A4377
S-(5′-Adenosyl)-L-methionine iodide
≥80% (spectrophotometric assay), suitable for cell culture
동의어(들):
AdoMet, SAM
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모든 사진(3)
About This Item
실험식(Hill 표기법):
C15H23IN6O5S
CAS Number:
Molecular Weight:
526.35
Beilstein:
4120787
EC Number:
MDL number:
UNSPSC 코드:
12352209
PubChem Substance ID:
NACRES:
NA.26
추천 제품
제품명
S-(5′-Adenosyl)-L-methionine iodide, ≥80% (HPLC), ≥80% (spectrophotometric assay)
Quality Level
분석
≥80% (HPLC)
≥80% (spectrophotometric assay)
양식
powder
기술
cell culture | mammalian: suitable
색상
white to off-white
solubility
H2O: 100 mg/mL
배송 상태
dry ice
저장 온도
−20°C
SMILES string
[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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애플리케이션
S-(5′-Adenosyl)-L-methionine (SAM, AdoMet) is used as a primary methyl donor molecule in mammalian cell culture and the first step metabolite in methionine biosynthesis.
생화학적/생리학적 작용
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.
주의사항
This material is very unstable at room temperature.
분석 메모
Purity based on UV and HPLC.
신호어
Warning
유해 및 위험 성명서
Hazard Classifications
Skin Sens. 1
Storage Class Code
11 - Combustible Solids
WGK
WGK 3
Flash Point (°F)
Not applicable
Flash Point (°C)
Not applicable
개인 보호 장비
Eyeshields, Faceshields, Gloves, type N95 (US)
가장 최신 버전 중 하나를 선택하세요:
시험 성적서(COA)
Lot/Batch Number
이미 열람한 고객
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
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
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
Yui Yamashita et al.
The Journal of biological chemistry, 289(18), 12693-12704 (2014-03-22)
Expression of CGS1, which codes for an enzyme of methionine biosynthesis, is feedback-regulated by mRNA degradation in response to S-adenosyl-L-methionine (AdoMet). In vitro studies revealed that AdoMet induces translation arrest at Ser-94, upon which several ribosomes stack behind the arrested
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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