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Merck

A2408

Sigma-Aldrich

S-(5′-Adenosyl)-L-methionine p-toluenesulfonate salt

≥80% (HPLC), ≥80% (spectrophotometric assay)

Szinonimák:

AdoMet, SAM p-toluenesulfonate salt

Bejelentkezésa Szervezeti és Szerződéses árazás megtekintéséhez


About This Item

Tapasztalati képlet (Hill-képlet):
C15H23N6O5S · C7H7O3S · xC7H8O3S
CAS-szám:
Molekulatömeg:
570.64 (free base basis)
UNSPSC kód:
12352209
PubChem Substance ID:
NACRES:
NA.32

biológiai forrás

synthetic (Organic)

Minőségi szint

Teszt

≥80% (HPLC)
≥80% (spectrophotometric assay)

Forma

powder

összetétel

p-Toluenesulfonate content, 1.6-4.4 mol/mol

szín

white to off-white

oldhatóság

H2O: 100 mg/mL

kiszállítva

dry ice

tárolási hőmérséklet

−20°C

SMILES string

O=C(O[H])[C@](N([H])[H])([H])C([H])([H])C([H])([H])[S@+](C([H])([H])[H])C([H])([H])[C@@]([C@](O[H])([H])[C@@]1([H])O[H])([H])O[C@]1([H])N2C3=C(N=C2[H])C(N([H])[H])=NC([H])=N3.O=S(C4=C([H])C([H])=C(C([H])([H])[H])C([H])=C4[H])([O-])=O

InChI

1S/C15H22N6O5S.C7H8O3S/c1-27(3-2-7(16)15(24)25)4-8-10(22)11(23)14(26-8)21-6-20-9-12(17)18-5-19-13(9)21;1-6-2-4-7(5-3-6)11(8,9)10/h5-8,10-11,14,22-23H,2-4,16H2,1H3,(H2-,17,18,19,24,25);2-5H,1H3,(H,8,9,10)/t7-,8+,10+,11+,14+,27?;/m0./s1

Nemzetközi kémiai azonosító kulcs

VHPOFDUCFKOUHV-XKGORWRGSA-N

Általános leírás

S-(5′-Adenosyl)-L-methionine p-toluenesulfonate salt is used for the treatment of depression, liver cirrhosis, cholestasis and degenerative joint disease.

Alkalmazás

S-(5′-Adenosyl)-L-methionine p-toluenesulfonate salt has been used for cell proliferation assay. It has also been used for methylation assay.

Biokémiai/fiziológiai hatások

Methyl donor; cofactor for enzyme-catalyzed methylations, including catechol O-methyltransferase (COMT) and DNA methyltransferases (DNMT). Although present in all cells, it is concentrated in liver where 85% of all methylation reactions occur. It is also involved in regulating liver function, growth, and response to injury.
S-(5′-Adenosyl)-L-methionine (SAM) is anti-apoptotic in normal hepatocytes and normal colon epithelial cells but pro-apoptotic in liver human hepatocellular carcinoma (HCC), HepG2 cells and colon cancer cells.

Vigyázat

This material is unstable at room temperature.

Tárolási osztály kódja

11 - Combustible Solids

WGK

WGK 3

Lobbanási pont (F)

Not applicable

Lobbanási pont (C)

Not applicable

Egyéni védőeszköz

Eyeshields, Gloves, type N95 (US)


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Analitikai tanúsítványok (COA)

Lot/Batch Number

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Dokumentumtár megtekintése

Yang-Liu Xia et al.
Journal of chromatography. B, Analytical technologies in the biomedical and life sciences, 1157, 122333-122333 (2020-09-01)
Catechol-O-methyltransferase (COMT) is a major drug metabolizing enzyme in humans. COMT expression is directedly associated with various mental diseases and cancers due to its essential role in catalyzing metabolic inactivation of endogenous catecholamines and catechol estrogens. However, a practical method
Negative regulation of interferon-induced transmembrane protein 3 by SET7-mediated lysine monomethylation
Shan Z, et al.
The Journal of biological chemistry, 288(49), 35093-35103 (2013)
Tao Guo et al.
Cell death & disease, 12(4), 306-306 (2021-03-24)
Nonalcoholic fatty liver disease (NAFLD) has emerged globally and is associated with inflammatory signaling. The underlying mechanisms remain poorly delineated, although NAFLD has attracted considerable attention and been extensively investigated. Recent publications have determined that angiotensin II (Ang II) plays
Allison B Norvil et al.
Nucleic acids research, 48(7), 3761-3775 (2020-03-04)
We have previously shown that the highly prevalent acute myeloid leukemia (AML) mutation, Arg882His, in DNMT3A disrupts its cooperative mechanism and leads to reduced enzymatic activity, thus explaining the genomic hypomethylation in AML cells. However, the underlying cause of the
Le Thanh Mai Pham et al.
Enzyme and microbial technology, 82, 66-73 (2015-12-18)
Using bioinformatic homology search tools, this study utilized sequence phylogeny, gene organization and conserved motifs to identify members of the family of O-methyltransferases from lignin-degrading fungus Phanerochaete chrysosporium. The heterologous expression and characterization of O-methyltransferases from P. chrysosporium were studied.

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