Cy5 maleimide labelling for sensitive detection of free thiols in native protein extracts: identification of seed proteins...
Barley thioredoxin h isoforms HvTrxh1 and HvTrxh2 differ in temporal and spatial distribution and in kinetic properties. Target proteins of HvTrxh1 and HvTrxh2 were identified in mature seeds and in seeds after 72 h of germination. Improvement of the established method for identification of thioredoxin-targeted proteins based on two-dimensional electrophoresis and fluorescence labelling of thiol groups was achieved by application of a highly sensitive Cy5 maleimide dye and large-format two-dimensional gels, resulting in a 10-fold increase in the observed number of labelled protein spots. The technique also provided information about accessible thiol groups in the proteins identified in the barley seed proteome. In total, 16 different putative target proteins were identified from 26 spots using tryptic in-gel digestion, matrix-assisted laser-desorption ionization-time-of-flight MS and database search. HvTrxh1 and HvTrxh2 were shown to have similar target specificity. Barley ...http://www.biochemj.org/content/378/2/497
The tert-butylhydroquinone-mediated activation of the human thioredoxin gene reveals a novel promoter structure | Biochemical...
Thioredoxin is a redox-active protein that plays multiple roles in regulating cell growth, cell signalling and apoptosis. Here, we have demonstrated that a complex mechanism involving multiple regulatory elements is involved in the tBHQ [tert-butylhydroquinone or 2,5-di-(t-butyl)-1,4-hydroquinone]-mediated activation of the thioredoxin gene. Luciferase assays, utilizing various wild-type and mutated thioredoxin promoter fragments, revealed roles for the ORE (oxidative stress responsive element), ARE (antioxidant responsive element), three Sp1 (specificity protein 1)-binding sites and the TATA box in the activation of the thioredoxin gene by tBHQ. The ORE required the presence of the ARE to elicit its response, whereas the independent removal of three Sp1-binding sites and the TATA box also decreased activation of the thioredoxin gene, with mutation of the TATA box having the greatest effect. Real-time RT (reverse ...http://www.biochemj.org/content/398/2/269
RCSB PDB - 1EP8: CRYSTAL STRUCTURE OF A MUTATED THIOREDOXIN, D30A, FROM CHLAMYDOMONAS REINHARDTII Macromolecule...
1EP8: Crystal structure of the wild-type and D30A mutant thioredoxin h of Chlamydomonas reinhardtii and implications for the catalytic mechanism.http://www.rcsb.org/pdb/explore/derivedData.do?structureId=1EP8
Analysis of Arabidopsis thioredoxin-h isotypes identifies discrete domains that confer specific structural and functional...
Multiple isoforms of Arabidopsis thaliana h-type thioredoxins (AtTrx-hs) have distinct structural and functional specificities. AtTrx-h3 acts as both a disulfide reductase and as a molecular chaperone. We prepared five representative AtTrx-hs and compared their protein structures and disulfide reductase and molecular chaperone activities. AtTrx-h2 with an N-terminal extension exhibited distinct functional properties with respect to other AtTrx-hs. AtTrx-h2 formed low-molecular-mass structures and exhibited only disulfide reductase activity, whereas the other AtTrx-h isoforms formed high-molecular-mass complexes and displayed both disulfide reductase and molecular chaperone activities. The domains that determine the unique structural and functional properties of each AtTrx-hs protein were determined by constructing a domain-swap between the N- and C-terminal regions of AtTrx-h2 and AtTrx-h3 (designated AtTrx-h-2N3C and AtTrx-h-3N2C respectively), an N-terminal deletion mutant of AtTrx-h2 ...http://www.biochemj.org/content/456/1/13
A "Control Workgroup" Of Twenty-Four Protein Targets Used To Test Platform Changes David J. Aceti Center for Eukaryotic...
#ORF IDProtein NameSource OrganismMWAssay cytoplasmic dynein light chainM. musculus unknown protein At1g A. thaliana thioredoxin h1A. thaliana12673 Spec assay following NADPH/insulin-DS redox reaction zinc finger proteinH. sapiens unknown heme-binding proteinC. merolae16474Red-colored from heme binding 62361unknown protein At1g A. thaliana unknown protein At3g A. thaliana thioredoxin-like proteinA. thaliana allene oxide cyclase variant1A. thaliana allene oxide cyclase variant2A. thaliana cysteine dioxygenase 1M. musculus23026HLPC assay for cysteine sulfinic acid formation 12605phosphataseA. thaliana24537pNPP phosphatase assay Enhanced C3 green fluorescent proteinA. victoria26748Green/fluorescent TEV proteaseTobacco etch virus26922Fluoresence anisotropy-based protease assay Pre-mRNA processing factor 24S. cerevisiae27223Gel mobility shift assay sarcosine dimethylglycine methyltransferaseG. sulphuraria33324 Coupled spec. assay following deamination of adenine ...http://slideplayer.com/slide/4340049/
Sptrx-2, a fusion protein composed of one thioredoxin and three tandemly repeated NDP-kinase domains is expressed in human...
