Tetrameric recombinant pMHCI antigens were produced as described previously (54 (link)). In brief, biotin-tagged HLA-A*0201 heavy chains and mutants thereof were expressed under the control of a T7 promoter as insoluble inclusion bodies in Escherichia coli strain BL21(DE3)pLysS (Novagen). IPTG-induced E. coli were lysed by repeated freeze/thaw cycles to release inclusion bodies that were subsequently purified by washing with a 0.5% Triton X-100 buffer (Sigma-Aldrich). The compound D227K/T228A mutation in the α3 domain of HLA A*0201 has been shown to abrogate CD8 binding without affecting the biophysical properties of the TCR docking platform (30 (link)). HLA A*0201 heavy chain and β2m inclusion body preparations were denatured separately in 8 M of urea buffer (Sigma-Aldrich) and mixed at a 1:1 molar ratio; pMHCI was refolded in 2-mercaptoethylamine/cystamine (Sigma-Aldrich) redox buffer with the appropriate synthetic peptide (BioSynthesis). After buffer exchange into 10 mM Tris, pH 8.1, refolded monomer was purified by anion exchange. Purified monomers were biotinylated using d-biotin (Sigma-Aldrich) and BirA enzyme. Excess biotin was removed by gel filtration. Biotinylated pMHCI monomers were conjugated by addition of fluorochrome-conjugated streptavidin at a 4:1 molar ratio, respectively, to produce tetrameric pMHCI complexes. All pMHCI tetramers were freshly prepared for each experiment from pMHCI monomers stored at −80°C to avoid effects due to differences in protein stability (54 (link)). The concentration of tetramer as expressed throughout this work refers to the pMHCI component and was standardized for each comparative experiment. Once prepared, tetramers were stored in the dark at 4°C. Tetramer stains were performed at 37°C for 20 min as described previously (26 (link)). For competition assays, protease inhibitor mixes were excluded from the tetramer preparations.
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Cystamine
Cystamine
Cystamine is a disulfide compound that has been extensively studied for its potential therapeutic applications.
It is a cysteine-derived molecule with a range of pharmacological properties, including antioxidant, neuroprotective, and anti-inflammatory effects.
Cystamine has been investigated for its ability to modulate cellular pathways involved in oxidative stress, apoptosis, and neurodegeneration, making it a promising candidate for the treatment of various diseases such as Huntington's disease, Parkinson's disease, and cysstamine-deficient disorders.
Researchers utilizing PubCompare.ai can optimize their cystamine studies by accessing the best protocols from literature, preprints, and patents, enhancing reproducibility and accuracy.
This AI-driven platform provides intelligent comparisons and insightful analysis to take the guesswork out of cystamine research, ultimately advancing our understanding of this versatile compound.
It is a cysteine-derived molecule with a range of pharmacological properties, including antioxidant, neuroprotective, and anti-inflammatory effects.
Cystamine has been investigated for its ability to modulate cellular pathways involved in oxidative stress, apoptosis, and neurodegeneration, making it a promising candidate for the treatment of various diseases such as Huntington's disease, Parkinson's disease, and cysstamine-deficient disorders.
Researchers utilizing PubCompare.ai can optimize their cystamine studies by accessing the best protocols from literature, preprints, and patents, enhancing reproducibility and accuracy.
This AI-driven platform provides intelligent comparisons and insightful analysis to take the guesswork out of cystamine research, ultimately advancing our understanding of this versatile compound.
