Dithiothreitol
Reducing Agents
Sulfhydryl Reagents
Disulfides
Oxidation-Reduction
A chemical reaction in which an electron is transferred from one molecule to another. The electron-donating molecule is the reducing agent or reductant; the electron-accepting molecule is the oxidizing agent or oxidant. Reducing and oxidizing agents function as conjugate reductant-oxidant pairs or redox pairs (Lehninger, Principles of Biochemistry, 1982, p471).
Dithionitrobenzoic Acid
Diamide
Glutathione
Enzyme Reactivators
Hydrogen-Ion Concentration
Electrophoresis, Polyacrylamide Gel
Thioredoxins
Hydrogen-donating proteins that participates in a variety of biochemical reactions including ribonucleotide reduction and reduction of PEROXIREDOXINS. Thioredoxin is oxidized from a dithiol to a disulfide when acting as a reducing cofactor. The disulfide form is then reduced by NADPH in a reaction catalyzed by THIOREDOXIN REDUCTASE.
Hydroxymercuribenzoates
Thimerosal
Dithioerythritol
Edetic Acid
Glutathione Disulfide
Chromatography, Gel
Substrate Specificity
Hydrogen Peroxide
Amino Acid Sequence
Molecular Sequence Data
Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories.
Enzyme Activation
Cattle
Macromolecular Substances
Dimercaprol
Escherichia coli
A species of gram-negative, facultatively anaerobic, rod-shaped bacteria (GRAM-NEGATIVE FACULTATIVELY ANAEROBIC RODS) commonly found in the lower part of the intestine of warm-blooded animals. It is usually nonpathogenic, but some strains are known to produce DIARRHEA and pyogenic infections. Pathogenic strains (virotypes) are classified by their specific pathogenic mechanisms such as toxins (ENTEROTOXIGENIC ESCHERICHIA COLI), etc.
Oxidants
Cystamine
Iodoacetates
Protein Conformation
The characteristic 3-dimensional shape of a protein, including the secondary, supersecondary (motifs), tertiary (domains) and quaternary structure of the peptide chain. PROTEIN STRUCTURE, QUATERNARY describes the conformation assumed by multimeric proteins (aggregates of more than one polypeptide chain).
Phosphorous Acids
Temperature
Amino Acids
Adenosine Triphosphate
Binding Sites
Chromatography, Ion Exchange
Trypsin
Rabbits
Cystine
NADP
Nicotinamide adenine dinucleotide phosphate. A coenzyme composed of ribosylnicotinamide 5'-phosphate (NMN) coupled by pyrophosphate linkage to the 5'-phosphate adenosine 2',5'-bisphosphate. It serves as an electron carrier in a number of reactions, being alternately oxidized (NADP+) and reduced (NADPH). (Dorland, 27th ed)
Chromatography, High Pressure Liquid
Cations, Divalent
Chromatography, Affinity
Magnesium
Calcium
A basic element found in nearly all organized tissues. It is a member of the alkaline earth family of metals with the atomic symbol Ca, atomic number 20, and atomic weight 40. Calcium is the most abundant mineral in the body and combines with phosphorus to form calcium phosphate in the bones and teeth. It is essential for the normal functioning of nerves and muscles and plays a role in blood coagulation (as factor IV) and in many enzymatic processes.
Liver
Affinity Labels
Alkylation
Cross-Linking Reagents
Reagents with two reactive groups, usually at opposite ends of the molecule, that are capable of reacting with and thereby forming bridges between side chains of amino acids in proteins; the locations of naturally reactive areas within proteins can thereby be identified; may also be used for other macromolecules, like glycoproteins, nucleic acids, or other.
