4371-52-2

Usage

Chemical Description

Cysteine, homocysteine, and serine are starting materials used in the synthesis of L-cystathionine and L-allocystathionine.

InChI:InChI=1/C3H7NO2S/c4-2(1-7)3(5)6/h2,7H,1,4H2,(H,5,6)/t2-/m0/s1

Upstream product

• 56-89-3 cysteine disulfide 
• 56-89-3 L-cystine 
• 143-33-9 sodium cyanide 
• 19538-81-9 N,S-diacetyl-cysteine 
• 91641-78-0 N-benzoyl-cysteine ethyl ester 
• 5680-65-9 2-amino-3-(benzylthio)propionic acid 
• 52-90-4 L-Cysteine 
• 7732-18-5 water 
• 10034-85-2 hydrogen iodide 
• 922-56-5 meso-lanthionine 
• 600-05-5 2,3-dibromopropionic acid 
• 498-59-9 S,S'-methylenebis(cysteine) 
• 7664-93-9 sulfuric acid 
• 7218-04-4 N-Acetylcysteine 

Downstream Products

• 89299-66-1 (RS)-2-amino-3-<(2-chloroethyl)sulfanyl>propanoic acid hydrochloride 
• 2139-90-4 2-amino-3-(ethylthio)propionic acid 
• 109819-52-5 N,S-bis-[(2,4,5-trichloro-phenoxy)-acetyl]-cysteine 
• 75-07-0 acetaldehyde 
• 921-01-7 D-cysteine 
• 56-89-3 cysteine disulfide 
• 6020-39-9 L-cystine 
• 923-32-0 DL-cystine 
• 56-89-3 L-cystine 
• 107-36-8 2-hydroxyethanesulfonic acid 
• 5680-65-9 2-amino-3-(benzylthio)propionic acid 
• 52386-79-5 S-(4-chloro-benzyl)-cysteine 
• 16708-09-1 2-methyl-thiazolidine-2,4-dicarboxylic acid 
• 49621-03-6 S-propenyl-L-cysteine 

Relevant academic research and scientific papers

MODIFIED INTERLEUKIN-7 PROTEINS AND USES THEREOF

Provided are a modified IL-7 polypeptide and a fusion protein containing the modified IL-7 polypeptide. The fusion protein of the modified IL-7 includes: a first domain containing an interleukin-7 polypeptide; a second domain containing an oligopeptide having 1 to 10 amino acid residues (with proviso that the second domain excludes the oligopeptide consisting of methionine and/or glycine); and (c) a third domain which prolongs the half-life of the IL-7 fusion protein. The modified IL-7 polypeptide is composed of the (a) first domain and the (b) second domain. The modified IL-7 polypeptide and the fusion protein are expressed in a higher yield than the wild-type IL-7 and shows increased stability.

Synthesis method of DL-cysteine

The invention discloses a synthetic method of DLcysteine. The method comprises the following steps: by using acrylonitrile as a raw material, chlorinating to generate 2, 3dichloropropionitrile, hydrolyzing to generate corresponding acid, reacting the acid with thiourea to cyclize to generate 2-aminothiazoline-4-carboxylic acid, adding alkali sulfide to generate 2-mercaptothiazoline-4-carboxylic acid, and hydrolyzing to generate cysteine. The synthesis method provided by the invention has the advantages of short synthesis steps, mild preparation conditions, sufficient and cheap raw material sources and higher product yield.

Cysteine Chemistry in Connection with Abiogenesis

Theoretical and experimental work has been conducted about possible prebiotic syntheses of cysteine. Activated derivatives of this amino acid can oligomerize and polymerize to afford various poly-thiazolines and cysteine-rich chains.

Dynamic Kinetic Resolution for Asymmetric Synthesis of L-Noncanonical Amino Acids from D-Ser Using Tryptophan Synthase and Alanine Racemase

L-Ser is often used to synthesize some significant l-noncanonical α-amino acids(l-ncAAs), which are the prevalent intermediates and precursors for functional synthetic compounds. In this study, threonine aldolase from Escherichia coli k-12 MG1655 has been used to synthesize l-Ser. In contrast to the maximum catalytic capacity (20 g/L) for l-threonine aldolase(LTA), d-Ser was synthesized with high yield (240 g/L) from cheap Gly and paraformaldehyde using d-threonine aldolase (DTA) from Arthrobacter sp ATCC. In order to fully utilize d-Ser and expand the resource of l-Ser, a dynamic kinetic resolution system was constructed to convert d/dl-Ser to l-Ser through combining alanine racemase (Alr) from Bacillus subtilis with l-tryptophan synthase (TrpS) from Escherichia coli k-12 MG1655, and l-ncAAs including l-Trp and l-Cys derivatives were synthesized with excellent enantioselectivity and in high yields. The results indicated l-ncAAs could be efficiently synthesized from d-Ser using this original and green dynamic kinetic resolution system, and the reliable l-Ser resource has been established from simple and achiral substrates.