Most cited protocols related to «Cystamine»
Anabolism
Anions
Antigens
Biological Assay
Biotin
Buffers
Cystamine
Cysteamine
Enzymes
Escherichia coli
Fluorescent Dyes
Freezing
Gel Chromatography
Inclusion Bodies
Isopropyl Thiogalactoside
Molar
Mutation
Oxidation-Reduction
Peptides
Protease Inhibitors
Staining
Strains
Streptavidin
Tetrameres
Triton X-100
Tromethamine
Urea
Expression and refolding of soluble constructs of DMF5 TCRs and HLA-A2 were performed as previously described [29] , [54] (link). In brief, the TCR α- and β-chains, the HLA-A2 heavy chain, and β2-microglobulin (β2m) were generated in Escherichia coli as inclusion bodies, which were isolated and denatured in 8 M urea. TCR α- and β-chains were diluted in TCR refolding buffer (50 mM Tris (pH 8), 2 mM EDTA, 2.5 M urea, 9.6 mM cysteamine, 5.5 mM cystamine, 0.2 mM PMSF) at a 1∶1 ratio. HLA-A2 and β2m were diluted in MHC refolding buffer (100 mM Tris (pH 8), 2 mM EDTA, 400 mM L-arginine, 6.3 mM cysteamine, 3.7 mM cystamine, 0.2 mM PMSF) at a 1∶1 ratio in the presence of excess peptide. TCR and pMHC complexes were incubated for 24 h at 4°C. Afterward, complexes were desalted by dialysis at 4°C and room temperature respectively, then purified by anion exchange followed by size-exclusion chromatography. Refolded protein absorptions at 280 nm were measured spectroscopically and concentrations determined with appropriate extinction coefficients. Mutations in the DMF5 α- and β-chains were generated by PCR mutagenesis and confirmed by sequencing. Peptides and plasmids were commercially synthesized and purified (Genscript).
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Anions
Arginine
Buffers
Cystamine
Cysteamine
Dialysis
Edetic Acid
Escherichia coli
Extinction, Psychological
Gel Chromatography
HLA-A2 Antigen
Inclusion Bodies
Mutagenesis
Mutation
Peptides
Plasmids
Proteins
Tromethamine
Urea
The reactivity of the sulfhydryl groups of the rRNase (1.25 µM final concentration) toward DTNB (20 µM) was evaluated in a continuous spectrophotometric assay at 412 nm where TNBS– absorbs (εM TNBS– = 11800 M−1 cm−1 at pH 5.0). The first-order kinetic constants were evaluated on the basis of t1/2 at different DTNB concentrations. The reactivity of the rRNase (1.25 µM) toward homocystine (0.4 mM), cystine (0.2 mM), and cystamine (0.2 mM) was determined in 10 mM potassium phosphate buffer, pH 7.4, 0.2 M urea. At fixed times, aliquots were placed in 0.1 M acetate buffer, pH 5.0, 0.2 M urea and the disappearance of the reactive cysteines of the rRNase was determined using DTNB as the titrant (25 °C).
The reactivity toward CDNB was evaluated using continuous spectrophotometry at 340 nm where the Cys-DNB adduct absorbs (ԑM = 9600 M−1 cm−1) [16 (link)]. The rRNase (1.25 µM) was reacted with 0.4 mM CDNB in 0.1 M potassium phosphate buffer, pH 7.4, 0.2 M urea (25 °C). A slight turbidity due to the CDNB-modified enzyme was subtracted by each determination.
The reaction of the rRNase (1.25 µM) toward NBD-Cl (20 µM) was determined spectrophotometrically at 419 nm, where the Cys-NBD adduct absorbs (ԑM = 13000 M−1 cm−1) [32 (link)], in 0.1 M potassium phosphate buffer, pH 7.4, 0.2 M urea (25 °C).
Second-order kinetic constants of the reaction between free GSH (0.1 mM) and homocystine(0.4 mM) were determined by using 0.1 M potassium phosphate buffer, pH 7.4, to determine the amount of homocysteine released as a consequence of the reaction at fixed times. Homocysteine was determined by adding NaOH (20 mM final concentration) to the mixture and after the reaction with 0.3 mM bromopyruvate. The corresponding product is a cyclic ketimine sulfur compound (cystathionine ketimine) absorbing at 296 nm (ԑM = 3200 M−1 cm−1) [33 (link)]. Second-order kinetic constants for the reaction of free cysteine toward GSSG and free GSH toward all other reagents were derived from our previous study [17 (link)]. GSH solutions were freshly prepared and the amount of GSSG was less than 1% as assayed by standard analytical procedures.
The reactivity toward CDNB was evaluated using continuous spectrophotometry at 340 nm where the Cys-DNB adduct absorbs (ԑM = 9600 M−1 cm−1) [16 (link)]. The rRNase (1.25 µM) was reacted with 0.4 mM CDNB in 0.1 M potassium phosphate buffer, pH 7.4, 0.2 M urea (25 °C). A slight turbidity due to the CDNB-modified enzyme was subtracted by each determination.
