464 Results for: "Redox-"

Supplier: Bioss

Increases cell migration by inducing filopodia formation at the leading edge of migrating cells. Plays a role in regulation of apoptosis, possibly through control of CASP3. May be involved in a redox-related process (By similarity).

Supplier: Bioss

Plays a role as a glutathione (GSH)-dependent antioxidant. May be involved in a redox-related process. May play a role in the myopathies of selenium deficiency.

Supplier: Bioss

Involved in redox regulation of the cell. Protects radical-sensitive enzymes from oxidative damage by a radical-generating system. Acts synergistically with MAP3K13 to regulate the activation of NF-kappa-B in the cytosol.

Supplier: Bioss

Ribonuclease inhibitor which inhibits RNASE1, RNASE2 and ANG. May play role in redox homeostasis.

Supplier: Bioss

Ribonuclease inhibitor which inhibits RNASE1, RNASE2 and ANG. May play role in redox homeostasis.

Supplier: Bioss

Ribonuclease inhibitor which inhibits RNASE1, RNASE2 and ANG. May play role in redox homeostasis.

Supplier: PanReac AppliChem

DNA/RNA-ExitusPlus™ activity test is a quick and convenient tool to test the activity of PanReac AppliChem solutions for nucleic acid decontamination DNA/RNA-ExitusPlus™(A7089), DNA/RNA-ExitusPlus™ IF (A7409) and RNase-ExitusPlus™ (A7153). The test strips are very sensitive and designed to detect the redox reaction of DNA/RNA-ExitusPlus™ solutions.

Supplier: Apollo Scientific

Redox indicator.

Supplier: Bel-Art Products, a Part of SP

This handy rack made from PP holds eight test tubes for storing and conditioning pH and ion electrodes.

Supplier: Bioss

Plays a key role in regulating maximal capacity for electron transport and oxidative phosphorylation (By similarity). May be involved in Fe-S cluster shuttling and/or in redox reactions.

Supplier: Bioss

May act as a redox regulator involved in DUOX proteins folding. The interaction with DUOX1 and DUOX2 suggest that it belongs to a multiprotein complex constituting the thyroid H₂O₂ generating system. It is however not sufficient to assist DUOX1 and DUOX2 in H₂O₂ generation.

Supplier: Bioss

Involved in redox regulation of the cell. Protects radical-sensitive enzymes from oxidative damage by a radical-generating system. Acts synergistically with MAP3K13 to regulate the activation of NF-kappa-B in the cytosol.

Supplier: Bioss

Calcium-dependent NADPH oxidase that generates superoxide. Also functions as a calcium-dependent proton channel and may regulate redox-dependent processes in lymphocytes and spermatozoa. May play a role in cell growth and apoptosis.

Supplier: Bioss

Increases cell migration by inducing filopodia formation at the leading edge of migrating cells. Plays a role in regulation of apoptosis, possibly through control of CASP3. May be involved in a redox-related process (By similarity).

Supplier: SELENOZYME

The human TrxR2 selenoprotein is encoded by the TXNRD2 gene and exerts a wide range of functions in mitochondrial redox control and antioxidant systems. We provide the main mitochondrial isoform of the human TrxR2 enzyme with more than 90% Sec contents and more than 95% purity in aliquots at amounts from 5 to 50 units.

Supplier: Apollo Scientific

Tetrazolium dye which produces a fluorescent formazandye in coupled redox reactions

Supplier: Thermo Fisher Scientific

3,4-Ethylenedioxythiophene is used as a monomer to synthesise the conductive polymers and used as a reductant in the one-pot synthesis of gold nanoparticles from chloroauric acid, as starting material used in palladium-catalysed mono and bis-arylation reactions and in the synthesis of conjugated polymers and copolymers, with potential optical applications. It is also used in redox activity, electroactivity and conductivity.

Supplier: Bioss

Increases cell migration by inducing filopodia formation at the leading edge of migrating cells. Plays a role in regulation of apoptosis, possibly through control of CASP3. May be involved in a redox-related process (By similarity).

Supplier: Bioss

May act as a redox regulator involved in DUOX proteins folding. The interaction with DUOX1 and DUOX2 suggest that it belongs to a multiprotein complex constituting the thyroid H(2)O(2) generating system. It is however not sufficient to assist DUOX1 and DUOX2 in H(2)O(2) generation.

Supplier: Bioss

Calcium-dependent NADPH oxidase that generates superoxide. Also functions as a calcium-dependent proton channel and may regulate redox-dependent processes in lymphocytes and spermatozoa. May play a role in cell growth and apoptosis.

Supplier: Bioss

Increases cell migration by inducing filopodia formation at the leading edge of migrating cells. Plays a role in regulation of apoptosis, possibly through control of CASP3. May be involved in a redox-related process (By similarity).

