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Key Documents

C2196

Sigma-Aldrich

L-Cysteine S-sulfate

≥98% (TLC), suitable for ligand binding assays

Synonyme(s) :

S-Sulfo-L-cysteine

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About This Item

Formule empirique (notation de Hill):
C3H7NO5S2
Numéro CAS:
Poids moléculaire :
201.22
Numéro Beilstein :
1726832
Numéro MDL:
Code UNSPSC :
12352209
ID de substance PubChem :
Nomenclature NACRES :
NA.26

product name

L-Cysteine S-sulfate, ≥98% (TLC)

Niveau de qualité

Pureté

≥98% (TLC)

Forme

powder

Technique(s)

ligand binding assay: suitable

Couleur

white

Température de stockage

−20°C

Chaîne SMILES 

N[C@@H](CSS(O)(=O)=O)C(O)=O

InChI

1S/C3H7NO5S2/c4-2(3(5)6)1-10-11(7,8)9/h2H,1,4H2,(H,5,6)(H,7,8,9)/t2-/m0/s1

Clé InChI

NOKPBJYHPHHWAN-REOHCLBHSA-N

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Actions biochimiques/physiologiques

L-Cysteine S-sulfate (LCSS) is used as an NMDA glutamatergic receptor agonist. It serves as a substrate for cystine lyase(s).
Cysteine is one of the functional amino acids that are associated with growth, reproduction, maintenance and immunity. Cysteine is a source of disulfide linkage in protein and is associated with sulfur transport. At physiological pH, cysteine undergoes rapid oxidation to form cystine. Reduced availability of cysteine or cystine, influences leukocyte metabolism. L-Cysteine serves as a precursor for the rate limiting step in glutathione synthesis that occurs in neurons. It donates inorganic sulfate for detoxification reactions. Therefore, L-cysteine might be associated with neuroprotection. It is found to obstruct the entry of heavy metal ions across the blood-brain barrier into the brain. Increased levels of L-cysteine might lead to neurotoxicity.

Pictogrammes

Exclamation mark

Mention d'avertissement

Warning

Mentions de danger

Classification des risques

Eye Irrit. 2 - Skin Irrit. 2 - STOT SE 3

Organes cibles

Respiratory system

Code de la classe de stockage

11 - Combustible Solids

Classe de danger pour l'eau (WGK)

WGK 3

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable

Équipement de protection individuelle

dust mask type N95 (US), Eyeshields, Gloves


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Les clients ont également consulté

R Nahum-Levy et al.
Biophysical journal, 80(5), 2152-2166 (2001-04-28)
Two distinct forms of desensitization have been characterized for N-methyl-D-aspartate (NMDA) receptors. One form results from a weakening of agonist affinity when channels are activated whereas the other form of desensitization results when channels enter a long-lived nonconducting state. A
Desensitization of NMDA receptor channels is modulated by glutamate agonists.
Nahum-Levy R
Biophysical Journal, 80(5), 2152-2166 (2001)
Takeshi Nakatani et al.
Microbial cell factories, 11, 62-62 (2012-05-23)
Escherichia coli has two L-cysteine biosynthetic pathways; one is synthesized from O-acetyl L-serine (OAS) and sulfate by L-cysteine synthase (CysK), and another is produced via S-sulfocysteine (SSC) from OAS and thiosulfate by SSC synthase (CysM). SSC is converted into L-cysteine
E C Ramírez et al.
Journal of agricultural and food chemistry, 47(6), 2218-2225 (2000-05-04)
Cystine lyase is the enzyme responsible for off-aroma deterioration in fresh unblanched broccoli. In this research, cystine lyase purification from broccoli has been optimized. Only one protein peak with cystine lyase activity was found during purification. Broccoli cystine lyase was
Claus Jacob et al.
Angewandte Chemie (International ed. in English), 42(39), 4742-4758 (2003-10-17)
Sulfur and selenium occur in proteins as constituents of the amino acids cysteine, methionine, selenocysteine, and selenomethionine. Recent research underscores that these amino acids are truly exceptional. Their redox activity under physiological conditions allows an amazing variety of posttranslational protein

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