The reaction of the rRNase (1.25 µM) toward NBD-Cl (20 µM) was determined spectrophotometrically at 419 nm, where the Cys-NBD adduct absorbs (ԑM = 13000 M−1 cm−1) [32 (link)], in 0.1 M potassium phosphate buffer, pH 7.4, 0.2 M urea (25 °C).
Second-order kinetic constants of the reaction between free GSH (0.1 mM) and homocystine(0.4 mM) were determined by using 0.1 M potassium phosphate buffer, pH 7.4, to determine the amount of homocysteine released as a consequence of the reaction at fixed times. Homocysteine was determined by adding NaOH (20 mM final concentration) to the mixture and after the reaction with 0.3 mM bromopyruvate. The corresponding product is a cyclic ketimine sulfur compound (cystathionine ketimine) absorbing at 296 nm (ԑM = 3200 M−1 cm−1) [33 (link)]. Second-order kinetic constants for the reaction of free cysteine toward GSSG and free GSH toward all other reagents were derived from our previous study [17 (link)]. GSH solutions were freshly prepared and the amount of GSSG was less than 1% as assayed by standard analytical procedures.
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Acetate
bromopyruvate
Buffers
Cystamine
cystathionine ketimine
Cysteine
Cystine
Dithionitrobenzoic Acid
Enzymes
Glutathione Disulfide
Homocysteine
ketimine
Kinetics
potassium phosphate
Spectrophotometry
Sulfhydryl Compounds
Sulfur Compounds
Urea
Blood breakdown product, hemin, was used to induce cell death in primary cortical neurons. For the protective studies, cells were treated with hemin (100 μM) in the presence of NAC (0.01–1.00mM), Trolox (0.1–100.0 μM), α‐lipoic acid (0.01–2.00mM), U 73122 (0.1–100.0 μM), β carotene (0.1–100.0 μM), MS‐PPOH (0.1–100.0 μM), aspirin (0.1–100.0 μM), celecoxib (0.1–100.0 μM), Indomethacin (0.1–100.0 μM), Zileuton (0.1–100.0 μM), BW B70 (0.1–100.0 μM), BW A4C (0.1–100.0 μM), NCTT‐956 (0.1–100.0 μM), PD146176 (0.1–100.0 μM), MK 561 (0.1–100.0 μM), glutathione ethyl ester (1–10mM), L‐oxothiazolidine‐4‐carboxylate (1–10mM), cystamine (0.1–10.0 μM), and nordihydroguaiaretic acid (0.1–10.0 μM). Cell viability was analyzed 24 hours after treatment. Cells were rinsed with warm phosphate‐buffered saline (PBS) and assessed by methyl thiazolyl tetrazolium (MTT) assay. The fidelity of MTT assays in measuring viability was verified by calcein‐AM/ethidium homodimer‐1 staining (Live/Dead assay; Molecular Probes, Eugene, OR), following the manufacturer's instructions.
Aftercare
Aspirin
Biological Assay
BLOOD
BWA 4C
Carotene
Catabolism
Celecoxib
Cell Death
Cells
Cell Survival
Cortex, Cerebral
Cystamine
ethidium homodimer-1
fluorexon
Hemin
Indomethacin
Masoprocol
Molecular Probes
N-methylsulfonyl-6-(2-propargyloxyphenyl)hexanamide
Neurons
Phosphates
S-ethyl glutathione
Saline Solution
Tetrazolium Salts
Thioctic Acid
Trolox C
U 73122
zileuton
Expression constructs of the three His-tagged NTS-DBL1α domains used here was performed as described [52 (link)]. For IT4var60 the expression was carried out in Escherichia coli Shuffle T7 express: bacteria were grown at 30°C till OD600 = 0.6 and subsequently induced with 0.4 mM IPTG for 20h at 16°C. Pelleted cells were first subjected to osmotic shock, as described [53 (link)], and subsequently lysed by sonication. The soluble part, containing the recombinant protein, was separated by centrifugation at 12,000 g for 15 min and subsequently purified.
