NAD(P) transhydrogenase/NNT Protein, Human, Recombinant (His)

Catalog No. TMPJ-01106

NAD(P)+transhydrogenase (NNT) is located in the inner mitochondrial membrane and catalyzes a reversible hydride transfer between NAD(H) and NADP(H) that is coupled to proton translocation between the intermembrane space and mitochondrial matrix. NNT activity has an essential role in maintaining the NADPH supply for antioxidant defense and biosynthetic pathways. Structurally, NNT is composed of three domains; domains I and III are hydrophilic and have binding sites for NAD and NADP, respectively, while domain II is hydrophobic and is a transmembrane pathway through which protons translocate. NNT forms dimers, whose monomers act in an anti-phase way; domain III (NADP(H)- binding) flips, allowing proton translocation across the inner mitochondrial membrane one moment and favoring hydride transfer between NAD(H) and NADP(H) the next. And NNT pathophysiological roles after the discovery of a spontaneous Nnt mutation in C57BL/6J mice. And Nnt silencing reduced the growth of cancer cell lines, suggesting that NNT might be a therapeutic target in some cancers.

NAD(P) transhydrogenase/NNT Protein, Human, Recombinant (His)

Catalog No. TMPJ-01106

Pack Size	Price	Availability
10 μg	$118	7-10 days
50 μg	$355	7-10 days
500 μg	$2,010	7-10 days
1 mg	$3,020	7-10 days

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Product Information

Biological Activity	Activity has not been tested. It is theoretically active, but we cannot guarantee it. If you require protein activity, we recommend choosing the eukaryotic expression version first.
Description	NAD(P)+transhydrogenase (NNT) is located in the inner mitochondrial membrane and catalyzes a reversible hydride transfer between NAD(H) and NADP(H) that is coupled to proton translocation between the intermembrane space and mitochondrial matrix. NNT activity has an essential role in maintaining the NADPH supply for antioxidant defense and biosynthetic pathways. Structurally, NNT is composed of three domains; domains I and III are hydrophilic and have binding sites for NAD and NADP, respectively, while domain II is hydrophobic and is a transmembrane pathway through which protons translocate. NNT forms dimers, whose monomers act in an anti-phase way; domain III (NADP(H)- binding) flips, allowing proton translocation across the inner mitochondrial membrane one moment and favoring hydride transfer between NAD(H) and NADP(H) the next. And NNT pathophysiological roles after the discovery of a spontaneous Nnt mutation in C57BL/6J mice. And Nnt silencing reduced the growth of cancer cell lines, suggesting that NNT might be a therapeutic target in some cancers.
Species	Human
Expression System	E. coli
Tag	N-6xHis
Accession Number	Q13423
Synonyms	NNT,NAD(P) transhydrogenase
Amino Acid	Met880-Lys1086
Construction	Met880-Lys1086
Protein Purity	Greater than 95% as determined by reducing SDS-PAGE. (QC verified)
Molecular Weight	30 KDa (reducing condition)
Endotoxin	< 0.1 ng/µg (1 EU/µg) as determined by LAL test.
Formulation	Supplied as a 0.2 μm filtered solution of PBS, 10 mM GSH, 50% Glycerol, pH7.4.
Stability & Storage	Lyophilized powders can be stably stored for over 12 months, while liquid products can be stored for 6-12 months at -80°C. For reconstituted protein solutions, the solution can be stored at -20°C to -80°C for at least 3 months. Please avoid multiple freeze-thaw cycles and store products in aliquots.
Shipping	Shipping with blue ice.
Research Background	NAD(P)+transhydrogenase (NNT) is located in the inner mitochondrial membrane and catalyzes a reversible hydride transfer between NAD(H) and NADP(H) that is coupled to proton translocation between the intermembrane space and mitochondrial matrix. NNT activity has an essential role in maintaining the NADPH supply for antioxidant defense and biosynthetic pathways. Structurally, NNT is composed of three domains; domains I and III are hydrophilic and have binding sites for NAD and NADP, respectively, while domain II is hydrophobic and is a transmembrane pathway through which protons translocate. NNT forms dimers, whose monomers act in an anti-phase way; domain III (NADP(H)- binding) flips, allowing proton translocation across the inner mitochondrial membrane one moment and favoring hydride transfer between NAD(H) and NADP(H) the next. And NNT pathophysiological roles after the discovery of a spontaneous Nnt mutation in C57BL/6J mice. And Nnt silencing reduced the growth of cancer cell lines, suggesting that NNT might be a therapeutic target in some cancers.

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