T1660
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
NACRES:
NA.26
PubChem Substance ID:
UNSPSC Code:
12352202
MDL number:
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
SMILES string
[Cl-].C[N+](C)(C)CCCC[C@H](N)C(O)=O
InChI key
ZKIJKCHCMFGMCM-QRPNPIFTSA-N
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
Quality Level
Related Categories
Storage Class
11 - Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
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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
Lei Xiong et al.
Journal of the American Society for Mass Spectrometry, 20(6), 1172-1181 (2009-03-24)
Core histones are susceptible to a range of post-translational modifications (PTMs), including acetylation, phosphorylation, methylation, and ubiquitination, which play important roles in the epigenetic control of gene expression. Here, we observed an unusual discrepancy between MALDI-MS/MS and ESI-MS/MS on the
Yasunori Tokuda et al.
Journal of bioscience and bioengineering, 111(4), 402-407 (2011-01-11)
The preparation of posttranslationally modified proteins is required to investigate the function and structure of modified proteins. However, homogeneously modified proteins are not easily isolated from natural sources or prepared using modification enzymes. Non-natural amino acid mutagenesis has enabled us
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