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485-80-3 Usage

Veterinary Drugs and Treatments

In small animal medicine, SAMe is most commonly used as an adjunctive treatment for liver disease (chronic hepatitis, hepatic lipidosis, cholangiohepatitis, feline triad disease, etc.). It may also be of benefit in osteoarthritis, treatment of acute hepatotoxin-induced liver toxicity (e.g., acetaminophen toxicity), and at-risk patients on long-term therapy using drugs with hepatotoxic potential. In humans, SAMe is being used as a treatment for depression, osteoarthritis, AIDS-related myopathy, intrahepatic cholestasis, liver disease, alcoholic liver cirrhosis, fibromyalgia, adult ADHD, Alzheimer’s, migraines, etc.

Check Digit Verification of cas no

The CAS Registry Mumber 485-80-3 includes 6 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 3 digits, 4,8 and 5 respectively; the second part has 2 digits, 8 and 0 respectively.
Calculate Digit Verification of CAS Registry Number 485-80:
83 % 10 = 3
So 485-80-3 is a valid CAS Registry Number.



According to Globally Harmonized System of Classification and Labelling of Chemicals (GHS) - Sixth revised edition

Version: 1.0

Creation Date: Aug 20, 2017

Revision Date: Aug 20, 2017


1.1 GHS Product identifier

Product name 13CH3-SAM

1.2 Other means of identification

Product number -
Other names S-adenosylmethionine

1.3 Recommended use of the chemical and restrictions on use

Identified uses For industry use only.
Uses advised against no data available

1.4 Supplier's details

1.5 Emergency phone number

Emergency phone number -
Service hours Monday to Friday, 9am-5pm (Standard time zone: UTC/GMT +8 hours).

More Details:485-80-3 SDS

485-80-3Relevant articles and documents

Directed Evolution of a Halide Methyltransferase Enables Biocatalytic Synthesis of Diverse SAM Analogs

Tang, Qingyun,Grathwol, Christoph W.,Aslan-üzel, A?k?n S.,Wu, Shuke,Link, Andreas,Pavlidis, Ioannis V.,Badenhorst, Christoffel P. S.,Bornscheuer, Uwe T.

supporting information, p. 1524 - 1527 (2020/11/30)

Biocatalytic alkylations are important reactions to obtain chemo-, regio- and stereoselectively alkylated compounds. This can be achieved using S-adenosyl-l-methionine (SAM)-dependent methyltransferases and SAM analogs. It was recently shown that a halide methyltransferase (HMT) from Chloracidobacterium thermophilum can synthesize SAM from SAH and methyl iodide. We developed an iodide-based assay for the directed evolution of an HMT from Arabidopsis thaliana and used it to identify a V140T variant that can also accept ethyl-, propyl-, and allyl iodide to produce the corresponding SAM analogs (90, 50, and 70 % conversion of 15 mg SAH). The V140T AtHMT was used in one-pot cascades with O-methyltransferases (IeOMT or COMT) to achieve the regioselective ethylation of luteolin and allylation of 3,4-dihydroxybenzaldehyde. While a cascade for the propylation of 3,4-dihydroxybenzaldehyde gave low conversion, the propyl-SAH intermediate could be confirmed by NMR spectroscopy.

Preparation, Assay, and Application of Chlorinase SalL for the Chemoenzymatic Synthesis of S-Adenosyl-L-Methionine and Analogs

Davis, Tony D.,Kunakom, Sylvia,Burkart, Michael D.,Eustaquio, Alessandra S.

, p. 367 - 388 (2018/06/16)

S-adenosyl-L-methionine (SAM) is universal in biology, serving as the second most common cofactor in a variety of enzymatic reactions. One of the main roles of SAM is the methylation of nucleic acids, proteins, and metabolites. Methylation often imparts regulatory control to DNA and proteins, and leads to an increase in the activity of specialized metabolites such as those developed as pharmaceuticals. There has been increased interest in using SAM analogs in methyltransferase-catalyzed modification of biomolecules. However, SAM and its analogs are expensive and unstable, degrading rapidly under physiological conditions. Thus, the availability of methods to prepare SAM in situ is desirable. In addition, synthetic methods to generate SAM analogs suffer from low yields and poor diastereoselectivity. The chlorinase SalL from the marine bacterium Salinispora tropica catalyzes the reversible, nucleophilic attack of chloride at the C5′ ribosyl carbon of SAM leading to the formation of 5′-chloro-5′-deoxyadenosine (ClDA) with concomitant displacement of L-methionine. It has been demonstrated that the in vitro equilibrium of the SalL-catalyzed reaction favors the synthesis of SAM. In this chapter, we describe methods for the preparation of SalL, and the chemoenzymatic synthesis of SAM and SAM analogs from ClDA and L-methionine congeners using SalL. In addition, we describe procedures for the in situ chemoenzymatic synthesis of SAM coupled to DNA, peptide, and metabolite methylation, and to the incorporation of isotopes into alkylated products.

A general NMR-based strategy for the in Situ characterization of sugar-nucleotide-dependent biosynthetic pathways

Singh, Shanteri,Peltier-Pain, Pauline,Tonelli, Marco,Thorson, Jon S.

supporting information, p. 3220 - 3223 (2014/07/08)

A simple method for the study of sugar-nucleotide-dependent multienzyme cascades is highlighted where the use of selectively 13C-labeled sugar nucleotides and inverse 13C detection NMR offers fast, direct detection and quantification of reactants and products and circumvents the need for chromatographic separation. The utility of the method has been demonstrated by characterizing four previously uncharacterized sugar nucleotide biosynthetic enzymes involved in calicheamicin biosynthesis.

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