Supplier: Bioss

Increases cell migration by inducing filopodia formation at the leading edge of migrating cells. Plays a role in regulation of apoptosis, possibly through control of CASP3. May be involved in a redox-related process (By similarity).

Supplier: Bioss

Calcium-dependent NADPH oxidase that generates superoxide. Also functions as a calcium-dependent proton channel and may regulate redox-dependent processes in lymphocytes and spermatozoa. May play a role in cell growth and apoptosis.

Supplier: Bioss

DnaJ-like proteins interact with HSP 70 molecular chaperones and function to facilitate protein folding and mitochondrial protein import. HSP 40-4, also known as HDJ2, is the human DnaJ homolog that functions as a co-chaperone with a cysteine-rich zinc finger domain. The cellular redox enzyme thioredoxin interacts with HSP 40-4, and oxidation and reduction reversibly regulate HSP 40-4 function in response to the changing redox states of the cell. The zinc finger domain of HSP 40-4 may act as a redox sensor of chaperone-mediated protein-folding machinery, since HSP 40-4 inactivation leads to the oxidation of cysteine thiols and a simultaneous release of coordinated zinc. Loss of the HSP 40-4 protein may be linked to severe defects in spermatogenesis that involve aberrant androgen signaling.

Supplier: Bioss

Thioredoxins (Trx) are small, multi-functional proteins with oxidoreductase activity and are ubiquitous in essentially all living cells. Trx contains a redox-active disulfide/dithiol group within the conserved Cys-Gly-Pro-Cys active site. The two cysteine residues in the conserved active centers can be oxidized to form intramolecular disulfide bonds. Reduction of the active site disulfide in oxidized Trx is catalyzed by Trx reductase with NADPH as the electron donor. The reduced Trx is a hydrogen donor for ribonucleotide reductase, the essential enzyme for DNA synthesis, and a potent general protein disulfide reductase with numerous functions in growth and redox regulations. Specific protein disulfide targets for reduction by Trx include protein disulfide isomerase(PDI) and a number of transcription factors such as p53, NF-kB and AP-1. Trx is also capable of removing H2O2, particularly when it is coupled with either methionine sulfoxide reductase or several isoforms of peroxiredoxins.

Supplier: Bioss

Calcium-dependent NADPH oxidase that generates superoxide. Also functions as a calcium-dependent proton channel and may regulate redox-dependent processes in lymphocytes and spermatozoa. May play a role in cell growth and apoptosis.

Supplier: Bioss

May act as a redox regulator involved in DUOX proteins folding. The interaction with DUOX1 and DUOX2 suggest that it belongs to a multiprotein complex constituting the thyroid H(2)O(2) generating system. It is however not sufficient to assist DUOX1 and DUOX2 in H(2)O(2) generation.

Supplier: Bioss

May act as a redox regulator involved in DUOX proteins folding. The interaction with DUOX1 and DUOX2 suggest that it belongs to a multiprotein complex constituting the thyroid H(2)O(2) generating system. It is however not sufficient to assist DUOX1 and DUOX2 in H(2)O(2) generation.

Supplier: Merck

2,6-Dichloroindophenol sodium salt hydrate is a blue redox dye.

Supplier: Bioss

Multifunctional protein that plays a central role in the cellular response to oxidative stress. The two major activities of APEX1 in DNA repair and redox regulation of transcriptional factors. Functions as a apurinic/apyrimidinic (AP) endodeoxyribonuclease in the DNA base excision repair (BER) pathway of DNA lesions induced by oxidative and alkylating agents. Initiates repair of AP sites in DNA by catalyzing hydrolytic incision of the phosphodiester backbone immediately adjacent to the damage, generating a single-strand break with 5'-deoxyribose phosphate and 3'-hydroxyl ends. Does also incise at AP sites in the DNA strand of DNA/RNA hybrids, single-stranded DNA regions of R-loop structures, and single-stranded RNA molecules. Has a 3'-5' exoribonuclease activity on mismatched deoxyribonucleotides at the 3' termini of nicked or gapped DNA molecules during short-patch BER. Possesses a DNA 3' phosphodiesterase activity capable of removing lesions (such as phosphoglycolate) blocking the 3' side of DNA strand breaks. May also play a role in the epigenetic regulation of gene expression by participating in DNA demethylation. Acts as a loading factor for POLB onto non-incised AP sites in DNA and stimulates the 5'-terminal deoxyribose 5'-phosphate (dRp) excision activity of POLB. Plays a role in the protection from granzymes-mediated cellular repair leading to cell death. Also involved in the DNA cleavage step of class switch recombination (CSR). On the other hand, APEX1 also exerts reversible nuclear redox activity to regulate DNA binding affinity and transcriptional activity of transcriptional factors by controlling the redox status of their DNA-binding domain, such as the FOS/JUN AP-1 complex after exposure to IR. Involved in calcium-dependent down-regulation of parathyroid hormone (PTH) expression by binding to negative calcium response elements (nCaREs).