Isomerases
Chemistry
Peroxides
A group of compounds that contain a bivalent O-O group, i.e., the oxygen atoms are univalent. They can either be inorganic or organic in nature. Such compounds release atomic (nascent) oxygen readily. Thus they are strong oxidizing agents and fire hazards when in contact with combustible materials, especially under high-temperature conditions. The chief industrial uses of peroxides are as oxidizing agents, bleaching agents, and initiators of polymerization. (From Hawley's Condensed Chemical Dictionary, 11th ed)
Cytosol
Enzyme Stability
Chemical Phenomena
Protein Disulfide-Isomerases
Cell Membrane
Oxidoreductases
The class of all enzymes catalyzing oxidoreduction reactions. The substrate that is oxidized is regarded as a hydrogen donor. The systematic name is based on donor:acceptor oxidoreductase. The recommended name will be dehydrogenase, wherever this is possible; as an alternative, reductase can be used. Oxidase is only used in cases where O2 is the acceptor. (Enzyme Nomenclature, 1992, p9)
Mersalyl
Detergents
Protein Binding
Isoelectric Focusing
Rats, Inbred Strains
NAD
A coenzyme composed of ribosylnicotinamide 5'-diphosphate coupled to adenosine 5'-phosphate by pyrophosphate linkage. It is found widely in nature and is involved in numerous enzymatic reactions in which it serves as an electron carrier by being alternately oxidized (NAD+) and reduced (NADH). (Dorland, 27th ed)
Protein Denaturation
Nitric Oxide Donors
A diverse group of agents, with unique chemical structures and biochemical requirements, which generate NITRIC OXIDE. These compounds have been used in the treatment of cardiovascular diseases and the management of acute myocardial infarction, acute and chronic congestive heart failure, and surgical control of blood pressure. (Adv Pharmacol 1995;34:361-81)
Solubility
Chromatography
Techniques used to separate mixtures of substances based on differences in the relative affinities of the substances for mobile and stationary phases. A mobile phase (fluid or gas) passes through a column containing a stationary phase of porous solid or liquid coated on a solid support. Usage is both analytical for small amounts and preparative for bulk amounts.
Sperm Head
Plants
Multicellular, eukaryotic life forms of kingdom Plantae (sensu lato), comprising the VIRIDIPLANTAE; RHODOPHYTA; and GLAUCOPHYTA; all of which acquired chloroplasts by direct endosymbiosis of CYANOBACTERIA. They are characterized by a mainly photosynthetic mode of nutrition; essentially unlimited growth at localized regions of cell divisions (MERISTEMS); cellulose within cells providing rigidity; the absence of organs of locomotion; absence of nervous and sensory systems; and an alternation of haploid and diploid generations.
Regulation of 2-carboxy-D-arabinitol 1-phosphate phosphatase: activation by glutathione and interaction with thiol reagents. (1/2188)
2-Carboxy-D-arabinitol 1-phosphate (CA1P) phosphatase de- grades CA1P, an inhibitor associated with the regulation of ribulose bisphosphate carboxylase/oxygenase in numerous plant species. CA1P phosphatase purified from Phaseolus vulgaris was partially inactivated by oxidizing conditions during dialysis in air-equilibrated buffer. Phosphatase activity could then be stimulated 1.3-fold by dithiothreitol and also by addition of reduced thioredoxin from Escherichia coli. These effects were enhanced synergistically by the positive effector, fructose 1, 6-bisphosphate (FBP). Most notably, CA1P phosphatase activity was stimulated up to 35-fold by glutathione, and was sensitive to the ratio of reduced (GSH) to oxidized (GSSG) forms. At concentrations of glutathione approximating measured levels in chloroplasts of P. vulgaris (5 mM total S), CA1P phosphatase exhibited >20-fold stimulation by a change in the redox status of glutathione from 60 to 100% GSH. This stimulation was augmented further by reduced E. coli thioredoxin. In contrast, FBP, which activates CA1P phosphatase under reducing conditions, was strongly inhibitory in the presence of GSSG. We propose that glutathione may have an appreciable role in the light/dark regulation of CA1P phosphatase in vivo. A model for the reversible activation of CA1P phosphatase by GSH was derived based upon the various responses of the enzyme's activity to a range of thiol reagents including N-ethylmaleimide, 5, 5'-dithiobis-(2-nitrobenzoic acid) and arsenite. These data indicate that the bean enzyme contains two physically distinct sets of thiol groups that are critical to its redox regulation. (+info)In vivo formation of Cu,Zn superoxide dismutase disulfide bond in Escherichia coli. (2/2188)
