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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
14 Results for "
Flavin-Adenine Dinucleotide
" in MedChemExpress (MCE) Product Catalog:
Products (14)
14 Results for "Flavin-Adenine Dinucleotide" in MCE Product Catalog:
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Cardiovascular Disease Human Gut Microbiota Metabolites Natural Products other families Microorganisms Plants Endogenous metabolite Disease Research Fields
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1 Cited Publications
Synonyms: Vitamin B2 (Standard); E101 (Standard)
Cat. No.: HY-B1654S
Synonyms: FAD-13C5 ammonium
Cat. No.: HY-175593
CAS No.: 696628-90-7
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M6766 is a selective endoplasmic reticulum oxidoreductase 1α (ERO1α) inhibitor with an IC50 of 1.4 μM and a KD of 1.1 μM. M6766 also inhibits ERO1β with an IC50 of 7.2 μM. M6766 binds to the flavin adenine dinucleotide-binding pocket in ERO1α. M6766 inhibits granule secretion, αIIbβ3 integrin activation, Ca 2+ mobilization, and platelet aggregation. M6766 can be used for the research of neurological disease, such as ischemic stroke .
Cat. No.: HY-B1654AR
CAS No.: 84366-81-4
Synonyms: FAD disodium salt (Standard); FAD-Na2 (Standard)
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Cat. No.: HY-B0456S5
Synonyms: Vitamin B2-d8 ; E101-d8
Cat. No.: HY-P2889A
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Pyranose Oxidase, E. coli (EC 1.1.3.10) catalyzes the oxidation of aldopyranoses at position C-2 to yield the corresponding 2-ketoaldoses. Pyranose Oxidase is a homotetrameric protein that contains covalently bound flavin adenine dinucleotide (FAD).
Cat. No.: HY-186116
CAS No.: 1422533-70-7
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LSD1-IN-49 is an irreversible LSD1/KDM1A inhibitor with an IC50 of 29 nM against hLSD1. LSD1-IN-49 irreversibly inhibits the enzymatic activity of LSD1 by forming an adduct with flavin adenine dinucleotide (FAD) in the binding pocket of LSD1. LSD1-IN-49 is applicable to research related to schizophrenia, autism spectrum disorder and Huntington's disease .
Cat. No.: HY-186116A
CAS No.: 1422534-06-2
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LSD1-IN-49 hydrochloride (Compound (±) 1) is an irreversible LSD1/KDM1A inhibitor with an IC50 of 29 nM against hLSD1. LSD1-IN-49 hydrochloride irreversibly inhibits the enzymatic activity of LSD1 by forming an adduct with flavin adenine dinucleotide (FAD) in the binding pocket of LSD1. LSD1-IN-49 hydrochloride is applicable to research related to schizophrenia, autism spectrum disorder and Huntington's disease .
Cat. No.: HY-E70989
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D-Fructose Dehydrogenase, Gluconobacter industrius (EC 1.1.99.11) is a heterotrimeric membrane-bound enzyme commonly seen in various Gluconobacter sp. especially in Gluconobacter japonicus (Gluconobacter industrius) .D-Fructose Dehydrogenase consists of subunits I (67kDa), II (51 kDa), and III (20 kDa) and catalyzes the oxidation of D-fructose to produce 5-keto-D-fructose. D-Fructose Dehydrogenase is a flavoprotein-cytochrome c complex with subunits I and II covalently bound to flavin adenine dinucleotide (FAD) and heme C as prosthetic groups, respectively.
Cat. No.: HY-E70989A
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D-Fructose Dehydrogenase, Gluconobacter industrius (EC 1.1.99.11) is a heterotrimeric membrane-bound enzyme commonly seen in various Gluconobacter sp. especially in Gluconobacter japonicus (Gluconobacter industrius) .D-Fructose Dehydrogenase consists of subunits I (67kDa), II (51 kDa), and III (20 kDa) and catalyzes the oxidation of D-fructose to produce 5-keto-D-fructose. D-Fructose Dehydrogenase is a flavoprotein-cytochrome c complex with subunits I and II covalently bound to flavin adenine dinucleotide (FAD) and heme C as prosthetic groups, respectively.
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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
