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Didodecyl+hydrogen+phosphate


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Supplier:  Bioss
Description:   Glutathione-dependent oxidoreductase that facilitates the maintenance of mitochondrial redox homeostasis upon induction of apoptosis by oxidative stress. Involved in response to hydrogen peroxide and regulation of apoptosis caused by oxidative stress. Acts as a very efficient catalyst of monothiol reactions because of its high affinity for protein glutathione-mixed disulfides. Can receive electrons not only from glutathione (GSH), but also from thioredoxin reductase supporting both monothiol and dithiol reactions. Efficiently catalyzes both glutathionylation and deglutathionylation of mitochondrial complex I, which in turn regulates the superoxide production by the complex. Overexpression decreases the susceptibility to apoptosis and prevents loss of cardiolipin and cytochrome c release.
Catalog Number: (10288-652)

Supplier:  Bioss
Description:   Iron metabolism is essential for sustaining mammalian homeostasis. Iron uptake and distribution is a highly regulated process in mammalian cells that is monitored by two iron sensing proteins; iron regulatory protein-1 and -2 (IRP-1 and -2), also known as iron responsive element-binding protein-1 and -2 (IRE–BP-1 and -2) or aconitase 1 and 2. IRP-1 and IRP-2 are important soluble regulatory factors that mediate iron uptake and storage in mammalian cells. They are capable of either repressing translation or enhancing mRNA stability by associating with stem-loop motifs known as iron-responsive elements (IREs). IRPs respond to stress mediators, iron concentration and signaling factors, including nitrogen monoxide, cytokines and hydrogen peroxide.

Supplier:  Bioss
Description:   Glutathione-dependent oxidoreductase that facilitates the maintenance of mitochondrial redox homeostasis upon induction of apoptosis by oxidative stress. Involved in response to hydrogen peroxide and regulation of apoptosis caused by oxidative stress. Acts as a very efficient catalyst of monothiol reactions because of its high affinity for protein glutathione-mixed disulfides. Can receive electrons not only from glutathione (GSH), but also from thioredoxin reductase supporting both monothiol and dithiol reactions. Efficiently catalyzes both glutathionylation and deglutathionylation of mitochondrial complex I, which in turn regulates the superoxide production by the complex. Overexpression decreases the susceptibility to apoptosis and prevents loss of cardiolipin and cytochrome c release.

Supplier:  Bioss
Description:   Glutathione-dependent oxidoreductase that facilitates the maintenance of mitochondrial redox homeostasis upon induction of apoptosis by oxidative stress. Involved in response to hydrogen peroxide and regulation of apoptosis caused by oxidative stress. Acts as a very efficient catalyst of monothiol reactions because of its high affinity for protein glutathione-mixed disulfides. Can receive electrons not only from glutathione (GSH), but also from thioredoxin reductase supporting both monothiol and dithiol reactions. Efficiently catalyzes both glutathionylation and deglutathionylation of mitochondrial complex I, which in turn regulates the superoxide production by the complex. Overexpression decreases the susceptibility to apoptosis and prevents loss of cardiolipin and cytochrome c release.
Supplier:  Bioss
Description:   Glutathione-dependent oxidoreductase that facilitates the maintenance of mitochondrial redox homeostasis upon induction of apoptosis by oxidative stress. Involved in response to hydrogen peroxide and regulation of apoptosis caused by oxidative stress. Acts as a very efficient catalyst of monothiol reactions because of its high affinity for protein glutathione-mixed disulfides. Can receive electrons not only from glutathione (GSH), but also from thioredoxin reductase supporting both monothiol and dithiol reactions. Efficiently catalyzes both glutathionylation and deglutathionylation of mitochondrial complex I, which in turn regulates the superoxide production by the complex. Overexpression decreases the susceptibility to apoptosis and prevents loss of cardiolipin and cytochrome c release.

