About This Item
Polecane produkty
Próba
≥98% (TLC)
Postać
powder
kolor
white
ciąg SMILES
CC(N)(CO)C(O)=O
InChI
1S/C4H9NO3/c1-4(5,2-6)3(7)8/h6H,2,5H2,1H3,(H,7,8)
Klucz InChI
CDUUKBXTEOFITR-UHFFFAOYSA-N
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Działania biochem./fizjol.
α-Methyl-DL-serine is an amino acid derivative.
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Kod klasy składowania
13 - Non Combustible Solids
Klasa zagrożenia wodnego (WGK)
WGK 3
Temperatura zapłonu (°F)
Not applicable
Temperatura zapłonu (°C)
Not applicable
Środki ochrony indywidualnej
Eyeshields, Gloves, type N95 (US)
Certyfikaty analizy (CoA)
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Dokumenty związane z niedawno zakupionymi produktami zostały zamieszczone w Bibliotece dokumentów.
Bioscience, biotechnology, and biochemistry, 72(10), 2580-2588 (2008-10-08)
The alpha-methylserine aldolase gene from Variovorax paradoxus strains AJ110406, NBRC15149, and NBRC15150 was cloned and expressed in Escherichia coli. Formaldehyde release activity from alpha-methyl-L-serine was detected in the cell-free extract of E.coli expressing the gene from three strains. The recombinant
The Journal of organic chemistry, 74(24), 9305-9313 (2009-11-21)
The synthesis and the conformational analysis in aqueous solution of a peptide and a glycopeptide containing the sequence threonine-alanine-alanine (Thr-Ala-Ala) are reported. Furthermore, the threonine residue has been replaced by the quaternary amino acid alpha-methylserine (MeSer) and their corresponding non-natural
Chemical communications (Cambridge, England), 47(18), 5319-5321 (2011-04-01)
A novel Tn antigen mimic, in which the natural underlying amino acid has been replaced by the non-natural α-methylserine analogue, is reported. This derivative exhibits a similar affinity for a natural lectin as for the natural Tn and retains the
Biochemical and biophysical research communications, 340(3), 823-828 (2005-12-29)
In many complexes formed by serine proteinases and their inhibitors, the hydroxyl group provided by water molecule or by the inhibitor Ser residue is located close to the inhibitor P1-P1' reactive site. In order to investigate the role of this
Acta chemica Scandinavica (Copenhagen, Denmark : 1989), 46(10), 989-993 (1992-10-01)
The three-dimensional structure of the RGD-adhesion sequence has been studied previously by means of linear and cyclic peptides. These peptides show widely differing affinities to integrins, ascribed to a strong dependence on steric factors in the receptor recognition. Insertion of
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