For IT4var9 and PAvarO, BL21 (DE3) bacteria were grown till OD600 = 0.8. Culture was induced for 3 h at 37°C with 0.1 mM IPTG. Following induction the cells were lysed by sonication, crude inclusion bodies were pelleted upon centrifugation at 12,000g for 30 min and solubilized in denaturing solution (6M Guanidine HCl, 50mM Tris–HCl pH 8, 100mM NaCl, 10mM EDTA pH 8, 10 mM DTT) overnight at +4°C. The recombinant proteins were refolded by the method of rapid dilution: the protein solution was filtered and added dropwise to ice-cold refolding solution (200 mM Tris–HCl pH 8, 10mM EDTA pH 8, 0.6M L-arginine, 6.5 mM cysteamine, 3.7mM cystamine) to a final concentration of 0.2 mg/ml. Refolding was allowed to proceed at +4°C for 36 h.
The recombinant DBL1α-domains were then dialysed to remove the excess of arginine and EDTA and concentrated using Amicon Ultracel centrifugal filter units (Millipore). All proteins were purified by Immobilized Metal Affinity Chromatography over TALON Cobalt column (Clontech), eluted with 200 mM imidazole and further purified to homogeneity by size exclusion chromatography on a HiLoad 16/60 Superdex 75pg colum (GE-Healthcare).
For IT4var9 and PAvarO, BL21 (DE3) bacteria were grown till OD600 = 0.8. Culture was induced for 3 h at 37°C with 0.1 mM IPTG. Following induction the cells were lysed by sonication, crude inclusion bodies were pelleted upon centrifugation at 12,000g for 30 min and solubilized in denaturing solution (6M Guanidine HCl, 50mM Tris–HCl pH 8, 100mM NaCl, 10mM EDTA pH 8, 10 mM DTT) overnight at +4°C. The recombinant proteins were refolded by the method of rapid dilution: the protein solution was filtered and added dropwise to ice-cold refolding solution (200 mM Tris–HCl pH 8, 10mM EDTA pH 8, 0.6M L-arginine, 6.5 mM cysteamine, 3.7mM cystamine) to a final concentration of 0.2 mg/ml. Refolding was allowed to proceed at +4°C for 36 h.
The recombinant DBL1α-domains were then dialysed to remove the excess of arginine and EDTA and concentrated using Amicon Ultracel centrifugal filter units (Millipore). All proteins were purified by Immobilized Metal Affinity Chromatography over TALON Cobalt column (Clontech), eluted with 200 mM imidazole and further purified to homogeneity by size exclusion chromatography on a HiLoad 16/60 Superdex 75pg colum (GE-Healthcare).
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Arginine
Bacteria
Cells
Centrifugation
Chromatography, Affinity
Claw
Cobalt
Cold Temperature
Cystamine
Cysteamine
Edetic Acid
Escherichia coli
Gel Chromatography
Guanidine
imidazole
Inclusion Bodies
Isopropyl Thiogalactoside
Metals
Osmotic Shock
Proteins
Recombinant Proteins
Sodium Chloride
Technique, Dilution
Tromethamine
Most recents protocols related to «Cystamine»
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Binding Sites
Carbon
Cardiac Arrest
CD3EAP protein, human
Centrifugation
Cystamine
Cystamine Dihydrochloride
DAC 1
Electric Conductivity
Glutaral
Graphite
Medical Devices
Nails
Phosphates
Polyethylene Terephthalates
Powder
Saline Solution
SARS-CoV-2
Silver
Soft Drinks
Vacuum
The unilateral ureteral obstruction (UUO) was performed according to the method described by Shweke et al. [26 (link)]. Briefly, under the anesthesia with 2% isoflurane, the left ureter was ligated at two separated points. Sham-operated mice had their ureter exposed but not ligated. Mice after UUO surgery were perfused with PBS to remove the blood in kidney, and pieces of the kidney were either fixed in 4% paraformaldehyde for histological examination. Cystamine was orally administrated at 1.86 mg/kg/day two days before UUO surgery.
