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Wichtige Dokumente
684538
Natriummethanthiosulfonat
95%
Synonym(e):
Methansulfonothiosäure Natriumsalz, Natrium-methylthiosulfonat
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About This Item
Empfohlene Produkte
Qualitätsniveau
Assay
95%
Form
crystals
mp (Schmelzpunkt)
265 °C (dec.)
SMILES String
CS(=O)(=O)S[Na]
InChI
1S/CH4O2S2.Na/c1-5(2,3)4;/h1H3,(H,2,3,4);/q;+1/p-1
InChIKey
JFTZUZWJGUCSTE-UHFFFAOYSA-M
Signalwort
Warning
H-Sätze
Gefahreneinstufungen
Eye Irrit. 2 - Skin Irrit. 2 - STOT SE 3
Zielorgane
Respiratory system
Lagerklassenschlüssel
11 - Combustible Solids
WGK
WGK 3
Persönliche Schutzausrüstung
dust mask type N95 (US), Eyeshields, Gloves
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SLC26A4/PDS mutations cause Pendred Syndrome and non-syndromic deafness. but some aspects of function and regulation of the SLC26A4 polypeptide gene product, pendrin, remain controversial or incompletely understood. We have therefore extended the functional analysis of wildtype and mutant pendrin in
Acta crystallographica. Section C, Crystal structure communications, 64(Pt 11), o586-o589 (2008-11-08)
The title compound, C(10)H(18)NO(3)S(2), which finds application as a spin label, has triclinic (P\overline{1}) symmetry at 100 (2) K with two independent molecules in the asymmetric unit. Both molecules are very similar with respect to bond lengths and angles, but
Proceedings of the National Academy of Sciences of the United States of America, 108(29), 12149-12154 (2011-07-07)
Despite its long history of use and abuse in human culture, the molecular basis for alcohol action in the brain is poorly understood. The recent determination of the atomic-scale structure of GLIC, a prokaryotic member of the pentameric ligand-gated ion
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Inhibitor and substrate interactions with equilibrative nucleoside transporter 1 (ENT1; SLC29A1) are known to be affected by cysteine-modifying reagents. Given that selective ENT1 inhibitors, such as nitrobenzylmercaptopurine riboside (NBMPR), bind to the N-terminal half of the ENT1 protein, we hypothesized
Nitric oxide : biology and chemistry, 25(2), 108-111 (2010-11-30)
S-nitrosylation is a well-characterized reaction involving the covalent binding of nitric oxide (NO) to cysteine residues (Cys) in a protein. Similar to protein phosphorylation, S-nitrosylation is a post-translational modification involved in the regulation of a large number of intracellular functions
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