≥94.0% (HPLC)

storage temp.

−20°C

storage temp.

-

storage temp.

2-8°C

storage temp.

2-8°C

color

white

color

-

color

white

color

white to off-white

Quality Level

200

Quality Level

100

Quality Level

200

Quality Level

100

Storage Class

11 - Combustible Solids

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)

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Certificates of Analysis (COA)

Lot/Batch Number
BCCM9624
BCCM7523
BCCM4026
BCCM0014
BCCK0582

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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
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
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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