T Cells with Increased Immunosuppression Resistance

This invention relates to the treatment of cancer in an individual by administration of a population of modified T cells that express a recombinant cAMP phosphodiesterase (PDE) or a fragment thereof and an antigen receptor which binds specifically to cancer cells in the individual. Populations of modified T cells and methods of producing populations of modified T cells are provided, along with pharmaceutical compositions and methods of treatment

Protection of Endogenous Thiols against Methylmercury with Benzimidazole-Based Thione by Unusual Ligand-Exchange Reactions

Organomercurials, such as methylmercury (MeHg+), are among the most toxic materials to humans. Apart from inhibiting proteins, MeHg+ exerts its cytotoxicity through strong binding with endogenous thiols cysteine (CysH) and glutathione (GSH) to form MeHgCys and MeHgSG complexes. Herein, it is reported that the N,N-disubstituted benzimidazole-based thione 1 containing a N?CH2CH2OH substituent converts MeHgCys and MeHgSG complexes to less toxic water-soluble HgS nanoparticles (NPs) and releases the corresponding free thiols CysH and GSH from MeHgCys and MeHgSG, respectively, in solution by unusual ligand-exchange reactions in phosphate buffer at 37 °C. However, the corresponding N-substituted benzimidazole-based thione 7 and N,N-disubstituted imidazole-based thione 3, in spite of containing a N?CH2CH2OH substituent, failed to convert MeHgX (X=Cys, and SG) to HgS NPs under identical reaction conditions, which suggests that not only the N?CH2CH2OH moiety but the benzimidazole ring and N,N-disubstitution in 1, which leads to the generation of a partial positive charge at the C2 atom of the benzimidazole ring in 1:1 MeHg-conjugated complex of 1, are crucial to convert MeHgX to HgS NPs under physiologically relevant conditions.

Anti-fibroblast activation protein antibodies and methods and uses thereof

Specific binding members, particularly antibodies and fragments thereof, which bind to Fibroblast Activation Protein (FAP) are provided, particularly recognizing both human and mouse FAP. These antibodies are useful in the diagnosis and treatment of conditions associated with activated stroma, including wound healing, epithelial cancers, osteoarthritis, rheumatoid arthritis, cirrhosis and pulmonary fibrosis. The anti-FAP antibodies, variable regions or CDR domain sequences thereof, and fragments thereof may also be used in therapy in combination with chemotherapeutics, immune modulators, or anti-cancer agents and/or with other antibodies or fragments thereof. Antibodies of this type are exemplified by the novel antibodies ESC1 1 and ESC 14 whose sequences are provided herein.

METHODS FOR TREATING MUSCLE SPECIFIC RECEPTOR KINASE MYASTHENIA GRAVIS

Agents, compositions, and medicaments that reduce interactions between muscle specific kinase receptor (MuSK) and pathogenic immunoglobulin G4 (IgG4) antibodies specific for the first Ig-like domain of MuSK and methods and uses thereof to reduce such interactions are encompassed herein. Also encompassed are screening assays to identify inhibitors of these pathogenic antibodies, particularly those that reduce binding to MuSK. Agents identified using the screening assays described herein are envisioned for use as therapeutics, alone or in compositions or in medicaments, to improve motor function in subjects afflicted MuSK-MG.

FUNCTIONALIZED FLUORINE CONTAINING PHTHALOCYANINE MOLECULES

Functionalized fluorine containing phthalocyanine molecules, methods of making, and methods of use in diagnostic applications and disease treatment are disclosed herein. In some embodiments, the fluorine containing phthalocyanine molecules are functionalized with a reactive functional group or at least one cancer-targeting ligand (CTL). The CTL can facilitate more efficient binding and/or internalization to a cancer cell than to a healthy cell. The CTL can inhibit expression of oncoprotein in some embodiments. The pthalocyanine moiety can be used in diagnostic applications, such as fluorescence labeling of a cancer cell, and/or treatment applications, such as catalyzing formation of a reactive oxygen species (ROS) which can contribute to cell death of a cancer cell.

Antibody molecules having specificity for human OX40

The invention relates to antibody molecules having specificity for antigenic determinants of human OX40, therapeutic uses of the antibody molecules and methods for producing said antibody molecules.