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Merck
CN

A4377

Sigma-Aldrich

S-(5′-腺苷)-L-甲硫氨酸碘盐

≥80% (spectrophotometric assay), suitable for cell culture

别名:

AdoMet, SAM

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关于此项目

经验公式(希尔记法):
C15H23IN6O5S
化学文摘社编号:
分子量:
526.35
Beilstein:
4120787
EC 号:
MDL编号:
UNSPSC代码:
12352209
PubChem化学物质编号:
NACRES:
NA.26
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产品名称

S-(5′-腺苷)-L-甲硫氨酸碘盐, ≥80% (HPLC), ≥80% (spectrophotometric assay)

质量水平

方案

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

表单

powder

技术

cell culture | mammalian: suitable

颜色

white to off-white

溶解性

H2O: 100 mg/mL

运输

dry ice

储存温度

−20°C

SMILES字符串

[I-].C[S+](CC[C@H](N)C(O)=O)C[C@H]1O[C@H]([C@H](O)[C@@H]1O)n2cnc3c(N)ncnc23

InChI

1S/C15H22N6O5S.HI/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;/h5-8,10-11,14,22-23H,2-4,16H2,1H3,(H2-,17,18,19,24,25);1H/t7-,8+,10+,11+,14+,27?;/m0./s1

InChI key

XQMWYLXPEGFCFT-XKGORWRGSA-N

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应用

S-(5′-腺苷)-L-甲硫氨酸(SAM,AdoMet)被用作哺乳动物细胞培养物的主要甲基供体分子以及甲硫氨酸生物合成的第一步代谢物。

生化/生理作用

甲基供体;作为酶催化甲基化的辅因子,包括儿茶酚O-甲基转移酶(COMT)和DNA甲基转移酶(DNMT)。 虽然它存在于所有细胞中,但在肝脏中较为集中,85%的甲基化反应发生在肝脏。 它还参与调节肝功能、生长和对损伤的反应中。

分析说明

通过UV和HPLC进行纯化。

免责声明

该材料在室温下非常不稳定。

象形图

Exclamation mark

警示用语:

Warning

危险声明

危险分类

Skin Sens. 1

储存分类代码

11 - Combustible Solids

WGK

WGK 3

闪点(°F)

Not applicable

闪点(°C)

Not applicable

个人防护装备

Eyeshields, Faceshields, Gloves, type N95 (US)


历史批次信息供参考:

分析证书(COA)

Lot/Batch Number

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Soon Goo Lee et al.
The Journal of biological chemistry, 287(2), 1426-1434 (2011-11-26)
In the malarial parasite Plasmodium falciparum, a multifunctional phosphoethanolamine methyltransferase (PfPMT) catalyzes the methylation of phosphoethanolamine (pEA) to phosphocholine for membrane biogenesis. This pathway is also found in plant and nematodes, but PMT from these organisms use multiple methyltransferase domains
T Kakutani et al.
Nucleic acids research, 23(1), 130-137 (1995-01-11)
We have recently isolated two Arabidopsis thaliana DNA hypomethylation mutations, identifying the DDM1 locus, that cause a 70% reduction in genomic 5-methylcytosine levels [1]. Here we describe further phenotypic and biochemical characterization of the ddm1 mutants. ddm1/ddm1 homozygotes exhibited altered
Benjamin R Duffus et al.
Biochimica et biophysica acta, 1824(11), 1254-1263 (2012-01-25)
Radical S-adenosylmethionine (AdoMet) enzymes comprise a large superfamily of proteins that engage in a diverse series of biochemical transformations through generation of the highly reactive 5'-deoxyadenosyl radical intermediate. Recent advances into the biosynthesis of unique iron-sulfur (FeS)-containing cofactors such as
Laura Gomez-Santos et al.
Methods in molecular biology (Clifton, N.J.), 826, 133-149 (2011-12-15)
S-Adenosylmethionine, abbreviated as SAM, SAMe or AdoMet, is the principal methyl group donor in the mammalian cell and the first step metabolite of the methionine cycle, being synthesized by MAT (methionine adenosyltransferase) from methionine and ATP. About 60 years after
Ernst G Malygin et al.
Critical reviews in biochemistry and molecular biology, 47(2), 97-193 (2012-01-21)
The sequence-specific transfer of methyl groups from donor S-adenosyl-L-methionine (AdoMet) to certain positions of DNA-adenine or -cytosine residues by DNA methyltransferases (MTases) is a major form of epigenetic modification. It is virtually ubiquitous, except for some notable exceptions. Site-specific methylation

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