BACKGROUND: Thioredoxins (Trx) are small redox proteins that function as general protein disulphide reductases and regulate several cellular processes such as transcription factor DNA binding activity, apoptosis and DNA synthesis. In mammalian organisms, thioredoxins are generally ubiquitously expressed in all tissues, with the exception of Sptrx-1 which is specifically expressed in sperm cells.. RESULTS: We report here the identification and characterization of a novel member of the thioredoxin family, the second with a tissue-specific distribution in human sperm, termed Sptrx-2. The Sptrx-2 ORF (open reading frame) encodes for a protein of 588 amino acids with two different domains: an N-terminal thioredoxin domain encompassing the first 105 residues and a C-terminal domain composed of three repeats of a NDP kinase domain. The Sptrx-2 gene spans about 51 kb organized in 17 exons and maps at locus 7p13-14. Sptrx-2 mRNA is exclusively ...http://liu.diva-portal.org/smash/record.jsf?pid=diva2:655954
Interaction of mitochondrial thioredoxin with glucocorticoid receptor and NF-κB modulates glucocorticoid receptor and NF-κB...
Trx2 (mitochondrial thioredoxin) is an antioxidant and anti-apoptotic factor essential for cell viability. Trx1 (cytoplasmic thioredoxin) is a co-factor and regulator of redox-sensitive transcription factors such as the GR (glucocorticoid receptor) and NF-κB (nuclear factor κB). Both transcription factors have been detected in mitochondria and a role in mitochondrial transcription regulation and apoptosis has been proposed. In the present study, we show using SPR (surface plasmon resonance) and immunoprecepitation that GR and the p65 subunit of NF-κB are Trx2-interacting proteins. The interaction of Trx2 with GR is independent of the presence of GR ligand and of redox conditions. The p65 subunit of NF-κB can interact with Trx2 in the oxidized, but not the reduced, form. Using HEK (human embryonic kidney)-293 cell lines with increased or decreased expression of Trx2, we show that Trx2 modulates transcription of GR and NF-κB reporter genes. Moreover, Trx2 overexpression ...http://www.biochemj.org/content/422/3/521
Thioredoxin reductase - Wikipedia
Thioredoxin reductases (TR, TrxR) (EC 184.108.40.206) are the only known enzymes to reduce thioredoxin (Trx). Two classes of thioredoxin reductase have been identified: one class in bacteria and some eukaryotes and one in animals. Both classes are flavoproteins which function as homodimers. Each monomer contains a FAD prosthetic group, a NADPH binding domain, and an active site containing a redox-active disulfide bond. Thioredoxin reductase is the only enzyme known to catalyze the reduction of thioredoxin and hence is a central component in the thioredoxin system. Together with thioredoxin (Trx) and NADPH this system's most general description is as a method of forming reduced disulfide bonds in cells. Electrons are taken from NADPH via TrxR and are transferred to the active site of Trx, which goes on to reduce protein disulfides or other substrates. The Trx system exists in all living cells and ...https://en.wikipedia.org/wiki/Thioredoxin_reductase
A biochemical analysis of the interaction of victorin and oats
Victoria blight of oats is caused by the fungus Cochhobolus victoriae. This fungus is pathogenic due to its ability to produce the host-selective toxin victorin. Previously, a 100-kD protein that binds victorin in vivo only in susceptible genotypes was identified as the P protein of the glycine decarboxylase complex (GDC). Victorin is a potent in vivo inhibitor of GDC. Leaf slices pretreated with victorin displayed an effective Victorin inhibited the concentration for 50% inhibition (EC₅₀) of 81 μM for GDA. glycine-bicarbonate exchange reaction in vitro with an EC₅₀ of 23 μM. We also identified a 15-kD mitochondrial protein in susceptible and resistant genotypes that hound victorin. Amino acid sequence analysis indicated this protein is the H protein component of the GDC. Thus, victorin specifically binds to two components of the GDC. Victorin had no detectable effect on GDC in isolated mitochondria, apparently due to the inability of isolated mitochondria to import victorin. The ...https://ir.library.oregonstate.edu/concern/graduate_thesis_or_dissertations/w0892f948
Pullulanase - Wikipedia
Pullulanase (EC 220.127.116.11, limit dextrinase, amylopectin 6-glucanohydrolase, bacterial debranching enzyme, debranching enzyme, alpha-dextrin endo-1,6-alpha-glucosidase, R-enzyme, pullulan alpha-1,6-glucanohydrolase) is a specific kind of glucanase, an amylolytic exoenzyme, that degrades pullulan. It is produced as an extracellular, cell surface-anchored lipoprotein by Gram-negative bacteria of the genus Klebsiella. Type I pullulanases specifically attack α-1,6 linkages, while type II pullulanases are also able to hydrolyse α-1,4 linkages. It is also produced by some other bacteria and archaea. Pullulanase is used as a processing aid in grain processing biotechnology (production of ethanol and sweeteners). Pullulanase is also known as pullulan-6-glucanohydrolase (Debranching enzyme). Its substrate, pullulan, is regarded as a chain of maltotriose units linked by alpha-1,6-glycosidic bonds. Pullulanase will hydrolytically cleave pullulan (alpha-glucan polysaccharides). Lee, E.Y.C.; Whelan, W.J. ...https://en.wikipedia.org/wiki/Pullulanase
Phage display identifies thioredoxin and superoxide dismutase as novel protein kinase C-interacting proteins: thioredoxin...
