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1,1-Diphenylhydrazin+Hydrochlorid
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1,1-Diphenylhydrazin+Hydrochlorid
Lieferant:
Cytiva
Beschreibung:
GSTrap™ 4B sind mit Glutathion Sepharose™ 4B vorgepackte Säulen, die eine bequeme Aufreinigung mit hoher Kapazität von GST-markierten Proteinen ermöglichen.
Artikel-Nr:
(ABNOMAB6676)
Lieferant:
Abnova
Hersteller-Artikelnummer::
MAB6676
Lokale Artikelnummer::
ABNOMAB6676
Beschreibung:
Mouse monoclonal antibody raised against Glutathione.
VE:
1 * 50 µG
Artikel-Nr:
(BOSSBS-3896R)
Lieferant:
Bioss
Hersteller-Artikelnummer::
BS-3896R
Lokale Artikelnummer::
BOSSBS-3896R
Beschreibung:
Superoxide dismutase (SOD) is an antioxidant enzyme involved in the defense system against reactive oxygen species (ROS). SOD catalyzes the dismutation reaction of superoxide radical anion (O2-) to hydrogen peroxide, which is then catalyzed to innocuous O2 and H2O by glutathione peroxidase and catalase. Several classes of SOD have been identified. These include intracellular copper, zinc SOD (Cu, Zn-SOD/SOD-1), mitochondrial manganese SOD (Mn-SOD/SOD-2) and extracellular Cu, Zn-SOD (EC-SOD/SOD-3). SOD1 is found in all eukaryotic species as a homodimeric 32 kDa enzyme containing one each of Cu and Zn ion per subunit. The manganese containing 80 kDa tetrameric enzyme SOD2, is located in the mitochondrial matrix in close proximity to a primary endogenous source of superoxide, the mitochondrial respiratory chain. SOD3 is a heparin-binding multimer of disulfide-linked dimers, primarily expressed in human lungs, vessel walls and airways. SOD4 is a copper chaperone for superoxide dismutase (CCS), which specifically delivers Cu to copper/zinc superoxide dismutase. CCS may activate copper/zinc superoxide dismutase through direct insertion of the Cu cofactor.
VE:
1 * 100 µl
Artikel-Nr:
(PRSI30-147)
Lieferant:
ProSci Inc.
Hersteller-Artikelnummer::
30-147
Lokale Artikelnummer::
PRSI30-147
Beschreibung:
CTH is a cytoplasmic enzyme in the trans-sulfuration pathway that converts cystathione derived from methionine into cysteine. Glutathione synthesis in the liver is dependent upon the availability of cysteine. Mutations in its gene cause cystathioninuria.This gene encodes a cytoplasmic enzyme in the trans-sulfuration pathway that converts cystathione derived from methionine into cysteine. Glutathione synthesis in the liver is dependent upon the availability of cysteine. Mutations in this gene cause cystathioninuria. Alternative splicing of this gene results in two transcript variants encoding different isoforms.
VE:
1 * 100 µG
Artikel-Nr:
(BOSSBS-3896R-CY5.5)
Lieferant:
Bioss
Hersteller-Artikelnummer::
BS-3896R-CY5.5
Lokale Artikelnummer::
BOSSBS-3896R-CY5.5
Beschreibung:
Superoxide dismutase (SOD) is an antioxidant enzyme involved in the defense system against reactive oxygen species (ROS). SOD catalyzes the dismutation reaction of superoxide radical anion (O2-) to hydrogen peroxide, which is then catalyzed to innocuous O2 and H2O by glutathione peroxidase and catalase. Several classes of SOD have been identified. These include intracellular copper, zinc SOD (Cu, Zn-SOD/SOD-1), mitochondrial manganese SOD (Mn-SOD/SOD-2) and extracellular Cu, Zn-SOD (EC-SOD/SOD-3). SOD1 is found in all eukaryotic species as a homodimeric 32 kDa enzyme containing one each of Cu and Zn ion per subunit. The manganese containing 80 kDa tetrameric enzyme SOD2, is located in the mitochondrial matrix in close proximity to a primary endogenous source of superoxide, the mitochondrial respiratory chain. SOD3 is a heparin-binding multimer of disulfide-linked dimers, primarily expressed in human lungs, vessel walls and airways. SOD4 is a copper chaperone for superoxide dismutase (CCS), which specifically delivers Cu to copper/zinc superoxide dismutase. CCS may activate copper/zinc superoxide dismutase through direct insertion of the Cu cofactor.