Supplier:  MP Biomedicals
Description:   Product is the lyophilized powder of goat antiserum to human serum and buffer salts.
The antiserum is prepared by immunizing goats with human serum; antiserum is delipidated and made specific by
immunoadsorption with soluble antigens or solid-phase immunoadsorption where appropriate. The resulting antiserum is
dialyzed into 0.02M sodium phosphate, 0.14M sodium chloride, pH 7.3, with 0.05% sodium azide, adjusted to standard titer,
filtered through a 0.22 µm filter, vialed and lyophilized

Supplier:  Bioss
Description:   Iron metabolism is essential for sustaining mammalian homeostasis. Iron uptake and distribution is a highly regulated process in mammalian cells that is monitored by two iron sensing proteins; iron regulatory protein-1 and -2 (IRP-1 and -2), also known as iron responsive element-binding protein-1 and -2 (IRE–BP-1 and -2) or aconitase 1 and 2. IRP-1 and IRP-2 are important soluble regulatory factors that mediate iron uptake and storage in mammalian cells. They are capable of either repressing translation or enhancing mRNA stability by associating with stem-loop motifs known as iron-responsive elements (IREs). IRPs respond to stress mediators, iron concentration and signaling factors, including nitrogen monoxide, cytokines and hydrogen peroxide.
Supplier:  Bioss
Description:   Iron metabolism is essential for sustaining mammalian homeostasis. Iron uptake and distribution is a highly regulated process in mammalian cells that is monitored by two iron sensing proteins; iron regulatory protein-1 and -2 (IRP-1 and -2), also known as iron responsive element-binding protein-1 and -2 (IREBP-1 and -2) or aconitase 1 and 2. IRP-1 and IRP-2 are important soluble regulatory factors that mediate iron uptake and storage in mammalian cells. They are capable of either repressing translation or enhancing mRNA stability by associating with stem-loop motifs known as iron-responsive elements (IREs). IRPs respond to stress mediators, iron concentration and signaling factors, including nitrogen monoxide, cytokines and hydrogen peroxide.
Supplier:  Bioss
Description:   Catalyzes the hydrolysis of fructose 1,6-bisphosphate to fructose 6-phosphate in the presence of divalent cations, acting as a rate-limiting enzyme in gluconeogenesis. Plays a role in regulating glucose sensing and insulin secretion of pancreatic beta-cells. Appears to modulate glycerol gluconeogenesis in liver. Important regulator of appetite and adiposity; increased expression of the protein in liver after nutrient excess increases circulating satiety hormones and reduces appetite-stimulating neuropeptides and thus seems to provide a feedback mechanism to limit weight gain.
Catalog Number: (10285-442)

Supplier:  Bioss
Description:   Iron metabolism is essential for sustaining mammalian homeostasis. Iron uptake and distribution is a highly regulated process in mammalian cells that is monitored by two iron sensing proteins; iron regulatory protein-1 and -2 (IRP-1 and -2), also known as iron responsive element-binding protein-1 and -2 (IRE–BP-1 and -2) or aconitase 1 and 2. IRP-1 and IRP-2 are important soluble regulatory factors that mediate iron uptake and storage in mammalian cells. They are capable of either repressing translation or enhancing mRNA stability by associating with stem-loop motifs known as iron-responsive elements (IREs). IRPs respond to stress mediators, iron concentration and signaling factors, including nitrogen monoxide, cytokines and hydrogen peroxide.

Supplier:  Bioss
Description:   Involved in transport from the ER to the Golgi apparatus as well as in intra-Golgi transport. It belongs to a super-family of proteins called t-SNAREs or soluble NSF (N-ethylmaleimide-sensitive factor) attachment protein receptor. May play a protective role against hydrogen peroxide induced cytotoxicity under glutathione depleted conditions in neuronal cells by regulating the intracellular ROS levels via inhibition of p38 MAPK (MAPK11, MAPK12, MAPK13 and MAPK14). Participates in docking and fusion stage of ER to cis-Golgi transport. Plays an important physiological role in VLDL-transport vesicle-Golgi fusion and thus in VLDL delivery to the hepatic cis-Golgi.

