nadp+

Malate dehydrogenase (oxaloacetate-decarboxylating, NADP+) is a biochemical reagent utilized as a biomaterial or organic compound in life science research.

Aromatic Alcohol Dehydrogenase (NADP+ dependent), from Thermoanaerobium sp. (EC 1.1.1.2), is involved in the reduction of both endogenous and exogenous aldehydes and is found in nearly all tissues.

Alcohol Dehydrogenase (NADP+ dependent), Thermoanaerobium brockii (EC 1.1.1.2), is involved in the reduction of endogenous and exogenous aldehydes and is found in nearly all tissues.

Thio-NADP (S-NADP) functions as an inhibitor of nicotinic acid adenine dinucleotide phosphate (NAADP) and induces partial Ca 2+ release [1].

Phosphogluconate dehydrogenase (NADP, decarboxylating) [6-Phosphogluconate dehydrogenase] is a biochemical reagent that serves as a biomaterial or organic compound utilized in life sciences research.

Isocitric Dehydrogenase (NADP), Porcine (EC 1.1.1.42) is an enzyme that catalyzes the oxidative decarboxylation of isocitric acid to produce α-ketoglutaric acid and carbon dioxide (CO2).

L-Glutamic Dehydrogenase (NADP) from Proteus sp. (EC 1.4.1.4) catalyzes the conversion of glutamic acid to α-ketoglutaric acid.

Glutamate Dehydrogenase (NADP-dependent), Proteus sp. (EC 1.4.1.4), is an enzyme located in the mitochondria of most microorganisms and eukaryotes, responsible for converting glutamate into α-ketoglutarate.

2',3'-Cyclic NADP disodium (2',3'-cNADP+; β-Nicotinamide adenine dinucleotide-2',3'-cyclic phosphate) is a substrate of 2',3'-cyclic nucleotide 3'-phosphodiesterase (CNP), an enzyme abundantly found in the myelin. It is utilized in coupled enzyme assays for the quantification of CNP activity. At a concentration of 5 μM, 2',3'-cNADP disodium can enhance calcium release due to calcium overload and prevent calcium-induced swelling in rat brain mitochondria.

Thioredoxin reductase (TrxR/NTR) is an enzyme of the pyridine nucleotide-disulfide oxidoreductase flavoprotein family. As a component of the thioredoxin system, which includes thioredoxin (Trx) and NADPH, TrxR facilitates the transfer of electrons from NADPH to Trx, acting as a reductant for proteins with disulfide bonds, and plays a role in the oxidative stress defense system.

Glucose dehydrogenase (GDH) is an oxidoreductase enzyme that facilitates the oxidation of β-D-glucose into β-D-glucono-1,5-lactone, while concurrently reducing cofactor NADP+ to NADPH, and to a lesser degree, NAD+ to NADH. It can utilize both NAD+ and NADP+ as cofactors and serves in the regeneration of NADH and NADPH [1] [2].

Glucose dehydrogenase, Pseudomonas sp. (EC 1.1.1.47) is a type of oxidoreductase that acts on the CH-OH group of donor molecules, utilizing either NAD+ or NADP+ as the acceptor. The enzyme's three substrates are β-D-glucose, NAD+, and NADP+, and its four products are D-glucono-1,5-lactone, NADH, NADPH, and H+.

D-3-hydroxybutyrate dehydrogenase, Pseudomonas sp. (EC 1.1.1.30), is a type of oxidoreductase enzyme that acts on the CH-OH group of donors and utilizes NAD+ or NADP+ as an acceptor. It plays a role in ketone body synthesis and degradation, as well as in butyrate metabolism.

6-Phosphogluconic Dehydrogenase, Sheep (EC 1.1.1.44) is an enzyme in the oxidoreductase family that acts on the CH-OH group of donor molecules using NAD+ or NADP+ as an acceptor. The enzyme's substrates are 6-phospho-D-gluconate and NADP+, and its products are D-ribulose-5-phosphate, CO2, and NADPH.

3α-Hydroxysteroid Dehydrogenase, Pseudomonas testosteroni (EC 1.1.1.50), is part of the oxidoreductase family. This enzyme utilizes three substrates: androsterone, NAD+, and NADP+, resulting in four products: 5α-androstan-3,17-dione, NADH, NADPH, and H+. It acts on the CH-OH group of donor molecules using NAD+ or NADP+ as an acceptor.

β-Galactose Dehydrogenase S, Pseudomonas fluorescens (EC 1.1.1.48) is an enzyme from the oxidoreductase family, which acts on CH-OH group donors using NAD+ or NADP+ as acceptors. It plays a role in galactose metabolism, using D-galactose and NAD+ as substrates to produce D-galacto-1,4-lactone, NADH, and H+.

Glutathione Reductase, Wheat germ (EC 1.6.4.2), is a crucial flavoprotein in the antioxidant defense system. In this process, reduced glutathione (GSH) detoxifies hydrogen peroxide via glutathione peroxidase, becoming oxidized to form oxidized glutathione (GSSG). Glutathione Reductase (GR) then reduces GSSG back to GSH using NADPH, which is converted to NADP+. The regenerated GSH is available for further hydrogen peroxide detoxification. Glutathione Reductase utilizes FAD as a cofactor.

Yeast 6-Phosphogluconic Dehydrogenase (EC 1.1.1.44) is a member of the oxidoreductase family, which acts on the CH-OH group of donor molecules using NAD+ or NADP+ as an acceptor. The two substrates for Yeast 6-Phosphogluconic Dehydrogenase are 6-phospho-D-gluconate and NADP+, and its three products are D-ribulose 5-phosphate, CO2, and NADPH.

Glutathione Reductase, Wheat germ (EC 1.6.4.2), is an essential flavoprotein in the antioxidant defense system. The reduced glutathione (GSH) is used by glutathione peroxidase to detoxify hydrogen peroxide, during which it is oxidized to form oxidized glutathione (GSSG). The GSSG is then reduced back to GSH by glutathione reductase (GR) using NADPH, which is converted to NADP+ in the process. The regenerated GSH can continue detoxifying hydrogen peroxide. Glutathione Reductase utilizes FAD as a cofactor.