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Anesthesia
BLOOD
Cystamine
Isoflurane
Kidney
Mice, House
Operative Surgical Procedures
paraform
Surgery, Day
Ureter
Ureteral Obstruction
Chemical reagents were mainly purchased from WAKO chemicals (Osaka, Japan) and Nacalai Tesque (Kyoto, Japan). Primary and fluorescein-conjugated secondary antibodies were listed in Suppl. Table S1 . Polyclonal anti-TG2 antibody was produced in our laboratory [29 (link)]. HRP-conjugated secondary antibodies were obtained from Jackson ImmunoResearch Laboratories (West Grove, PA, USA). Cystamine was obtained from Sigma-Aldrich (St. Louis, USA). Z-DON and Boc-DON were obtained from Zedira (Darmstadt, Germany). PD146176 and 15S-hydroxy-5Z,8Z,11Z,13E-eicosatetraenoic acid, 15(S)-HETE, were purchased from Cayman Chemical (Ann Arbor, MI, USA).
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Antibodies
Antibodies, Anti-Idiotypic
Caimans
Cystamine
Eicosatetraenoic Acids
Fluorescein
Hydroxyeicosatetraenoic Acids
The isolation of RLQ-specific TCR RLQ7 from COVID-19 CPs was described previously (16 (link)). Soluble TCR RLQ7 for structure determination was produced by in vitro folding from inclusion bodies expressed in Escherichia coli, as described previously for other SARS-CoV-2–specific TCRs (26 (link)). Codon-optimized genes encoding the TCR α (1–206) and β (1–245) chains were synthesized and cloned into the expression vector pET22b (GenScript). An interchain disulfide (CαCys160–CβCys172) was engineered to increase the folding yield of TCR RLQ7 αβ heterodimers. The mutated α and β chains were expressed separately as inclusion bodies in BL21(DE3) E. coli cells (Agilent Technologies). Bacteria were grown at 37 °C in LB medium to A600 = 0.6 to 0.8 and induced with 1 mM IPTG. After incubation for 3 h, the bacteria were harvested by centrifugation and resuspended in 50 mM Tris–HCl (pH 8.0) containing 0.1 M NaCl and 2 mM EDTA. Cells were disrupted by sonication. Inclusion bodies were washed with 50 mM Tris–HCl (pH 8.0) and 5% (v/v) Triton X-100, then dissolved in 8 M urea, 50 mM Tris–HCl (pH 8.0), 10 mM EDTA, and 10 mM DTT. For in vitro folding, the TCR α (45 mg) and β (35 mg) chains were mixed and diluted into 1 L folding buffer containing 5 M urea, 0.4 M L-arginine–HCl, 100 mM Tris–HCl (pH 8.0), 3.7 mM cystamine, and 6.6 mM cysteamine. After dialysis against 10 mM Tris–HCl (pH 8.0) for 72 h at 4 °C (buffer swapped at 48 h), the folding mixture was concentrated 20-fold and dialyzed against 50 mM MES buffer (pH 6.0) to precipitate misfolded protein. The supernatant was dialyzed overnight at 4 °C against 20 mM Tris–HCl (pH 8.0), 20 mM NaCl. Disulfide-linked TCR RLQ7 was purified using sequential Superdex 200 (20 mM Tris–HCl (pH 8.0), 20 mM NaCl) and Mono Q (20 mM Tris–HCl (pH 8.0), 0 to 1.0 M NaCl gradient) FPLC columns (GE Healthcare).
Soluble HLA-A2 loaded with RLQ peptide (RLQSLQTYV) or T1006I peptide (RLQSLQIYV) peptide was prepared by in vitro folding of E. coli inclusion bodies as described (52 (link)). Correctly folded RLQ–HLA-A2 and T1006I–HLA-A2 complexes were purified using consecutive Superdex 200 (20 mM Tris–HCl (pH 8.0), 20 mM NaCl) and Mono Q columns (20 mM Tris–HCl (pH 8.0), 0 to 1.0 M NaCl gradient).