Using phage display we identify the redox proteins thioredoxin and superoxide dismutase (SOD) as novel protein kinase C (PKC)-interacting proteins. Overlay assays demonstrated that PKC bound to immobilized thioredoxin, providing supporting evidence for the phage display results. Kinase assays demonstrated that SOD and thioredoxin were not direct substrates for PKC but that both proteins blocked autophosphorylation of PKC. Moreover, thioredoxin inhibited PKC-mediated phosphorylation of histone (IC50of approx. 20 ng/ml).. ...http://www.biochemj.org/content/343/2/301
Thioredoxin system in normal and transformed human cells
Background: Thioredoxin (Trx) and thioredoxin reductase (TrxR), together with NADPH, constitute the Trx system, a major antioxidant entity that helps maintain a reducing environment within living cells. Trx designates a family of proteins that are related on the basis of structure and function. Human full-length Trx is a 12 kDa redox-active protein that contains the evolutionarily conserved active site sequence Cys-Gly Pro-Cys. Truncated Trx is a shorter, 10 kDa form of human Trx that shows complete homology to the N-terminal 80 or 84 amino acids of 12 kDa Trx. Truncated Trx displays no reducing activity, even though it contains an intact active site. Human TrxR is a homodimeric, FAD-containing, selenoprotein that reduces oxidized Trx back to the enzymatically active form by consuming NADPH. Expression of human Trx and TrxR is induced by a variety of stressors. The Trx system functions directly and indirectly in important biological features such as DNA synthesis, gene ...http://liu.diva-portal.org/smash/record.jsf?pid=diva2:246255
Differential thioredoxin reductase activity from human normal...
Differential thioredoxin reductase activity from human normal hepatic and hepatoma cell lines.: Thioredoxin reductase (TrxR), a component of the thioredoxin syshttps://www.mysciencework.com/publication/show/differential-thioredoxin-reductase-activity-from-human-normal-hepatic-hepatoma-cell-lines-1340108b
KEGG ENZYME: 18.104.22.168
This enzyme, like EC 22.214.171.124 (amylo-alpha-1,6-glucosidase), can release an alpha-1->6-linked glucose, whereas the shortest chain that can be released by EC 126.96.36.199 (pullulanase), EC 188.8.131.52 (limit dextrinase), and EC 184.108.40.206 (isoamylase) is maltose. It also hydrolyses isomaltulose (palatinose), isomaltotriose and panose, but has no action on glycogen or phosphorylase limit dextrin. The enzyme from intestinal mucosa is a single polypeptide chain that also catalyses the reaction of EC 220.127.116.11 (sucrose alpha-glucosidase). Differs from EC 18.104.22.168 (amylo-alpha-1,6-glucosidase) in its preference for short-chain substrates and in its not requiring the 6-glucosylated residue to be at a branch point, i.e. linked at both C-1 and C-4 ...http://www.genome.jp/dbget-bin/www_bget?ec:22.214.171.124
Thioredoxins Summary Report | CureHunter
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.http://www.curehunter.com/public/keywordSummaryD013879-Thioredoxins.do
Thioredoxin Detection: ELISAs and Antibodies
The Thioredoxin Assay is a thioredoxin ELISA that can measure soluble human thioredoxin protein in serum, EDTA-plasma, urine or cell culturehttp://www.clontech.com/US/Products/Cell_Biology_and_Epigenetics/Cancer_and_Inflammation/Thioredoxin?sitex=10020:22372:US&PEBCL1=XycBPS5ep01D5HH439enKFKVt4&PEBCL1_pses=ZG278E2D79FD678EB2D804BB908D210D3123EBB45E18C2294CEDB12ED10DBAA4BDB1C8BBE730EDBF31523584EF681CEF3707077E50534BDEC8
Thioredoxin Detection: ELISAs and Antibodies