We have found that the in vivo folding of periplasmic Escherichia coli Cu,Zn superoxide dismutase is assisted by DsbA, which catalyzes the efficient formation of its single disulfide bond, whose integrity is essential to ensure full catalytic activity to the enzyme. In line with these findings, we also report that the production of recombinant Xenopus laevis Cu,Zn superoxide dismutase is enhanced when the enzyme is exported in the periplasmic space or is expressed in thioredoxin reductase mutant strains. Our data show that inefficient disulfide bond oxidation in the bacterial cytoplasm inhibits Cu,Zn superoxide dismutase folding in this cellular compartment. (+info)An intact sperm nuclear matrix may be necessary for the mouse paternal genome to participate in embryonic development. (3/2188)
We have been interested in determining the minimally required elements in the sperm head that are necessary in order for the paternal genome to participate in embryogenesis. We used an ionic detergent, mixed alkyltrimethylammonium bromide (ATAB), plus dithiothreitol (DTT) to remove the acrosome and almost all of the perinuclear theca, leaving only the sperm nucleus morphologically intact. We also tested the stability of the sperm nuclear matrix by the ability to form nuclear halos. Sperm nuclei washed in freshly prepared 0.5% ATAB + 2 mM DTT completely decondensed when extracted with salt, but nuclei washed in the same buffer that was 1 wk old, and then extracted with salt, produced nuclear halos, indicating stable nuclear matrices. When we treated sperm heads with freshly prepared ATAB+DTT and injected them into oocytes, none of the oocytes developed into live offspring. In contrast, sperm heads treated in the same way but with 1-wk-old ATAB+DTT solution could support development of about 30% of the oocytes to live offspring. Electron microscopy demonstrated that most of the perinuclear theca had been removed in both cases. These data suggest that at least in the mouse, the only component of the spermatozoa that is crucial for participation in embryologic development is the sperm nucleus with a stable nuclear matrix. (+info)A novel trans-complementation assay suggests full mammalian oocyte activation is coordinately initiated by multiple, submembrane sperm components. (4/2188)
To initiate normal embryonic development, an egg must receive a signal to become activated at fertilization. We here report that the ability of demembranated sperm heads to activate is abolished after incubation over the range 20-44 degreesC and is sensitive to reducing agents. On the basis of this observation, we have developed a microinjection-based, trans-complementation assay in order to dissect the heat-inactivated sperm-borne oocyte-activating factor(s) (SOAF). We demonstrate that the failure of heat-inactivated sperm heads to activate an egg is rescued by coinjection with dithiothreitol-solubilized SOAF from demembranated sperm heads. The solubilized SOAF (SOAFs) is trypsin sensitive and is liberated from demembranated heads in a temperature-dependent manner that inversely correlates with the ability of sperm heads to activate. This argues that SOAFs is a proteinaceous molecular species required to initiate activation. Injection of oocytes with mouse or hamster sperm cytosolic factors, but not SOAFs alone, induced resumption of meiosis, further suggesting that these cytosolic factors and SOAF are distinct. Collectively, these data strongly suggest that full mammalian oocyte activation is initiated by the coordinated action of one or more heat-sensitive protein constituents of the perinuclear matrix and at least one heat-stable submembrane component. (+info)Transforming growth factor-beta induces formation of a dithiothreitol-resistant type I/Type II receptor complex in live cells. (5/2188)