VE:
1 * 100 µl
Artikel-Nr:
(BOSSBS-3896R-CY5)
Lieferant:
Bioss
Hersteller-Artikelnummer::
BS-3896R-CY5
Lokale Artikelnummer::
BOSSBS-3896R-CY5
Beschreibung:
Superoxide dismutase (SOD) is an antioxidant enzyme involved in the defense system against reactive oxygen species (ROS). SOD catalyzes the dismutation reaction of superoxide radical anion (O2-) to hydrogen peroxide, which is then catalyzed to innocuous O2 and H2O by glutathione peroxidase and catalase. Several classes of SOD have been identified. These include intracellular copper, zinc SOD (Cu, Zn-SOD/SOD-1), mitochondrial manganese SOD (Mn-SOD/SOD-2) and extracellular Cu, Zn-SOD (EC-SOD/SOD-3). SOD1 is found in all eukaryotic species as a homodimeric 32 kDa enzyme containing one each of Cu and Zn ion per subunit. The manganese containing 80 kDa tetrameric enzyme SOD2, is located in the mitochondrial matrix in close proximity to a primary endogenous source of superoxide, the mitochondrial respiratory chain. SOD3 is a heparin-binding multimer of disulfide-linked dimers, primarily expressed in human lungs, vessel walls and airways. SOD4 is a copper chaperone for superoxide dismutase (CCS), which specifically delivers Cu to copper/zinc superoxide dismutase. CCS may activate copper/zinc superoxide dismutase through direct insertion of the Cu cofactor.
VE:
1 * 100 µl
Artikel-Nr:
(PRSI29-608)
Lieferant:
ProSci Inc.
Hersteller-Artikelnummer::
29-608
Lokale Artikelnummer::
PRSI29-608
Beschreibung:
Gamma-glutamyl transpeptidase is a membrane-bound protein that is important in the metabolism of glutathione. The protein is similar in sequence to several members of the gamma-glutamyl transpeptidase family.Gamma-glutamyl transpeptidase is a membrane-bound protein that is important in the metabolism of glutathione. The protein encoded by this gene is similar in sequence to several members of the gamma-glutamyl transpeptidase family. Three transcript variants encoding the same protein have been found for this gene.
VE:
1 * 100 µG
Artikel-Nr:
(BOSSBS-3896R-A350)
Lieferant:
Bioss
Hersteller-Artikelnummer::
BS-3896R-A350
Lokale Artikelnummer::
BOSSBS-3896R-A350
Beschreibung:
Superoxide dismutase (SOD) is an antioxidant enzyme involved in the defense system against reactive oxygen species (ROS). SOD catalyzes the dismutation reaction of superoxide radical anion (O2-) to hydrogen peroxide, which is then catalyzed to innocuous O2 and H2O by glutathione peroxidase and catalase. Several classes of SOD have been identified. These include intracellular copper, zinc SOD (Cu, Zn-SOD/SOD-1), mitochondrial manganese SOD (Mn-SOD/SOD-2) and extracellular Cu, Zn-SOD (EC-SOD/SOD-3). SOD1 is found in all eukaryotic species as a homodimeric 32 kDa enzyme containing one each of Cu and Zn ion per subunit. The manganese containing 80 kDa tetrameric enzyme SOD2, is located in the mitochondrial matrix in close proximity to a primary endogenous source of superoxide, the mitochondrial respiratory chain. SOD3 is a heparin-binding multimer of disulfide-linked dimers, primarily expressed in human lungs, vessel walls and airways. SOD4 is a copper chaperone for superoxide dismutase (CCS), which specifically delivers Cu to copper/zinc superoxide dismutase. CCS may activate copper/zinc superoxide dismutase through direct insertion of the Cu cofactor.
VE:
1 * 100 µl
Lieferant:
Merck Millipore (Calbiochem)
Beschreibung:
A utility carrier of nitric oxide.
Artikel-Nr:
(BSBTPB9723)
Lieferant:
BosterBio
Hersteller-Artikelnummer::
PB9723
Lokale Artikelnummer::
BSBTPB9723
Beschreibung:
Rabbit IgG polyclonal antibody for Microsomal glutathione S-transferase 1(MGST1) detection. Tested with WB in Human;Mouse;Rat.
VE:
1 * 100 µG
Artikel-Nr:
(BOSSBS-3896R-CY7)
Lieferant:
Bioss
Hersteller-Artikelnummer::
BS-3896R-CY7
Lokale Artikelnummer::
BOSSBS-3896R-CY7
Beschreibung:
Superoxide dismutase (SOD) is an antioxidant enzyme involved in the defense system against reactive oxygen species (ROS). SOD catalyzes the dismutation reaction of superoxide radical anion (O2-) to hydrogen peroxide, which is then catalyzed to innocuous O2 and H2O by glutathione peroxidase and catalase. Several classes of SOD have been identified. These include intracellular copper, zinc SOD (Cu, Zn-SOD/SOD-1), mitochondrial manganese SOD (Mn-SOD/SOD-2) and extracellular Cu, Zn-SOD (EC-SOD/SOD-3). SOD1 is found in all eukaryotic species as a homodimeric 32 kDa enzyme containing one each of Cu and Zn ion per subunit. The manganese containing 80 kDa tetrameric enzyme SOD2, is located in the mitochondrial matrix in close proximity to a primary endogenous source of superoxide, the mitochondrial respiratory chain. SOD3 is a heparin-binding multimer of disulfide-linked dimers, primarily expressed in human lungs, vessel walls and airways. SOD4 is a copper chaperone for superoxide dismutase (CCS), which specifically delivers Cu to copper/zinc superoxide dismutase. CCS may activate copper/zinc superoxide dismutase through direct insertion of the Cu cofactor.
