L-Cysteic acid monohydrate
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L-Cysteic acid monohydrate

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A major metabolite of non-essential amino acid L-Cysteine.

Category
L-Amino Acids
Catalog number
BAT-007699
CAS number
23537-25-9
Molecular Formula
C3H9NO6S
Molecular Weight
187.17
L-Cysteic acid monohydrate
IUPAC Name
(2R)-2-amino-3-sulfopropanoic acid;hydrate
Synonyms
3-Sulfo-L-alanine Monohydrate; (R)-2-Amino-3-sulfopropanoic Acid Monohydrate
Related CAS
498-40-8 (anhydrous)
Appearance
White to Off-White Solid
Purity
98%
Density
1.775 g/cm3
Melting Point
>245°C (dec.)
Storage
Store at -20°C
Solubility
Soluble in Methanol (Slightly), Water (Sparingly, Sonicated)
InChI
InChI=1S/C3H7NO5S.H2O/c4-2(3(5)6)1-10(7,8)9;/h2H,1,4H2,(H,5,6)(H,7,8,9);1H2/t2-;/m0./s1
InChI Key
PCPIXZZGBZWHJO-DKWTVANSSA-N
Canonical SMILES
C(C(C(=O)O)N)S(=O)(=O)O.O

L-Cysteic acid monohydrate, a versatile chemical compound, finds diverse applications in biological research and industry. Here are four key applications of L-Cysteic acid monohydrate:

Neuroscience Research: Serving as a pivotal research tool, L-Cysteic acid monohydrate plays a crucial role in probing excitatory neurotransmission within the intricate realms of the brain. Acting as an agonist for NMDA receptors, this compound facilitates the exploration of synaptic plasticity and sheds light on neurodegenerative disorders. Its significance lies in unraveling the intricate dance of amino acids within brain processes.

Protein Chemistry: In the realm of protein chemistry, L-Cysteic acid monohydrate emerges as a key player in the modification of cysteine residues on proteins, paving the way for a deeper understanding of protein structure and function. Its utility extends to the creation of stable protein derivatives with diverse applications. Researchers harness the power of this compound to illuminate the complex interplay of protein folding and interactions.

Biotechnology: A fundamental building block in peptide and protein synthesis, L-Cysteic acid monohydrate fuels advancements in biotechnology by underpinning the creation of peptides and proteins with tailored properties. Its inclusion in synthetic sequences drives progress in the realms of protein mimetics and novel biomolecule design. This application holds immense promise in the development of therapeutic peptides and the burgeoning field of synthetic biology.

Analytical Chemistry: A stalwart in high-performance liquid chromatography (HPLC), L-Cysteic acid monohydrate stands as a gold standard for amino acid analysis, facilitating the precise quantification and identification of amino acids within complex biological samples. This role is indispensable in the realms of proteomics studies, nutritional analysis, and quality control in biochemical production processes, offering a critical lens into the molecular tapestry of biological systems.

1.Free radical conformations and conversions in X-irradiated single crystals of L-cysteic acid by electron magnetic resonance and density functional theory studies.
Øhman KT1, Sagstuen E. J Phys Chem A. 2008 May 8;112(18):4284-93. doi: 10.1021/jp711821c. Epub 2008 Apr 16.
Single crystals of L-cysteic acid monohydrate were X-irradiated and studied at 295 K using EPR, ENDOR, and EIE techniques. Three spectroscopically different radicals were observed. These were a deamination radical reduction product (R1), and two oxidation products formed by hydrogen abstraction (radicals R2, R3). R2 and R3 were shown to exhibit the same chemical structure while exhibiting very different geometrical conformations. Cluster DFT calculations at the 6-31G(d,p) level of theory supported the experimental observations for radicals R1 and R2. It was not possible to simulate the R3 radical in any attempted cluster; hence, for this purpose a single molecule approach was used. The precursor radicals for R1, R2, and R3, identified in the low-temperature work on L-cysteic acid monohydrate by Box and Budzinski, were also investigated using DFT calculations. The experimentally determined EPR parameters for the low-temperature decarboxylated cation could only be reproduced correctly within the cluster when the carboxyl group remained in the proximity of the radical.
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