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Targeted therapy! The Capetin Prize winning "Click Chemistry" can be used like this!Targeted therapy! The Nobel Prize winning "Click Chemistry" can be used like this!2025-02-06
104 Results for "
NADH dehydrogenase
" in MedChemExpress (MCE) Product Catalog:
Products (104)
104 Results for "NADH dehydrogenase" in MCE Product Catalog:
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5 Cited Publications
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2 Cited Publications
Cat. No.: HY-B0817
CAS No.: 96489-71-3
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Pyridaben is a mitochondrial electron transport inhibitor (METI) acaricide that promotes the formation of damaging oxygen and nitrogen radicals. Pyridaben selectively inhibits complex I (NADH dehydrogenase) with an IC50 value of 2.4 nM (assay sites: rat liver and bovine heart mitochondria). Pyridaben also significantly inhibits rat mitochondrial mtNOS function .
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1 Cited Publications
Cat. No.: HY-17378
CAS No.: 429658-95-7
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Dabigatran ethyl ester is an inhibitor of ribosyldihydronicotinamide dehydrogenase (NQO2) and thrombin. Dabigatran ethyl ester inhibits NADH-dependent metabolism of mitomycin C mediated by purified recombinant human NQO2 .
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1 Cited Publications
CK-2-68 is an inhibitor for complex III in protozoan mitochondrial respiratory chain, by targeting the alternative NADH dehydrogenase (NDH2) of the malarial parasite Plasmodium. CK-2-68 exhibits antimalaria efficacy, that inhibits Plasmodium falciparum infected erythrocytes with an IC50 of 40 nM .
Cat. No.: HY-113128A
Purity: 99.90%
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Formate dehydrogenase is a class of oxidoreductases widely distributed in bacteria, fungi, plants and animals. Formate dehydrogenase catalyzes the reversible conversion between formic acid and carbon dioxide, accompanied by redox reactions of the coenzyme NAD +/NADH or other electron carriers .
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Ketones, Aldehydes, Acids Other Diseases Disease markers Nervous System Disorder Endogenous metabolite Disease Research Fields
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Beta-galactose dehydrogenase is a selective catalyst for β-galactose. Under pH 8.6 conditions, beta-galactose dehydrogenase catalyzes the oxidation of β-galactose, produced by the hydrolysis of lactose by β-galactosidase, with nicotinamide adenine dinucleotide (NAD) to produce reduced nicotinamide adenine dinucleotide (NADH). Beta-galactose dehydrogenase specifically mediates this oxidation reaction for the quantitative detection of the substrate, used in the analysis of lactose concentration in samples such as breast milk .
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L-Lactate dehydrogenase, E.coli is a redox enzyme. L-Lactate dehydrogenase, E.coli catalyzes the reduction of pyruvate to L-lactate by NADH in vivo with absolute enantiospecificity .
Synonyms: 4′‐BR
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4'-Bromo-resveratrol (4′‐BR) is a dual SIRT1/SIRT3 inhibitor with an IC50 of 0.2 mM for both targets. 4'-Bromo-resveratrol induces caspase-dependent apoptosis, induces G0/G1 cell cycle arrest, and inhiibits proliferation. 4'-Bromo-resveratrol reduces lactate production, glucose uptake, and NAD +/NADH ratio, and downregulates lactate dehydrogenase A and glucose transporter 1 (GLUT1). 4'-Bromo-resveratrol can be used for the research of melanoma .
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Glucose dehydrogenase, recombinant Microorganisms is a FDA-dependent oxidoreductase. Glucose dehydrogenase (GDH) catalyzes the oxidation of β-D-glucose to β-D-glucono-1,5-lactone with simultaneous reduction of the cofactor NADP + to NADPH or, to a lesser extent, NAD + to NADH. Glucose dehydrogenase (GDH) accepts both NAD + and NADP + as cofactors and can be used for the regeneration of NADH and NADPH .
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NAD-dependent glucose dehydrogenase (GDH-NAD) is an oxidoreductase that uses NAD + as a coenzyme, specifically catalyzes the dehydrogenation of glucose to gluconolactone, and reduces NAD + to NADH. NAD-dependent glucose dehydrogenase exhibits favorable substrate selectivity and stability, and is not affected by oxygen .
