Skip to Content
MilliporeSigma
All Photos(3)

Documents

A4377

Sigma-Aldrich

S-(5′-Adenosyl)-L-methionine iodide

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

Synonym(s):

AdoMet, SAM

Sign Into View Organizational & Contract Pricing
All Photos(3)

About This Item

Empirical Formula (Hill Notation):
C15H23IN6O5S
CAS Number:
3493-13-8
Molecular Weight:
526.35
Beilstein/REAXYS Number:
4120787
EC Number:
222-486-5
MDL number:
MFCD00043192
UNSPSC Code:
12352209
PubChem Substance ID:
24890852
NACRES:
NA.26

product name

S-(5′-Adenosyl)-L-methionine iodide, ≥80% (HPLC), ≥80% (spectrophotometric assay)

assay

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

form

powder

technique(s)

cell culture | mammalian: suitable

color

white to off-white

solubility

H2O: 100 mg/mL

shipped in

dry ice

storage temp.

−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

Looking for similar products? Visit Product Comparison Guide

Application

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.

Biochem/physiol Actions

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.

Caution

This material is very unstable at room temperature.

Analysis Note

Purity based on UV and HPLC.

pictograms

Exclamation mark
GHS07

signalword

Warning

hcodes

H317

Hazard Classifications

Skin Sens. 1

Storage Class

11 - Combustible Solids

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Faceshields, Gloves, type N95 (US)

Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

Already Own This Product?

Find documentation for the products that you have recently purchased in the Document Library.

Visit the Document Library

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
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
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
View All Related Papers

Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.

Contact Technical Service