Supplier:  Bioss
Description:   Involved in transport from the ER to the Golgi apparatus as well as in intra-Golgi transport. It belongs to a super-family of proteins called t-SNAREs or soluble NSF (N-ethylmaleimide-sensitive factor) attachment protein receptor. May play a protective role against hydrogen peroxide induced cytotoxicity under glutathione depleted conditions in neuronal cells by regulating the intracellular ROS levels via inhibition of p38 MAPK (MAPK11, MAPK12, MAPK13 and MAPK14). Participates in docking and fusion stage of ER to cis-Golgi transport. Plays an important physiological role in VLDL-transport vesicle-Golgi fusion and thus in VLDL delivery to the hepatic cis-Golgi.
Supplier:  Bioss
Description:   Involved in transport from the ER to the Golgi apparatus as well as in intra-Golgi transport. It belongs to a super-family of proteins called t-SNAREs or soluble NSF (N-ethylmaleimide-sensitive factor) attachment protein receptor. May play a protective role against hydrogen peroxide induced cytotoxicity under glutathione depleted conditions in neuronal cells by regulating the intracellular ROS levels via inhibition of p38 MAPK (MAPK11, MAPK12, MAPK13 and MAPK14). Participates in docking and fusion stage of ER to cis-Golgi transport. Plays an important physiological role in VLDL-transport vesicle-Golgi fusion and thus in VLDL delivery to the hepatic cis-Golgi.
Catalog Number: (103004-434)

Supplier:  Anaspec Inc
Description:   The unlabeled phosphopeptide is an excellent substrate for mammalian protein tyrosine phosphatase 1B (Km = 3.9 µM) and Yersinia PTP. The sequence is derived from an autophosphorylation site (Tyr992) of EGFR. The unlabeled peptide is used to assay PTB based on marked fluorescence increase upon the removal of the phosphate group (Em = 305 nm and Ex = 282 nm).
Sequence:Biotin-DADE-pY-LIPQQG
MW:1556.6 Da
% peak area by HPLC:95
Storage condition:-20° C
Supplier:  Bioss
Description:   Glutathione-dependent oxidoreductase that facilitates the maintenance of mitochondrial redox homeostasis upon induction of apoptosis by oxidative stress. Involved in response to hydrogen peroxide and regulation of apoptosis caused by oxidative stress. Acts as a very efficient catalyst of monothiol reactions because of its high affinity for protein glutathione-mixed disulfides. Can receive electrons not only from glutathione (GSH), but also from thioredoxin reductase supporting both monothiol and dithiol reactions. Efficiently catalyzes both glutathionylation and deglutathionylation of mitochondrial complex I, which in turn regulates the superoxide production by the complex. Overexpression decreases the susceptibility to apoptosis and prevents loss of cardiolipin and cytochrome c release.
Supplier:  MP Biomedicals
Description:   Storage: -20°C, desiccate
This is an ultrapure NAD, chromatographically purified to remove trace inhibitors.
β-NAD, a pyridine nucleotide and biologically active form of nicotinic acid, is a coenzyme necessary for the catalytic reaction of certain enzymes. It occurs in living cells primarily in the oxidized state. Serves as a coenzyme of the dehydrogenases, especially in the dehydrogenation of primary and secondary alcohols. NAD usually acts as a hydrogen acceptor, forming NADH which then serves as a hydrogen donor in the respiratory chain.
Many metabolites and enzymes of biological interest are present in tissues at low concentrations. With the use of β-NAD as a catalyst intermediate and several enzymes in a multistep system, known as enzyme cycling, much greater sensitivity for detection of these components is achieved. The reduced form, β-NADH, is fluorescent whereas β-NAD is not. This difference in fluorescence provides a sensitive fluorescent measurement of the oxidized or reduced pyridine nucleotides at concentrations down to 10-7 M.
Electron acceptor. β-NAD is a carrier for hydride ion, forming b-NADH. Hydride ion is enzymatically removed from a substrate molecule by the action of dehydrogenases such as malic dehydrogenase and lactic dehydrogenase. Such enzymes catalyze the reversible transfer of a hydride ion from malate or lactate to b-NAD to form the reduced product, b-NADH. Unlike b-NAD which has no absorbance at 340 nm, b-NADH absorbs at 340 nm (EmM = 6.22). The increase in absorbance at 340 nm with the formation of b-NADH is the basis for measurement of activity of many enzymes.
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Stock for this item is limited, but may be available in a warehouse close to you. Please make sure that you are logged in to the site so that available stock can be displayed. If the call is still displayed and you need assistance, please call us at 1-800-932-5000.
This product is marked as restricted and can only be purchased by approved Shipping Accounts. If you need further assistance, email VWR Regulatory Department at Regulatory_Affairs@vwr.com
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