Synonyms: GPDH, rabbit muscle; α-Glycerophosphate dehydrogenase, rabbit muscle; Glycerol phosphate dehydrogenase, rabbit muscle
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Glycerol‑3‑phosphate dehydrogenase, rabbit muscle (GPDH; α-Glycerophosphate dehydrogenase; Glycerol phosphate dehydrogenase) is an NADH-dependent oxidoreductase derived from rabbit muscle that participates in glycolysis, gluconeogenesis, and the glycerol‑3‑phosphate shuttle metabolic pathway. Glycerol‑3‑phosphate dehydrogenase, rabbit muscle uses NADH as a reducing equivalent donor, and its substrate binding relies on the phosphate-binding site in the active center; it catalyzes the reversible reduction of dihydroxyacetone phosphate to L‑α‑glycerol‑3‑phosphate. The catalytic activity of the enzymatic reaction of Glycerol‑3‑phosphate dehydrogenase, rabbit muscle is regulated by pH and divalent metal ions. Glycerol‑3‑phosphate dehydrogenase, rabbit muscle can be used in metabolism-related studies .
Cat. No.: HY-113128S
Purity: 98.7%
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Sorbitol dehydrogenase (L-Iditol dehydrogenase) is an oxidoreductasea and catalyses the conversion of sorbitol to fructose with NAD + as the coenzyme. Sorbitol dehydrogenase catalyses pH-dependent redox reactions between NAD +/NADH and sorbitol/fructose. Sorbitol dehydrogenase is implicated in diabetic complications and is a biomarker of drug-induced liver injury. Sorbitol dehydrogenase can be used for the research of diabetes and liver injury .
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RYL-552, a mitochondrial electron transport chain (ETC) inhibitor, is a P. falciparum NADH dehydrogenase 2 (PfNDH2) inhibtor .
Cat. No.: HY-E70075
Synonyms: GDH-TIM; GDH-TPI
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α-Glycerophosphate Dehydrogenase-Triosephosphate (GDH-TIM) is a bifunctional enzyme with activity toward glyceraldehyde 3-phosphate and dihydroxyacetone phosphate. α-Glycerophosphate Dehydrogenase-Triosephosphate catalyzes the conversion of glyceraldehyde 3-phosphate to dihydroxyacetone phosphate. α-Glycerophosphate Dehydrogenase-Triosephosphate can utilize NADH to catalyze the reduction of dihydroxyacetone phosphate to glycerol-1-P .
Synonyms: GPDH, microorganism; α-Glycerophosphate dehydrogenase, microorganism; Glycerol phosphate dehydrogenase, microorganism
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Glycerol-3-phosphate dehydrogenase, microorganism (GPDH; α-Glycerophosphate dehydrogenase; Glycerol phosphate dehydrogenase) is an NADH-dependent oxidoreductase derived from microorganism that participates in glycolysis, gluconeogenesis, and the glycerol‑3‑phosphate shuttle metabolic pathway. Glycerol-3-phosphate dehydrogenase, microorganism uses NADH as a reducing equivalent donor, and its substrate binding relies on the phosphate-binding site in the active center; it catalyzes the reversible reduction of dihydroxyacetone phosphate to L‑α‑glycerol‑3‑phosphate. The catalytic activity of the enzymatic reaction of Glycerol-3-phosphate dehydrogenase, microorganism is regulated by pH and divalent metal ions. Glycerol-3-phosphate dehydrogenase, microorganism can be used in metabolism-related studies .
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Protocols
Targeted therapy! The Capetin Prize winning "Click Chemistry" can be used like this!Targeted therapy! The Nobel Prize winning "Click Chemistry" can be used like this!A suitable model is crucial in drug screening experiments. Organs can mimic the three-dimensional functional structure of internal organs, have similar spatial organization to corresponding organs, maintain some key characteristics, and reproduce some physiological functions. They are widely used for modeling and personalized drug screening physiological functions.2025-02-06
