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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
28 Results for "
Glycerol dehydrogenase
" in MedChemExpress (MCE) Product Catalog:
Products (28)
28 Results for "Glycerol dehydrogenase" in MCE Product Catalog:
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Glycerol dehydrogenase is a polyol dehydrogenase that catalyzes the NAD-dependent oxidation of glycerol to dihydroxyacetone. Glycerol dehydrogenase can be used for glycerol metabolism in diverse microorganisms .
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Infection Ardisia brevicaulis Diels Phenols Polyphenols Plants Myrsinaceae Disease Research Fields
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Glycerol-3-phosphate oxidase, E. coli (GPO) is a key intermediate in glycerol metabolism. Glycerol-3-phosphate oxidase, E. coli is the skeleton of phospholipids in membrane lipids, and also a substrate in the respiratory chain. Glycerol-3-phosphate oxidase, E. coli produces electrons through oxidation. Glycerol-3-phosphate oxidase, E. coli is an enzyme with important functions in the field of biochemistry, and is widely used in medical testing and scientific research .
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1 Cited Publications
Synonyms: Triose phosphate
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1 Cited Publications
Cat. No.: HY-121970
CAS No.: 27031-00-1
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Phosphoglycerate Dehydrogenase (PHGDH) Reactive Oxygen Species (ROS) HIF/HIF Prolyl-Hydroxylase
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iGP-1 is a cell-permeable, selective mixed inhibitor of mitochondrial sn-glycerol-3-phosphate dehydrogenase (mGPDH), with IC50s of 6.3 μM and 13.6 μM for rat mGPDH activity and H2O2 production, respectively. iGP-1 specifically blocks the mitochondrial component of the glycerophosphate shuttle without affecting cytosolic GPDH. iGP-1 not only inhibits cell proliferation and glutaminolysis, and enhances glycolysis, but also significantly alters key cellular physiological processes such as apoptosis, ROS production, HIF-1α stability and mitochondrial membrane potential. iGP-1 remains active in neutrophil cultures under both normoxic and hypoxic conditions, and serves as an ideal probe for glycerol-3-phosphate metabolic mechanisms. iGP-1 has been applied to studies on prostate cancer and related metabolic pathways .
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1 Cited Publications
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KM04416, an isothiazolone derivative, is a potent glycerol-3-phosphate dehydrogenase (GPD2) inhibitor. KM04416 significantly inhibits PNT1A cell proliferation .
Cat. No.: HY-113128A
Purity: 99.90%
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Ketones, Aldehydes, Acids Other Diseases Disease markers Nervous System Disorder Endogenous metabolite Disease Research Fields
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Human Gut Microbiota Metabolites Natural Products Microorganisms Metabolic Disease Endogenous metabolite Disease Research Fields
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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%
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 .
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 .
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CAY10762 is an inhibitor of monoacylglycerol lipase (MAGL; IC50=34.1 nM). It reduces hydrogen peroxide-induced lactate dehydrogenase (LDH) release from Neuro2a cells when used at a concentration of 1 μM. CAY10762 (10 mg/kg) increases levels of 2-arachidonoyl glycerol in mouse brain.
Cat. No.: HY-113128B
CAS No.: 29849-82-9
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Synonyms: 7α-Hydroxydehydroepiandrosterone; 3β,7α-Dihydroxy-Δ5-androsten-17-one
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Cat. No.: HY-P2765B
Synonyms: GPDH, Rabbit; α-Glycerophosphate dehydrogenase, Rabbit; Glycerol phosphate dehydrogenase, Rabbit
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Glycerol-3-phosphate dehydrogenase, Rabbit (GPDH; α-Glycerophosphate dehydrogenase; Glycerol phosphate dehydrogenase) is an NADH-dependent oxidoreductase derived from Rabbit that participates in glycolysis, gluconeogenesis, and the glycerol‑3‑phosphate shuttle metabolic pathway. Glycerol-3-phosphate dehydrogenase, Rabbit 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 is regulated by pH and divalent metal ions. Glycerol-3-phosphate dehydrogenase, Rabbit can be used in metabolism-related studies .
Cat. No.: HY-P2765C
Synonyms: GPDH, Chicken; α-Glycerophosphate dehydrogenase, Chicken; Glycerol phosphate dehydrogenase, Chicken
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Glycerol-3-phosphate dehydrogenase, Chicken (GPDH; α-Glycerophosphate dehydrogenase; Glycerol phosphate dehydrogenase) is an NADH-dependent oxidoreductase derived from Chicken that participates in glycolysis, gluconeogenesis, and the glycerol‑3‑phosphate shuttle metabolic pathway. Glycerol-3-phosphate dehydrogenase, Chicken 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, Chicken is regulated by pH and divalent metal ions. Glycerol-3-phosphate dehydrogenase, Chicken can be used in metabolism-related studies .
Cat. No.: HY-P2765D
Synonyms: GPDH, Human; α-Glycerophosphate dehydrogenase, Human; Glycerol phosphate dehydrogenase, Human
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Glycerol-3-phosphate dehydrogenase, Human (GPDH; α-Glycerophosphate dehydrogenase; Glycerol phosphate dehydrogenase) is an NADH-dependent oxidoreductase derived from Human that participates in glycolysis, gluconeogenesis, and the glycerol‑3‑phosphate shuttle metabolic pathway. Glycerol-3-phosphate dehydrogenase, Human 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, Human is regulated by pH and divalent metal ions. Glycerol-3-phosphate dehydrogenase, Human 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