Transforming growth factor-beta (TGF-beta) binds to and signals via two serine-threonine kinase receptors, the type I (TbetaRI) and type II (TbetaRII) receptors. We have used different and complementary techniques to study the physical nature and ligand dependence of the complex formed by TbetaRI and TbetaRII. Velocity centrifugation of endogenous receptors suggests that ligand-bound TbetaRI and TbetaRII form a heteromeric complex that is most likely a heterotetramer. Antibody-mediated immunofluorescence co-patching of epitope-tagged receptors provides the first evidence in live cells that TbetaRI. TbetaRII complex formation occurs at a low but measurable degree in the absence of ligand, increasing significantly after TGF-beta binding. In addition, we demonstrate that pretreatment of cells with dithiothreitol, which inhibits the binding of TGF-beta to TbetaRI, does not prevent formation of the TbetaRI.TbetaRII complex, but increases its sensitivity to detergent and prevents TGF-beta-activated TbetaRI from phosphorylating Smad3 in vitro. This indicates that either a specific conformation of the TbetaRI. TbetaRII complex, disrupted by dithiothreitol, or direct binding of TGF-beta to TbetaRI is required for signaling. (+info)Gamma-Actinin, a new regulatory protein from rabbit skeletal muscle. I. Purification and characterization. (6/2188)
A new regulatory protein which we have designated as gamma-actinin has been isolated from native thin filaments of rabbit skeletal muscle. Depolymerized native thin filaments were fractionated by salting out with ammonium sulfate, and the precipitates obtained at 40--60% ammonium sulfate saturation were further subjected to DEAE-Sephadex and Sephadex G-200 column chromatography. The purified gamma-actinin was shown to have a chain weight of 35,000 daltons and had a strong inhibitory action on the polymerization of G-actin. The results of amino acid analysis indicated a unique amino acid composition of gamma-actinin as compared with other structural proteins of muscle. Non-polar and neutral amino acid residues were abundant. One cysteine residue was contained per one molecule of gamma-actinin and played a critical role in the maintenance of the inhibitory activity. Pelleting of gamma-actinin with F-actin showed that gamma-actinin binds to F-action. (+info)Phospholipid hydroperoxide cysteine peroxidase activity of human serum albumin. (7/2188)
Human serum albumin (HSA) reduced the phospholipid hydroperoxide, 1-palmitoyl-2-(13-hydroperoxy-cis-9, trans-11-octadecadienoyl)-l-3-phosphatidylcholine (PLPC-OOH) to the corresponding hydroxy-derivative with a high apparent affinity (Km=9. 23+/-0.95 microM). Removal of bound lipid during purification increased this activity. At physiological concentration, HSA reduced the phospholipid hydroperoxide in the absence of a cofactor. However, in the presence of a cofactor (reductant), the rate of the reaction was increased. All of the major aminothiols in plasma could act as reductants, the best being the most abundant, cysteine (Km=600+/-80 microM). For every nanomole of PLPC-OOH reduced by HSA, 1.26 nmol of cystine was formed, indicating a reaction stoichiometry of 1 mol PLPC-OOH to 2 mol cysteine. We used chemical modification to determine which amino acid residues on HSA were responsible for the activity. Oxidation of thiol group(s) by N-ethylmaleimide led to a reduction in the rate of activity, whereas reduction of thiols by either dithiothreitol or the angiotensin-converting enzyme inhibitor, captopril, increased the activity. Both N-ethylmaleimide-modified HSA and dithiothreitol-treated HSA exhibited increased apparent affinities for PLPC-OOH. For a range of preparations of albumin with different modifications, the activity on PLPC-OOH was dependent on the amount of free thiol groups on the albumin (correlation coefficient=0.91). Patients with lowered albumin concentrations after septic shock showed lowered total plasma thiol concentrations and decreased phospholipid hydroperoxide cysteine peroxidase (PHCPx) activities. These results therefore show for the first time that HSA exhibits PHCPx activity, and that the majority of the activity depends on the presence of reduced thiol group(s) on the albumin. (+info)Respiratory chain strongly oxidizes the CXXC motif of DsbB in the Escherichia coli disulfide bond formation pathway. (8/2188)