Soluble HLA-A2 loaded with RLQ peptide (RLQSLQTYV) or T1006I peptide (RLQSLQIYV) peptide was prepared by in vitro folding of E. coli inclusion bodies as described (52 (link)). Correctly folded RLQ–HLA-A2 and T1006I–HLA-A2 complexes were purified using consecutive Superdex 200 (20 mM Tris–HCl (pH 8.0), 20 mM NaCl) and Mono Q columns (20 mM Tris–HCl (pH 8.0), 0 to 1.0 M NaCl gradient).
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Arginine Hydrochloride
Bacteria
Buffers
Cells
Centrifugation
Cloning Vectors
Codon
COVID 19
Cystamine
Cysteamine
Dialysis
Disulfides
Edetic Acid
Escherichia coli
Genes
HLA-A2 Antigen
Inclusion Bodies
isolation
Isopropyl Thiogalactoside
Mono Q
Peptides
Proteins
SARS-CoV-2
Sodium Chloride
Triton X-100
Tromethamine
Urea
The synthetic routes of AS1411-containing ACSSD are shown in Figure 1 . Briefly, CSSD was synthesized by our previous report with some modifications.16 (link) DOCA (2.0 g) and EDC (2.93 g) were placed into a flask and dissolved in 80 mL ethanol. Cystamine dihydrochloride (2.3 g) in distilled water was slowly dropped into the above solution. After 24 h stirring, the reacted solution was concentrated on a rotary evaporator in vacuo. The resulting solution was deposited at −20 ℃ and rinsed with ice-cold water. Then, DOCA conjugated cystamine (DOCA-Cys) was produced by drying under vacuum conditions. Next, 1.0 g CSA was dissolved in 20 mL of distilled water. EDC (0.165 g) and DOCA-Cys (0.19 g) in 20 mL ethanol were slowly introduced into the CSA solution. After 24 h reaction, the mixture was transferred into dialysis bags for dialysis as stated above. Further, the solution was freeze-dried for 72 h and CSSD was obtained. In the third step, for AS1411 conjugation, the carboxyl units of CSSD were activated. CSSD (50 mg) was dispersed in 5 mL distilled water and 8 mL dimethyl sulfoxide (DMSO). EDC (10.9 mg) was added. AS1411 (30 OD, oligonucleotide sequence: 5′-NH2-GGTGGTGGTGGTTGTGGTGGTGGTGG-3′) was dissolved in the mixture of DMSO and distilled water and introduced into the above solution under stirring. After 24 h, the reaction solution was dialyzed against water and lyophilized.
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Synthetic scheme of ACSSD conjugate.
1H NMR
AS 1411
Cold Temperature
Cystamine
Cystamine Dihydrochloride
Desoxycorticosterone Acetate
Dialysis
Ethanol
Fluorescent Probes
Freezing
Ice
Micelles
Oligonucleotides
pyrene
Spectroscopy, Fourier Transform Infrared
Spectroscopy, Nuclear Magnetic Resonance
Spectrum Analysis
Sulfoxide, Dimethyl
Vacuum
Top products related to «Cystamine»
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Cystamine is a chemical compound that serves as a laboratory reagent. It is a disulfide compound with the chemical formula HSCH2CH2NHCH2CH2SSH. Cystamine functions as a reducing agent and is commonly used in biochemical and organic synthesis applications.
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DMSO is a versatile organic solvent commonly used in laboratory settings. It has a high boiling point, low viscosity, and the ability to dissolve a wide range of polar and non-polar compounds. DMSO's core function is as a solvent, allowing for the effective dissolution and handling of various chemical substances during research and experimentation.
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Fetal Bovine Serum (FBS) is a cell culture supplement derived from the blood of bovine fetuses. FBS provides a source of proteins, growth factors, and other components that support the growth and maintenance of various cell types in in vitro cell culture applications.
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Dithiothreitol (DTT) is a reducing agent commonly used in biochemical and molecular biology applications. It is a small, water-soluble compound that helps maintain reducing conditions and prevent oxidation of sulfhydryl groups in proteins and other biomolecules.
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Sodium dodecyl sulfate (SDS) is a commonly used anionic detergent for various laboratory applications. It is a white, crystalline powder that has the ability to denature proteins by disrupting non-covalent bonds. SDS is widely used in biochemical and molecular biology techniques, such as protein electrophoresis, Western blotting, and cell lysis.
