Cysteamine - CAS 60-23-1
Catalog number: 60-23-1
Category: Inhibitor
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Molecular Formula:
C2H7NS
Molecular Weight:
77.15
COA:
Inquire
Targets:
Others
Description:
Cysteamine is an agent for the treatment of nephropathic cystinosis and an antioxidant. It has been shown to increase intracellular glutathione levels in cystinotic cells, thus restoring the altered redox state of the cells and increased rates of apoptosis in cystinotic cells, which are thought to be the result of increased caspase 3 and protein kinase Cε activity. Cysteamine has antioxidant properties as a result of increasing glutathione production.
Purity:
>98%
Synonyms:
Cysteamine; Cystagon; L 1573; L-1573; L1573; NSC 647528; NSC-647528; NSC647528; β-MEA; β-Mercaptoethylamine; 2-Aminoethanethiol; 2-Mercaptoethylamine; Decarboxycysteine; Thioethanolamine
MSDS:
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InChIKey:
UFULAYFCSOUIOV-UHFFFAOYSA-N
InChI:
InChI=1S/C2H7NS/c3-1-2-4/h4H,1-3H2
Canonical SMILES:
C(CS)N
1.A novel treatment of cystic fibrosis acting on-target: cysteamine plus epigallocatechin gallate for the autophagy-dependent rescue of class II-mutated CFTR.
Tosco A1, De Gregorio F1, Esposito S2, De Stefano D2, Sana I2, Ferrari E2, Sepe A1, Salvadori L1, Buonpensiero P1, Di Pasqua A1, Grassia R3, Leone CA3, Guido S4, De Rosa G5, Lusa S6, Bona G7, Stoll G8,9,10,11, Maiuri MC9, Mehta A12, Kroemer G9,13,14,15,16 Cell Death Differ. 2016 Apr 1. doi: 10.1038/cdd.2016.22. [Epub ahead of print]
We previously reported that the combination of two safe proteostasis regulators, cysteamine and epigallocatechin gallate (EGCG), can be used to improve deficient expression of the cystic fibrosis transmembrane conductance regulator (CFTR) in patients homozygous for the CFTR Phe508del mutation. Here we provide the proof-of-concept that this combination treatment restored CFTR function and reduced lung inflammation (P<0.001) in Phe508del/Phe508del or Phe508del/null-Cftr (but not in Cftr-null mice), provided that such mice were autophagy-competent. Primary nasal cells from patients bearing different class II CFTR mutations, either in homozygous or compound heterozygous form, responded to the treatment in vitro. We assessed individual responses to cysteamine plus EGCG in a single-centre, open-label phase-2 trial. The combination treatment decreased sweat chloride from baseline, increased both CFTR protein and function in nasal cells, restored autophagy in such cells, decreased CXCL8 and TNF-α in the sputum, and tended to improve respiratory function.
2.Manipulating proteostasis to repair the F508del-CFTR defect in cystic fibrosis.
Esposito S1, Tosco A2, Villella VR1, Raia V3, Kroemer G4,5,6,7,8,9,10, Maiuri L11,12. Mol Cell Pediatr. 2016 Dec;3(1):13. doi: 10.1186/s40348-016-0040-z. Epub 2016 Mar 14.
Cystic fibrosis (CF) is a lethal monogenic disease caused by mutations in the cystic fibrosis transmembrane conductance regulator (CFTR) gene that entails the (diagnostic) increase in sweat electrolyte concentrations, progressive lung disease with chronic inflammation and recurrent bacterial infections, pancreatic insufficiency, and male infertility. Therapies aimed at restoring the CFTR defect have emerged. Thus, a small molecule which facilitates chloride channel opening, the potentiator Ivacaftor, has been approved for the treatment of CF patients bearing a particular class of rare CFTR mutations. However, small molecules that directly target the most common misfolded CFTR mutant, F508del, and improve its intracellular trafficking in vitro, have been less effective than expected when tested in CF patients, even in combination with Ivacaftor. Thus, new strategies are required to circumvent the F508del-CFTR defect. Airway and intestinal epithelial cells from CF patients bearing the F508del-CFTR mutation exhibit an impressive derangement of cellular proteostasis, with oxidative stress, overactivation of the tissue transglutaminase (TG2), and disabled autophagy.
3.Electrochemical Label-Free Aptasensor for Specific Analysis of Dopamine in Serum in the Presence of Structurally Related Neurotransmitters.
Álvarez-Martos I1, Ferapontova EE1. Anal Chem. 2016 Apr 5;88(7):3608-16. doi: 10.1021/acs.analchem.5b04207. Epub 2016 Mar 8.
Cellular and brain metabolism of dopamine can be correlated with a number of neurodegenerative disorders, and as such, in vivo analysis of dopamine in the presence of structurally related neurotransmitters (NT) represents a holy grail of neuroscience. Interference from those NTs generally does not allow selective electroanalysis of dopamine, which redox transformation overlaps with those of other catecholamines. In our previous work, we reported an electrochemical RNA-aptamer-based biosensor for specific analysis of dopamine (Analytical Chemistry, 2013; Vol. 85, p 121). However, the overall design of the biosensor restricted its stability and impeded its operation in serum. Here, we show that specific biorecognition and electroanalysis of dopamine in serum can be performed by the RNA aptamer tethered to cysteamine-modified gold electrodes via the alkanethiol linker. The stabilized dopamine aptasensor allowed continuous 20 h amperometric analysis of dopamine in 10% serum within the physiologically important 0.
4.SMA-SH: Modified Styrene-Maleic Acid Copolymer for Functionalization of Lipid Nanodiscs.
Lindhoud S1, Carvalho V1, Pronk JW1, Aubin-Tam ME1. Biomacromolecules. 2016 Apr 11;17(4):1516-22. doi: 10.1021/acs.biomac.6b00140. Epub 2016 Mar 22.
Challenges in purification and subsequent functionalization of membrane proteins often complicate their biochemical and biophysical characterization. Purification of membrane proteins generally involves replacing the lipids surrounding the protein with detergent molecules, which can affect protein structure and function. Recently, it was shown that styrene-maleic acid copolymers (SMA) can dissolve integral membrane proteins from biological membranes into nanosized discs. Within these nanoparticles, proteins are embedded in a patch of their native lipid bilayer that is stabilized in solution by the amphipathic polymer that wraps the disc like a bracelet. This approach for detergent-free purification of membrane proteins has the potential to greatly simplify purification but does not facilitate conjugation of functional compounds to the membrane proteins. Often, such functionalization involves laborious preparation of protein variants and optimization of labeling procedures to ensure only minimal perturbation of the protein.
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CAS 60-23-1 Cysteamine

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