Escherichia coli DsbB has four essential cysteine residues, among which Cys41 and Cys44 form a CXXC redox active site motif and the Cys104-Cys130 disulfide bond oxidizes the active site cysteines of DsbA, the disulfide bond formation factor in the periplasm. Functional respiratory chain is required for the cell to keep DsbA oxidized. In this study, we characterized the roles of essential cysteines of DsbB in the coupling with the respiratory chain. Cys104 was found to form the inactive complex with DsbA under respiration-defective conditions. While DsbB, under normal aerobic conditions, is in the oxidized state, having two intramolecular disulfide bonds, oxidation of Cys104 and Cys130 requires the presence of Cys41-Cys44. Remarkably, the Cys41-Cys44 disulfide bond is refractory to reduction by a high concentration of dithiothreitol, unless the membrane is solubilized with a detergent. This reductant resistance requires both the respiratory function and oxygen, since Cys41-Cys44 became sensitive to the reducing agent when membrane was prepared from quinone- or heme-depleted cells or when a membrane sample was deaerated. Thus, the Cys41-Val-Leu-Cys44 motif of DsbB is kept both strongly oxidized and strongly oxidizing when DsbB is integrated into the membrane with the normal set of respiratory components. (+info)
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Sulfhydryl Compounds
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Lysis buffer
Add 1 mM fresh dithiothreitol (DTT). ACK (Ammonium-Chloride-Potassium) lysing buffer[edit]. ACK is used for lysis of red blood ...
Reducing agent
Dithiothreitol (DTT) - used in biochemistry labs to avoid S-S bonds. *Carbon monoxide (CO) ...
Disulfide
In biochemistry, thiols such as β-mercaptoethanol (β-ME) or dithiothreitol (DTT) serve as reductants; the thiol reagents are ... Typically, the thiolate of a redox reagent such as glutathione or dithiothreitol attacks the disulfide bond on a protein ...
TST (gene)
1976). "Reaction of rhodanese with dithiothreitol". Biochim. Biophys. Acta. 445 (1): 104-11. doi:10.1016/0005-2744(76)90163-7. ...
Dithioerythritol
It is an epimer of dithiothreitol (DTT). The molecular formula for DTE is C4H10O2S2. Like DTT, DTE makes an excellent reducing ... Cleland, W.W. (April 1964). "Dithiothreitol, A New Protective Reagent for SH Groups". Biochemistry. 3 (4): 480-2. doi:10.1021/ ...
Maleylacetoacetate isomerase
It also binds the sulfate ion and dithiothreitol. Maleylacetoacetate isomerase deficiency is a disease caused by a mutation in ...
List of people from Madison, Wisconsin
biographical article Cleland, W.W. (April 1964). "Dithiothreitol, A New Protective Reagent for SH Groups". Biochemistry. 3 (4 ...
Glycoprotein N-palmitoyltransferase
This enzyme has at least one effector, Dithiothreitol. Liau YH, Slomiany BL, Slomiany A, Piasek A, Palmer D, Rosenthal WS (1985 ...
W. Wallace Cleland
Cleland was well known for being the first to utilize dithiothreitol for the reduction of disulfide bonds in proteins. The ... Cleland, W.W. (April 1964). "Dithiothreitol, A New Protective Reagent for SH Groups". Biochemistry. 3 (4): 480-2. doi:10.1021/ ...
D-ornithine 4,5-aminomutase
It has 3 cofactors: pyridoxal phosphate, Cobamide coenzyme, and Dithiothreitol. Somack R, Costilow RN (1973). "Purification and ...
Radioimmunoprecipitation assay buffer
5-10 mM dithiothreitol (DTT) or β-mercaptoethanol as antioxidant. DTT is more expensive than βME, but its redox potential is ...
Glutathione
The thiols are then reduced with dithiothreitol and labelled by monobromobimane. Monobromobimane becomes fluorescent after ...
Polyphenol oxidase
Another inhibitor of this enzyme is potassium pyrosulphite (K2S2O5). Banana root PPO is strongly inhibited by dithiothreitol ...
Blood compatibility testing
If this is not effective, dithiothreitol can be used to destroy the antibodies.:141 Cord blood samples may be contaminated with ...
