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T1660

Sigma-Aldrich

Nε,Nε,Nε-Trimethyllysine hydrochloride

≥97% (TLC)

Sinónimos:

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

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About This Item

Fórmula empírica (notación de Hill):
C9H20N2O2 · HCl
Número de CAS:
55528-53-5
Peso molecular:
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

Categorías relacionadas

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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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
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)
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
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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