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alcohol dehydrogenase (ADH)

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By Targets:	Aldehyde Dehydrogenase (ALDH) (3) Bacterial (1) Drug Metabolite (2) Endogenous Metabolite (1) GABA Receptor (1) Reference Standards (1)
By Research Areas:	Infection (1) Inflammation/Immunology (2) Metabolic Disease (5) Neurological Disease (2)

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Cat. No.	Product Name	Target	Research Areas	Chemical Structure

HY-164690A

Nicotinamide-guanine dinucleotide sodium	Endogenous Metabolite	Metabolic Disease
Nicotinamide-guanine dinucleotide sodium, a NAD sodium (HY-B0445A) analog, is an oxidized forms of nicotinamide guanine dinucleotide. Nicotinamide-guanine dinucleotide sodium serves as coenzymes for alcohol dehydrogenase (ADH) in vitro .

HY-118980

Sorbitol dehydrogenase-IN-1	Aldehyde Dehydrogenase (ALDH)	Metabolic Disease
Sorbitol dehydrogenase-IN-1 is a potent and orally active sorbitol dehydrogenase inhibitor with IC₅₀ s of 4, 5 nM for rat and human, respectively. Sorbitol Dehydrogenase (SDH) is an enzyme that belongs to the zinc-containing alcohol dehydrogenase (ADH) family. ADH and ALDH are enzymes that work together to metabolize alcohol .

HY-N1177

Taraxerone	Aldehyde Dehydrogenase (ALDH)	Inflammation/Immunology
Taraxerone is isolated from Sedum sarmentosum. Taraxerone enhances effects on alcohol dehydrogenase (ADH) and acetaldehyde dehydrogenase (ALDH) activities with EC₅₀ values of 512.42 and 500.16 μM, respectively .

HY-B1229

Isovaleramide 1 Publications Verification 3-Methylbutanamide	GABA Receptor	Neurological Disease Metabolic Disease
Isovaleramide (3-Methylbutanamide) is an orally active anticonvulsant. Isovaleramide inhibits alcohol dehydrogenase (ADH) activity and regulates GABAergic system. Isovaleramide reduces acute kidney injury. Isovaleramide has antiepileptic, anxiolytic, sedative and hypnotic effects[1] .

HY-33914

4-Hydroxymethylpyrazole	Drug Metabolite	Metabolic Disease
4-Hydroxymethylpyrazole is the primary metabolite of Fomepizole (HY-B0876) produced through hepatic oxidative metabolism. 4-Hydroxymethylpyrazole exhibits a plasma concentration that is positively correlated with the administered dosage of Fomepizole, and it demonstrates a relatively short half-life. 4-Hydroxymethylpyrazole demonstrates inhibitory effects on alcohol dehydrogenase (ADH) in both humans and monkeys, but its inhibition constant is significantly higher than that of Fomepizole, rendering its in vivo impact negligible .

HY-N13031

Bellericagenin A	Bacterial	Infection
Bellericagenin A is a pentacyclic triterpenic acid isolated from the bark of Terminalia bellerica. Bellericagenin A exhibits antimicrobial activity. Bellericagenin A exhibits a high affinity to **alcohol dehydrogenase** (ADH), which has the potential for ameliorating the alcoholic liver injury .

HY-N16144

Osmanthuside H	Aldehyde Dehydrogenase (ALDH)	Neurological Disease Inflammation/Immunology
Osmanthuside H (Compound 1), a phenylethanoid glycoside (PhG), is a **alcohol dehydrogenase (ADH) inhibitor with an IC₅₀** of 175.4 μg/mL. Osmanthuside H can be isolated from the leaves of persimmon Diospyros kaki. Osmanthuside H has anti-inflammatory and neuroprotective activities .

HY-33914R

4-Hydroxymethylpyrazole (Standard)	Drug Metabolite Reference Standards	Metabolic Disease
4-Hydroxymethylpyrazole (Standard) is an analytical standard for 4-Hydroxymethylpyrazole (HY-33914). This product is intended for research and analytical applications. 4-Hydroxymethylpyrazole is the primary metabolite of fomepizole (HY-B0876) via hepatic oxidative metabolism. 4-Hydroxymethylpyrazole exhibits a plasma concentration that is positively correlated with the administered dosage of Fomepizole, and it demonstrates a relatively short half-life. 4-Hydroxymethylpyrazole inhibits alcohol dehydrogenase (ADH) in humans and monkeys, but the inhibition constant is much higher than that of fomepizole and is therefore negligible in vivo

Cat. No.	Product Name	Target	Research Area

HY-122297

H-Arg-Phe-OH	Peptides	Others
H-Arg-Phe-OH is an amphipathic peptide. H-Arg-Phe-OH has the ability to induce native-like protein aggregation. H-Arg-Phe-OH can induce aggregation of the neutral model protein yeast alcohol dehydrogenase (ADH) .

Taraxerone	Triterpenes Classification of Application Fields Terpenoids Crassulaceae Astragalus oleifolius DC. Source classification Sedum sarmentosum Bunge Plants Compositae Inflammation/Immunology Disease Research Fields	Aldehyde Dehydrogenase (ALDH)
Taraxerone is isolated from Sedum sarmentosum. Taraxerone enhances effects on alcohol dehydrogenase (ADH) and acetaldehyde dehydrogenase (ALDH) activities with EC₅₀ values of 512.42 and 500.16 μM, respectively .