Gel electrophoresis
Reducing conditions are usually maintained by the addition of beta-mercaptoethanol or dithiothreitol. For a general analysis of ...
Threitol
Antifreeze protein Dithiothreitol, a thiol derivative of threitol Threitol at Sigma-Alrich Elks, J.; Ganellin, C. R. (1990). ...
Organophosphorus acid anhydrolase
OPAA activity is enhanced by reducing agents such as dithiothreitol (DTT) and beta-mercaptoethanol. OPAA is also catalytically ...
Unfolded protein response
A23187 upregulates expression of ER stress proteins 2-deoxyglucose dithiothreitol reduces the disulfide bridges of proteins. ...
GPX3
The sources of reducing power for GPx-3 in vitro include GSH, cysteine, mercaptoethanol, and dithiothreitol. There is an ...
MPGES-2
The activity of PTGES2 is thought to be increased in the presence of sulfhydryl compounds, in particular dithiothreitol. The ...
Vitamin-K-epoxide reductase (warfarin-sensitive)
4-dithiothreitol Thus, the two substrates of this enzyme are 2-methyl-3-phytyl-1,4-naphthoquinone and oxidized dithiothreitol, ... The systematic name of this enzyme class is 2-methyl-3-phytyl-1,4-naphthoquinone:oxidized-dithiothreitol oxidoreductase. This ... whereas its two products are 2,3-epoxy-2,3-dihydro-2-methyl-3-phytyl-1,4-naphthoquinone and 1,4-dithiothreitol. This enzyme ... oxidized dithiothreitol ⇌ {\displaystyle \rightleftharpoons } 2,3-epoxy-2,3-dihydro-2-methyl-3-phytyl-1,4-naphthoquinone + 1, ...
TCEP
Dithiothreitol will slowly over time absorb more and more light in this spectrum as various redox reactions occur. Ruegg, U.T ... TCEP can keep the cysteines from forming di-sulfide bonds and unlike dithiothreitol and β-mercaptoethanol, it will not react as ... Compared to the other two most common agents used for this purpose (dithiothreitol and β-mercaptoethanol), TCEP has the ... Rhee, S. S.; Burke, D. H. (2004). "Tris(2-carboxyethyl)phosphine stabilization of RNA: comparison with dithiothreitol for use ...
2-Mercaptoethanol
However, since 2-mercaptoethanol forms adducts with free cysteines and is somewhat more toxic, dithiothreitol (DTT) is ... 2-Mercaptoethanol is often used interchangeably with dithiothreitol (DTT) or the odorless tris(2-carboxyethyl)phosphine (TCEP) ...
Violaxanthin de-epoxidase
... effects of dithiothreitol and pepstatin A". Plant & Cell Physiology. 40 (11): 1119-26. doi:10.1093/oxfordjournals.pcp.a029496. ...
Coenzyme A
Free CoA can be regenerated from CoA disulfide and mixed CoA disulfides with reducing agents such as dithiothreitol or 2- ...
Vitamin-K-epoxide reductase (warfarin-insensitive)
The systematic name of this enzyme class is 3-hydroxy-2-methyl-3-phytyl-2,3-dihydronaphthoquinone:oxidized-dithi othreitol ... 4-dithiothreitol. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH or CH2 groups of ... 4-dithiothreitol Thus, the two substrates of this enzyme are 3-hydroxy-2-methyl-3-phytyl-2,3-dihydronaphthoquinone and oxidized ... oxidized dithiothreitol ⇌ {\displaystyle \rightleftharpoons } 2,3-epoxy-2,3-dihydro-2-methyl-3-phytyl-1,4-naphthoquinone + 1, ...
Differential extraction
... uses a chemical called dithiothreitol (DTT) to disrupt the sulfur bonds in the protamines in order to ...
Dithiol
A common 1,4-dithiol is dithiothreitol (DTT), HSCH2CH(OH)CH(OH)CH2SH, sometimes called Cleland's reagent, for to reduce protein ... a vitamin Dithiothreitol, a reagent in protein biochemistry Geminal dithiols have the formula RR'C(SH)2. They are derived from ...
