C2196
L-Cysteine S-sulfate
≥98% (TLC), suitable for ligand binding assays
Synonym(s):
S-Sulfo-L-cysteine
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About This Item
Empirical Formula (Hill Notation):
C3H7NO5S2
CAS Number:
Molecular Weight:
201.22
Beilstein:
1726832
MDL number:
UNSPSC Code:
12352209
PubChem Substance ID:
NACRES:
NA.26
Product Name
L-Cysteine S-sulfate, ≥98% (TLC)
Quality Level
Assay
≥98% (TLC)
form
powder
technique(s)
ligand binding assay: suitable
color
white
storage temp.
−20°C
SMILES string
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
InChI key
NOKPBJYHPHHWAN-REOHCLBHSA-N
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Biochem/physiol Actions
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.
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.
Signal Word
Warning
Hazard Statements
Precautionary Statements
Hazard Classifications
Eye Irrit. 2 - Skin Irrit. 2 - STOT SE 3
Target Organs
Respiratory system
Storage Class Code
11 - Combustible Solids
WGK
WGK 3
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
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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
Mechanisms of L-Cysteine Neurotoxicity
R. Janaky
Neurochemical Research, 25, 1397-1405 (2000)
L H Ngu et al.
Singapore medical journal, 50(10), e365-e367 (2009-11-13)
Molybdenum cofactor deficiency is a rare autosomal recessive disorder with devastating neurological manifestations, characterised by neonatal-onset encephalopathy mimicking hypoxic-ischaemic insult, intractable seizure, and feeding and respiratory difficulties. It is often fatal in the early life. We report an affected 8-year-old
Emma E Hobson et al.
European journal of pediatrics, 164(11), 655-659 (2005-07-19)
Isolated sulphite oxidase deficiency (ISOD) is a rare autosomal recessive inborn error of metabolism, which may present at birth with intractable seizures (often of prenatal onset) and severe neurological abnormalities. In infants who survive, lens dislocation may occur from 8
Cecilia Gotor et al.
Plant signaling & behavior, 5(8), 1028-1030 (2010-08-12)
The cysteine molecule plays an essential role in cells because it is part of proteins and because it functions as a reduced sulfur donor molecule. In addition, the cysteine molecule may also play a role in the redox signaling of
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