Ethyl 4-O-methylhaematommate

Ethyl 4-O-methylhaematommate

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Ethyl 4-O-methylhaematommate
Category Others
Catalog number BBF-05323
CAS 38629-37-7
Molecular Weight 238.24
Molecular Formula C12H14O5

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Description

Ethyl 4-O-methylhaematommate is a derivative of Haematomma, which is a genus of crustose lichens.

Specification

Synonyms Benzoic acid, 3-formyl-2-hydroxy-4-methoxy-6-methyl-, ethyl ester; ethyl 2-hydroxy-3-formyl-4-methoxy-6-methylbenzoate; 3-Formyl-2-hydroxy-4-methoxy-6-methylbenzoic acid ethyl ester
IUPAC Name ethyl 3-formyl-2-hydroxy-4-methoxy-6-methylbenzoate
Canonical SMILES CCOC(=O)C1=C(C(=C(C=C1C)OC)C=O)O
InChI InChI=1S/C12H14O5/c1-4-17-12(15)10-7(2)5-9(16-3)8(6-13)11(10)14/h5-6,14H,4H2,1-3H3
InChI Key YQMIEZNZSAHWLU-UHFFFAOYSA-N

Properties

Boiling Point 354.6±42.0°C at 760 mmHg
Density 1.2±0.1 g/cm3

Reference Reading

1. Copper-catalyzed N-methylation/ethylation of sulfoximines
Fan Teng, Jiang Cheng, Jin-Tao Yu Org Biomol Chem. 2015 Oct 21;13(39):9934-7. doi: 10.1039/c5ob01558h.
A protocol for the copper-catalyzed N-methylation of sulfoximines with di-tert-butyl peroxide (DTBP) was developed. This protocol has good functional group tolerance leading to N-methylated sulfoximines in moderate to good yields. Besides, N-ethylation of sulfoximines was achieved in the presence of bis(1,1-dimethylpropyl)peroxide as the ethylating agent under a standard procedure.
2. Lysine Ethylation by Histone Lysine Methyltransferases
Abbas H K Al Temimi, Michael Martin, Qingxi Meng, Danny C Lenstra, Ping Qian, Hong Guo, Elmar Weinhold, Jasmin Mecinović Chembiochem. 2020 Feb 3;21(3):392-400. doi: 10.1002/cbic.201900359. Epub 2019 Oct 24.
Biomedicinally important histone lysine methyltransferases (KMTs) catalyze the transfer of a methyl group from S-adenosylmethionine (AdoMet) cosubstrate to lysine residues in histones and other proteins. Herein, experimental and computational investigations on human KMT-catalyzed ethylation of histone peptides by using S-adenosylethionine (AdoEth) and Se-adenosylselenoethionine (AdoSeEth) cosubstrates are reported. MALDI-TOF MS experiments reveal that, unlike monomethyltransferases SETD7 and SETD8, methyltransferases G9a and G9a-like protein (GLP) do have the capacity to ethylate lysine residues in histone peptides, and that cosubstrates follow the efficiency trend AdoMet>AdoSeEth>AdoEth. G9a and GLP can also catalyze AdoSeEth-mediated ethylation of ornithine and produce histone peptides bearing lysine residues with different alkyl groups, such as H3K9meet and H3K9me2et. Molecular dynamics and free energy simulations based on quantum mechanics/molecular mechanics potential supported the experimental findings by providing an insight into the geometry and energetics of the enzymatic methyl/ethyl transfer process.
3. EMS Mutagenesis of Arabidopsis Seeds
C Stewart Gillmor, Wolfgang Lukowitz Methods Mol Biol. 2020;2122:15-23. doi: 10.1007/978-1-0716-0342-0_2.
The ethylating agent ethyl methanesulfonate (EMS) is widely used for inducing random point mutations. In Arabidopsis, treatment with EMS causes GC-to-AT transitions with great efficiency: it has been estimated that a population of 50,000 well-mutagenized plants harbors one or more transitions in almost every GC pair of the genome. These properties, combined with ease of use, make EMS a mutagen of choice for genetic screens. Here, we describe a protocol for mutagenizing Arabidopsis seed with EMS. In addition, we briefly consider the germ line sectors typically induced by this treatment, and approaches for estimating the rate of induced mutations.

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