CD38
This can be sidelined by either pretreatment of the erythrocytes with dithiothreitol (DTT) or by using an anti-CD38 antibody ...
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The method is based on the catalytic effect of selenium on the reduction of tetranitro blue tetrazolium by dithiothreitol; it ... N2 - The method is based on the catalytic effect of selenium on the reduction of tetranitro blue tetrazolium by dithiothreitol ... AB - The method is based on the catalytic effect of selenium on the reduction of tetranitro blue tetrazolium by dithiothreitol ... "The method is based on the catalytic effect of selenium on the reduction of tetranitro blue tetrazolium by dithiothreitol; it ...
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Cleland's Reagent2
- Dithiothreitol (DTT) is the common name for a small-molecule redox reagent also known as Cleland's reagent. (wikipedia.org)
- Dithiothreitol, DTT or Cleland's reagent is a small-molecule redox reagent. (glentham.com)
Oxidation2
- Dithiothreitol shelf life can be extended with refrigeration at 2-8 °C. Oxidation presents further complications as oxidized DTT exhibits a strong absorbance peak at 280 nm. (wikipedia.org)
- Due to air oxidation, DL-dithiothreitol (DTT) is a relatively unstable compound whose useful life can be extended by refrigeration and handling in an inert atmosphere. (24marketreports.com)
Reagents1
- Dithiothreitol (DTT) is the common name of the more popular of the two Cleland's Reagents (the other being Dithioerythritol or DTE). (goldbio.com)
EDTA1
- EDTA ), and reducing agents like dithiothreitol (DTT). (wikipedia.org)
Compounds3
- N-acetylcysteine (NAC) and Dithiothreitol (DTT), two compounds that prevent experimental amyotrophic lateral sclerosis (ALS) in the vitamin C - deficient guinea pig[1], were given to patients with motor neuron disease (MND). (springer.com)
- The reduction of disulfide-containing compounds by Dithiothreitol is a two-step reaction. (cfmot.de)
- Dithiol compounds such as dithiothreitol inhibited AA release from both the thimerosal- and the PAO-treated cells, and monothiol compounds (l-Cys and glutathione) decreased the thimerosal response. (biomedsearch.com)
Ligand1
- Dithiothreitol markedly increased the ligand binding affinity of angiotensin II (AII) receptor type II (AT 2 ) without affecting its antagonist selectivity in cultured ovarian granulosa cells, demonstrating that this AT 2 is of the dithiothreitol-sensitive type. (elsevier.com)
Commonly2
- Most commonly, Dithiothreitol is used to reduce disulfide bonds in peptides and proteins. (cfmot.de)
- The most commonly used reductant is dithiothreitol (DTT). (thomassci.com)
Descriptor1
- Dithiothreitol" is a descriptor in the National Library of Medicine's controlled vocabulary thesaurus, MeSH (Medical Subject Headings) . (harvard.edu)
Assay1
- OH) in dithiothreitol (DTT) assay. (illinois.edu)
Proteins1
- Dithiothreitol is an integral reagent, together with denaturants such as GdmCl, for the solubilization of proteins from inclusion bodies. (cfmot.de)
Consumption2
- In consumption market, the global consumption value of DL-dithiothreitol (DTT) increases with the 4.55% average growth rate. (24marketreports.com)
- To study and analyze the global DL-Dithiothreitol (DTT) consumption (value & volume) by key regions /countries, product type and application, history data from 2014 to 2018, and forecast to 2024. (24marketreports.com)
Protective1
- The protective effect of hypoxia and dithiothreitol on X-ray-induced genetic damage in Arabidopsis. (wur.nl)
Concentration1
- Dithiothreitol repairs up to 30% of DNA radicals, but an increase in the thiol concentration above 10 mM, even up to 1000 mM, does not further enhance the overall level of the repair process. (warwick.ac.uk)
Structure1
- To understand the structure of DL-Dithiothreitol (DTT) market by identifying its various subsegments. (24marketreports.com)