VE:
1 * 100 µl
Artikel-Nr:
(BOSSBS-3896R-CY3)
Lieferant:
Bioss
Hersteller-Artikelnummer::
BS-3896R-CY3
Lokale Artikelnummer::
BOSSBS-3896R-CY3
Beschreibung:
Superoxide dismutase (SOD) is an antioxidant enzyme involved in the defense system against reactive oxygen species (ROS). SOD catalyzes the dismutation reaction of superoxide radical anion (O2-) to hydrogen peroxide, which is then catalyzed to innocuous O2 and H2O by glutathione peroxidase and catalase. Several classes of SOD have been identified. These include intracellular copper, zinc SOD (Cu, Zn-SOD/SOD-1), mitochondrial manganese SOD (Mn-SOD/SOD-2) and extracellular Cu, Zn-SOD (EC-SOD/SOD-3). SOD1 is found in all eukaryotic species as a homodimeric 32 kDa enzyme containing one each of Cu and Zn ion per subunit. The manganese containing 80 kDa tetrameric enzyme SOD2, is located in the mitochondrial matrix in close proximity to a primary endogenous source of superoxide, the mitochondrial respiratory chain. SOD3 is a heparin-binding multimer of disulfide-linked dimers, primarily expressed in human lungs, vessel walls and airways. SOD4 is a copper chaperone for superoxide dismutase (CCS), which specifically delivers Cu to copper/zinc superoxide dismutase. CCS may activate copper/zinc superoxide dismutase through direct insertion of the Cu cofactor.
VE:
1 * 100 µl
Lieferant:
Avantor Fluid Handling
Beschreibung:
Bricht und oxidiert nicht.
Artikel-Nr:
(BSBTPA1590)
Lieferant:
BosterBio
Hersteller-Artikelnummer::
PA1590
Lokale Artikelnummer::
BSBTPA1590
Beschreibung:
Rabbit IgG polyclonal antibody for Glutathione S-transferase P(GSTP1) detection. Tested with WB, IHC-P in Human; Mouse; Rat.
VE:
1 * 0,1 mg
Artikel-Nr:
(BSBTPB9625)
Lieferant:
BosterBio
Hersteller-Artikelnummer::
PB9625
Lokale Artikelnummer::
BSBTPB9625
Beschreibung:
Rabbit IgG polyclonal antibody for Phospholipid hydroperoxide glutathione peroxidase, mitochondrial(GPX4) detection. Tested with WB, IHC-P in Human;Mouse;Rat.
VE:
1 * 100 µG
Artikel-Nr:
(PRSI4413)
Lieferant:
ProSci Inc.
Hersteller-Artikelnummer::
4413
Lokale Artikelnummer::
PRSI4413
Beschreibung:
GSTP1 Antibody: Glutathione S-transferases (GSTs) are a family of enzymes that play an important role in detoxification by catalyzing the conjugation of many hydrophobic and electrophilic compounds with reduced glutathione. Based on their biochemical, immunologic, and structural properties, the soluble GSTs are categorized into 4 main classes: alpha, mu, pi, and theta. The glutathione S-transferase pi gene (GSTP1) is a polymorphic gene encoding active, functionally different GSTP1 variant proteins that are thought to function in xenobiotic metabolism (i.e., the metabolism of environmental mutagens and carcinogens) and may play a role in susceptibility to cancer. More recent experiments have suggested that differential expression of GSTP1 also contributes to the sensitivity of xenobiotics in the substantia nigra and may influence the pathogenesis of reactive oxygen species-induced neurological disorders such as Parkinson's disease. CpG island hypermethylation of the GSTP1 promoter leading to the silencing of the GSTP1 gene has also been linked to cancer.
VE:
1 * 100 µG
Preis auf Anfrage
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 noch angezeigt wird und Sie Hilfe benötigen, rufen Sie uns an 1-800-932 - 5000.
Lager für diesen Artikel ist begrenzt, kann aber in einem Lagerhaus in Ihrer Nähe zur Verfügung. Bitte stellen Sie sicher, dass Sie in sind angemeldet auf dieser Seite, so dass verfügbare Bestand angezeigt werden können. Wenn das
noch angezeigt wird und Sie Hilfe benötigen, rufen Sie uns an 1-800-932 - 5000.
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