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제품정보 (DICE 배송 시 비용 별도)
실험식(Hill 표기법):
C15H23ClN6O5S · 2 HCl
CAS 번호:
Molecular Weight:
507.82
UNSPSC Code:
12352209
NACRES:
NA.32
PubChem Substance ID:
MDL number:
Beilstein/REAXYS Number:
6560002
Form:
powder
Assay:
≥75%
Solubility:
H2O: 100 mg/mL
Biological source:
synthetic (chemical)
Color:
white to off-white
biological source
synthetic (chemical)
Quality Level
assay
≥75%
form
powder
color
white to off-white
solubility
H2O: 100 mg/mL
application(s)
cell analysis
shipped in
dry ice
storage temp.
−20°C
SMILES string
Cl.Cl.[Cl-].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.3ClH/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);3*1H/t7-,8+,10+,11+,14+,27?;;;/m0.../s1
InChI key
KBAFOJZCBYWKPU-XQVUROGGSA-N
General description
S-(5′-Adenosyl)-L-methionine chloride dihydrochloride (SAM) facilitates the transfer of methyl groups to proteins, lipids and nucleic acids. Methionine adenosyl transferase catalyses the synthesis of SAM from methionine and adenosine triphosphate (ATP). SAM functions to regulate various cellular functions like cell division, cell death, transcription, genetic stability, oxidant/antioxidant balance and polyamine homeostasis. Therapeutically, SAM finds its application as a nutritional supplement in humans for various diseases like osteoarthritis and liver injury. SAM also regulates transsulfuration reactions by binding to the regulatory domain of key enzyme cystathionine-β-synthase (CBS).
Application
S-(5′-Adenosyl)-L-methionine chloride dihydrochloride has been used as a medium supplement for S30 cell extract. It also has been used for measuring the interaction with catechol-O-methyltransferase (COMT) by quartz crystal microbalance (QCM), surface plasmon resonance (SPR) and isothermal titration calorimetry (ITC) with supported lipid bilayers and vesicles.
Biochem/physiol Actions
Methyl donor; cofactor for enzyme-catalyzed methylations, including catechol O-methyltransferase (COMT) and DNA methyltransferases (DNMT).
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.
Analysis Note
Purity based on UV and HPLC.
Disclaimer
This material is 80-90% pure when prepared, but is very unstable. As much as 10% purity loss per day at 25 °C has been noted.
저장 등급
11 - Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
Leah C Beauchamp et al.
Journal of Alzheimer's disease : JAD, 77(4), 1705-1715 (2020-09-15)
Alterations in the methionine cycle and abnormal tau phosphorylation are implicated in many neurodegenerative diseases, including Alzheimer's disease and frontotemporal dementia. rTg4510 mice express mutant human P301L tau and are a model of tau hyperphosphorylation. The cognitive deficit seen in
Chemical communication between bacteria and cell-free gene expression systems within linear chains of emulsion droplets
Schwarz-Schilling M, et al.
Integrative Biology : Quantitative Biosciences from Nano to Macro, 8(4), 564-570 (2016)
Yan Zhang et al.
Archives of microbiology, 191(10), 773-783 (2009-09-05)
Enolase-phosphatase (E1), as an enzyme, is involved in methionine salvage pathway in many prokaryotic and eukaryotic organisms. But the identity and function of E1 in Xanthomonas oryzae pv. oryzae (Xoo) remain undetermined. Here, we report the cloning and characterization of
Andria V Rodrigues et al.
Chembiochem : a European journal of chemical biology, 21(5), 663-671 (2019-09-13)
We recently reported the discovery of phenylacetate decarboxylase (PhdB), representing one of only ten glycyl-radical-enzyme reaction types known, and a promising biotechnological tool for first-time biochemical synthesis of toluene from renewable resources. Here, we used experimental and computational data to
Ted M Lakowski et al.
Analytical biochemistry, 396(1), 158-160 (2009-09-08)
S-Adenosyl-L-homocysteine (AdoHcy) background signal in reactions with protein arginine N-methyltransferase 1 is investigated using an ultrahigh-performance liquid chromatography tandem mass spectrometry assay that measures AdoHcy. We identify three sources of AdoHcy background: enzymatic automethylation, AdoHcy contamination in commercial S-adenosyl-L-methionine (AdoMet)
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