Effect2
- Effect of zinc and dithiothreitol (DTT) on LLER oligomerization. (nih.gov)
- The effect of a thiol, dithiothreitol (DTT), on DNA radiolysis at cryogenic temperatures was investigated by the EPR method. (warwick.ac.uk)
Compound1
- Dithiothreitol is the trans isomer of the compound 2,3-dihydroxy-1,4-dithiolbutane. (cfmot.de)
High2
- High efficiency transformation by electroporation of Pichia pastoris pretreated with lithium acetate and dithiothreitol. (nih.gov)
- We conclude that NAT1 expression is not directly regulated by E 2 , DHT, 3 β -adiol, or dithiothreitol despite high NAT1 and ESR1 expression in luminal A breast cancer cells, suggesting that ESR1 , XBP1, and NAT1 expression may share a common transcriptional network arising from the luminal epithelium associated with better survival in breast cancer. (aspetjournals.org)
Terms1
- According to this study, over the next five years the DL-Dithiothreitol (DTT) market will register a 2.5% CAGR in terms of revenue, the global market size will reach US$ 1080 million by 2024, from US$ 950 million in 2019. (24marketreports.com)
Products1
- With reducing action of DL-dithiothreitol (DTT), the downstream application industries will need more DL-dithiothreitol (DTT) products. (24marketreports.com)
Cells3
- Herein, we used low-dose pharmacological UPR inducers such as tunicamycin (TM) and dithiothreitol (DTT) to efficiently activate the IRE1-XBP-1 pathway in myeloma cells characterized by transcriptional expression increase in spliced XBP-1 and molecular chaperons, accompanied by significant differentiation and maturation of these myeloma cells, without concomitant cytotoxicity. (sigmaaldrich.com)
- Dithiothreitol (DTT) effectively suppressed the phenylarsine oxide-inhibited cellular reductive capacity, but unexpectedly, enhanced As 2 O 3 -induced apoptosis in NB4 cells. (aspetjournals.org)
- Dithiothreitol increased levels of the activated, spliced XBP1 in ER α (+) MCF-7 and T47D breast cancer cells but did not affect NAT1 or ESR1 expression. (aspetjournals.org)
Publication1
- This graph shows the total number of publications written about "Dithiothreitol" by people in Harvard Catalyst Profiles by year, and whether "Dithiothreitol" was a major or minor topic of these publication. (harvard.edu)
Method1
- International validation of a dithiothreitol (DTT)-based method to resolve the daratumumab interference with blood compatibility testing. (harvard.edu)
Data2
- DL-Dithiothreitol Market also splits the market by region: Breakdown data in Chapter 4, 5, 6, 7 and 8. (24marketreports.com)
- The key manufacturers covered in DL-Dithiothreitol Market : Breakdown data in in Chapter 3. (24marketreports.com)
Addition2
- In addition, DL-Dithiothreitol Market discusses the key drivers influencing market growth, opportunities, the challenges and the risks faced by key manufacturers and the market as a whole. (24marketreports.com)
- Acid treatment of influenza A and B virus preparations followed by addition of dithiothreitol (DTT) and centrifugation through a sucrose cushion removes the HA1 subunit of hemagglutinin from virus. (nih.gov)
Overview1
- DL-Dithiothreitol Market presents a comprehensive overview, market shares, and growth opportunities of DL-Dithiothreitol (DTT) market by product type, application, key manufacturers and key regions and countries. (24marketreports.com)
Levels1
- Dithiothreitol is useful for specifically detecting low levels of the AT 2 in the ovary, where it plays roles that are probably related to atresia. (elsevier.com)
Patients1
- Chisholm KM, Getsinger D, Vaughan W, Hwang PH, Banaei N. Pretreatment of sinus aspirates with dithiothreitol improves yield of fungal cultures in patients with chronic sinusitis. (harvard.edu)
Potential1
- So, DL-dithiothreitol (DTT) has a huge market potential in the future. (24marketreports.com)