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N,N′-bis(acryloyl)cystamine is a chemical compound used in laboratory settings. It is a diacrylate-based crosslinking agent that can be utilized in various applications. The core function of this product is to facilitate crosslinking reactions, but a detailed description of its intended use would require further information that is not available to me at this time.
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2-Methylpyridine borane complex is a chemical compound used in laboratory settings. It serves as a reducing agent and a source of borane in chemical reactions and synthesis processes.
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Cystamine dihydrochloride is a chemical compound that is commonly used in research and laboratory settings. It is a white, crystalline powder that is soluble in water and other polar solvents. The core function of cystamine dihydrochloride is as a reducing agent and a source of the thiol group, which is important in various biochemical processes.
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D-galactose is a monosaccharide carbohydrate. It is a constituent of many natural polysaccharides, including lactose, cerebrosides, and gangliosides. D-galactose can be used as a laboratory reagent.
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N-isopropylacrylamide is a water-soluble monomer used in the synthesis of polymers. It exhibits temperature-responsive properties, undergoing a phase transition at around 32°C. This characteristic makes it a useful component in various applications involving temperature-sensitive materials.
More about "Cystamine"
Cystamine, a disulfide compound derived from the amino acid cysteine, has garnered significant attention for its potential therapeutic applications.
This versatile molecule exhibits a range of pharmacological properties, including antioxidant, neuroprotective, and anti-inflammatory effects, making it a promising candidate for the treatment of various diseases.
Researchers have extensively studied cystamine's ability to modulate cellular pathways involved in oxidative stress, apoptosis, and neurodegeneration.
This has led to investigations into its potential benefits for conditions such as Huntington's disease, Parkinson's disease, and cystamine-deficient disorders.
To optimize cystamine research, scientists can utilize the AI-driven platform PubCompare.ai.
This tool provides intelligent comparisons and insightful analysis, helping researchers locate the best protocols from literature, preprints, and patents.
By enhancing reproducibility and accuracy, PubCompare.ai takes the guesswork out of cystamine studies, ultimately advancing our understanding of this versatile compound.
In addition to cystamine, related molecules like DMSO, FBS, dithiothreitol, and sodium dodecyl sulfate have also been studied for their applications in biomedical research.
Compounds such as N,N′-bis(acryloyl)cystamine, 2-Methylpyridine borane complex, and cystamine dihydrochloride have been investigated for their potential therapeutic uses.
Furthermore, D-galactose and N-isopropylacrylamide have been explored in the context of cystamine research and related fields.
By leveraging the insights gained from the MeSH term description and the metadescription, researchers can navigate the complex landscape of cystamine-related studies with greater efficiency and confidence, ultimately contributing to the advancement of this promising area of research.
This versatile molecule exhibits a range of pharmacological properties, including antioxidant, neuroprotective, and anti-inflammatory effects, making it a promising candidate for the treatment of various diseases.
Researchers have extensively studied cystamine's ability to modulate cellular pathways involved in oxidative stress, apoptosis, and neurodegeneration.
This has led to investigations into its potential benefits for conditions such as Huntington's disease, Parkinson's disease, and cystamine-deficient disorders.
To optimize cystamine research, scientists can utilize the AI-driven platform PubCompare.ai.
This tool provides intelligent comparisons and insightful analysis, helping researchers locate the best protocols from literature, preprints, and patents.
By enhancing reproducibility and accuracy, PubCompare.ai takes the guesswork out of cystamine studies, ultimately advancing our understanding of this versatile compound.
In addition to cystamine, related molecules like DMSO, FBS, dithiothreitol, and sodium dodecyl sulfate have also been studied for their applications in biomedical research.
Compounds such as N,N′-bis(acryloyl)cystamine, 2-Methylpyridine borane complex, and cystamine dihydrochloride have been investigated for their potential therapeutic uses.
Furthermore, D-galactose and N-isopropylacrylamide have been explored in the context of cystamine research and related fields.
By leveraging the insights gained from the MeSH term description and the metadescription, researchers can navigate the complex landscape of cystamine-related studies with greater efficiency and confidence, ultimately contributing to the advancement of this promising area of research.