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Merck
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重要文件

A4377

Sigma-Aldrich

S-(5′-腺苷)-L-甲硫氨酸碘盐

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

同義詞:

AdoMet, SAM

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About This Item

經驗公式(希爾表示法):
C15H23IN6O5S
CAS號碼:
分子量::
526.35
Beilstein:
4120787
EC號碼:
MDL號碼:
分類程式碼代碼:
12352209
PubChem物質ID:
NACRES:
NA.26

產品名稱

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

品質等級

化驗

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

形狀

powder

技術

cell culture | mammalian: suitable

顏色

white to off-white

溶解度

H2O: 100 mg/mL

運輸包裝

dry ice

儲存溫度

−20°C

SMILES 字串

[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 密鑰

XQMWYLXPEGFCFT-XKGORWRGSA-N

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應用

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。

注意

该材料在室温下非常不稳定。

分析報告

通过UV和HPLC进行纯化。

象形圖

Exclamation mark

訊號詞

Warning

危險聲明

危險分類

Skin Sens. 1

儲存類別代碼

11 - Combustible Solids

水污染物質分類(WGK)

WGK 3

閃點(°F)

Not applicable

閃點(°C)

Not applicable

個人防護裝備

Eyeshields, Faceshields, Gloves, type N95 (US)


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分析證明 (COA)

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存取文件庫

Jianyu Zhang et al.
Journal of the American Chemical Society, 133(43), 17134-17137 (2011-10-01)
Human catechol-O-methyltransferase (COMT) catalyzes a methyl transfer from S-adenosylmethionine (AdoMet) to dopamine. Site-specific mutants at three positions (Tyr68, Trp38, and Val108) have been characterized with regard to product distribution, catalytic efficiency, and secondary kinetic isotope effects. The series of mutations
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
Renata Z Jurkowska et al.
Methods in molecular biology (Clifton, N.J.), 791, 157-177 (2011-09-14)
DNA methyltransferases are important enzymes and their inhibition has many potential applications. The investigation of DNA methyltransferases as well as screening for potential inhibitors requires specialized enzyme assays. In this chapter, we describe three DNA methyltransferase assays, each of them
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

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