The Thioredoxin Assay is a thioredoxin ELISA that can measure soluble human thioredoxin protein in serum, EDTA-plasma, urine or cell culturehttp://www.clontech.com/US/Products/Cell_Biology_and_Epigenetics/Cancer_and_Inflammation/Thioredoxin?sitex=10020:22372:US&PEBCL1=ZyGV5ASUEyim1V4kqlSbhHqcD5&PEBCL1_pses=ZGFA966EA6E6F95E0D39F28E378D3AD6A1B2926C74D032F0C1776C8A8C896BB52A1F998C6EFBFFD1ED58CA74061B55E8648D0FB7F336926CA2
Anti-NtrC thioredoxin reductase antibody
Chlamydomonas NtrC antibody, thioredoxin reductase plant antibody, Ntrc antibodies, thioredoxin reductase antibodyThioredoxin Reductase (TR, TrxR) is the only known enzyme (EC 126.96.36.199) which is reducing thoredoxin (Trx). Activity of thoredoxin is essentihttp://www.agrisera.com/en/artiklar/ntrc-thioredoxin-reductase-tr-trxr.html
Thioredoxin Reductase - AR10712PU-S | acris-antibodies.com
Thioredoxin Reductase, 5 µg. |p class='db_paraghraph'|Thioredoxin reductase (TrxR/NTR), an enzyme belonging to the flavoprotein family of pyridine nucleotide-disulfide oxidoreductases.https://www.acris-antibodies.com/proteins-growth-factors/thioredoxin-reductase-ar10712pu-s.htm
BSE Info - Unusual BSE Types
Representation of Western blots of the two major types of unusual/atypical BSE. M.W., molecular weight in kilodaltons; L type, "low molecular" pattern; H type, "high molecular" pattern.5. The H-type was named for the high molecular mass of the unglycosylated isoform of the PrPSc in Western blots. Not much is known about the distribution of PrPSc in the brain of H-type cases, but it appears that the staining intensity for PrPSc is less intense when compared to classical BSE cases. The H-type was first reported in France7. Additional cases have been found in Germany3, the Netherlands8, Sweden8, Switzerland9, Canada3 and the United Kingdom10. The two cases of BSE from animals born and raised in the United States display characteristics of H-type BSE cases11 and were discovered through the active surveillance program for classical BSE; the animals did not enter the food chain. ...http://bseinfo.org/unusualbsetypes.aspx
TXNRD2 - Thioredoxin reductase 2, mitochondrial precursor - Homo sapiens (Human) - TXNRD2 gene & protein
Maintains thioredoxin in a reduced state. Implicated in the defenses against oxidative stress. May play a role in redox-regulated cell signaling.http://www.uniprot.org/uniprot/Q9NNW7
Recombinant S. cerevisiae Thioredoxin / TRX protein (ab82731) References
References for Abcam's Recombinant |em|S. cerevisiae|/em| Thioredoxin / TRX protein (ab82731). Please let us know if you have used this product in your…http://www.abcam.com/recombinant-s-cerevisiae-thioredoxin-trx-protein-ab82731-references.html
Gentaur Molecular :Abfron \ Thioredoxin 1, Yeast, Protein \ LF-P0036
Gentaur molecular products has all kinds of products like :search , Abfron \ Thioredoxin 1, Yeast, Protein \ LF-P0036 for more molecular products just contact ushttp://www.antibody-antibodies.com/product_det.php?id=3045897&supplier=search&name=Thioredoxin%201,%20Yeast,%20Protein
SAUSA300 RS11395 - AureoWiki
Cellular processesCellular processesDetoxificationarsenate reductase (thioredoxin) (TIGR02691; EC 1.20.4.-,188.8.131.52; HMM-score: 28.3) ...http://aureowiki.med.uni-greifswald.de/SAUSA300_RS11395
XML Refactoring Tool adds xml attributes - Oxygen XML Forum
topicref keyref='g_1080p' type='glossentry' xra:oxy_AttrWS__oxy_ln_keys=' ###true' xra:oxy_AttrWS__oxy_ln_type=' ###true' xra:oxy_AttrWS__oxy_ln_href=' ###true' xra:oxy_StartTagInfo='#true' xra:oxy__attributes_order='keys type href' xra:oxy_oValue__oxy_ln_keys='g_1080p' xra:oxy_nonNormValue__oxy_ln_keys='g_1080p' xra:oxy_oValue__oxy_ln_type='glossentry' xra:oxy_nonNormValue__oxy_ln_type='glossentry' xra:oxy_oValue__oxy_ln_href='g_1080p.xml' xra:oxy_nonNormValue__oxy_ln_href='g_1080p.xml ...https://www.oxygenxml.com/forum/post41060.html