Isovaleramide 1 Publications Verification 3-Methylbutanamide	Natural Products other families Source classification Plants	GABA Receptor
Isovaleramide (3-Methylbutanamide) is an orally active anticonvulsant. Isovaleramide inhibits alcohol dehydrogenase (ADH) activity and regulates GABAergic system. Isovaleramide reduces acute kidney injury. Isovaleramide has antiepileptic, anxiolytic, sedative and hypnotic effects[1] .

4-Hydroxymethylpyrazole	Natural Products Classification of Application Fields Source classification Other Diseases Endogenous metabolite Disease Research Fields	Drug Metabolite
4-Hydroxymethylpyrazole is the primary metabolite of Fomepizole (HY-B0876) produced through hepatic oxidative metabolism. 4-Hydroxymethylpyrazole exhibits a plasma concentration that is positively correlated with the administered dosage of Fomepizole, and it demonstrates a relatively short half-life. 4-Hydroxymethylpyrazole demonstrates inhibitory effects on alcohol dehydrogenase (ADH) in both humans and monkeys, but its inhibition constant is significantly higher than that of Fomepizole, rendering its in vivo impact negligible .

Bellericagenin A	Terpenoids Combretaceae Source classification Plants Pentacyclic Triterpenoids Terminalia bellirica (Gaertn.) Roxb.	Bacterial
Bellericagenin A is a pentacyclic triterpenic acid isolated from the bark of Terminalia bellerica. Bellericagenin A exhibits antimicrobial activity. Bellericagenin A exhibits a high affinity to **alcohol dehydrogenase** (ADH), which has the potential for ameliorating the alcoholic liver injury .

Osmanthuside H	Monophenols Ipomoea nil (Linnaeus) Roth Source classification Phenols Plants Convolvulaceae	Aldehyde Dehydrogenase (ALDH)
Osmanthuside H (Compound 1), a phenylethanoid glycoside (PhG), is a **alcohol dehydrogenase (ADH) inhibitor with an IC₅₀** of 175.4 μg/mL. Osmanthuside H can be isolated from the leaves of persimmon Diospyros kaki. Osmanthuside H has anti-inflammatory and neuroprotective activities .

4-Hydroxymethylpyrazole (Standard)	Natural Products Source classification Endogenous metabolite	Drug Metabolite Reference Standards
4-Hydroxymethylpyrazole (Standard) is an analytical standard for 4-Hydroxymethylpyrazole (HY-33914). This product is intended for research and analytical applications. 4-Hydroxymethylpyrazole is the primary metabolite of fomepizole (HY-B0876) via hepatic oxidative metabolism. 4-Hydroxymethylpyrazole exhibits a plasma concentration that is positively correlated with the administered dosage of Fomepizole, and it demonstrates a relatively short half-life. 4-Hydroxymethylpyrazole inhibits alcohol dehydrogenase (ADH) in humans and monkeys, but the inhibition constant is much higher than that of fomepizole and is therefore negligible in vivo

Species:	Human (11)
Tag:	His (13) SUMO (1) Tag Free (14) Strep (8) GST (2)
Source:	HEK293 (1) E. coli (28)

Cat. No.	Compare	Product Name	Species	Source

HY-P702144

	Alcohol dehydrogenase Protein, Lentilactobacillus curieae ADH; alcohol dehydrogenase	Others	E. coli
	The alcohol dehydrogenase protein is part of the zinc-containing alcohol dehydrogenase family and catalyzes the oxidation of alcohol, which is critical in various metabolic processes. It is primarily active in the liver, where it converts ethanol into acetaldehyde during the breakdown of ethanol. Alcohol dehydrogenase Protein, Lentilactobacillus curieae is the recombinant Alcohol dehydrogenase protein, expressed by E. coli , with tag free.

HY-P702138

	ADH Protein, Geobacillus stearothermophilus adh; alcohol dehydrogenase; ADH	Others	E. coli
	ADH protein, active with primary alcohols, including methanol as a substrate, demonstrates specific enzymatic activity in alcohol metabolism. ADH Protein, Geobacillus stearothermophilus is the recombinant ADH protein, expressed by E. coli , with tag free.

HY-P701937

	ADH Protein, Drosophila melanogaster Adh; alcohol dehydrogenase	Others	E. coli
	ADH Protein, Drosophila melanogaster (S2-I256) is a dimeric Zn-containing enzyme in the oxidoreductase family with acetaldehyde dehydrogenase and alcohol dehydrogenase activity, therefore, can oxidize primary and secondary alcohols. ADH Protein, Drosophila melanogaster (S2-I256) is E.coli-sourced and tag-free, the initiator methionine is naturally removed. ADH Protein, Drosophila melanogaster is the recombinant ADH protein, expressed by E. coli , with tag free.

HY-P701928

	ADH4 Protein, Saccharomyces cerevisiae ADH4; alcohol dehydrogenase 4; alcohol dehydrogenase IV; ADHIV	Others	E. coli
	The ADH4 protein is a specific alcohol dehydrogenase that primarily functions as a mitochondrial formaldehyde dehydrogenase with a unique ethanol preference. It does not affect ethanol production and exhibits reduced activity on primary alcohols with four or more carbon atoms. ADH4 Protein, Saccharomyces cerevisiae is the recombinant ADH4 protein, expressed by E. coli , with tag free.

HY-P701931

	ADH6 Protein, Human ADH6; alcohol dehydrogenase 6	Human	E. coli
	The ADH6 protein is considered an alcohol dehydrogenase and is critical in cellular metabolism. It catalyzes the NAD-dependent oxidation of primary alcohols to aldehydes and promotes the oxidation of secondary alcohols to ketones. ADH6 Protein, Human is the recombinant human-derived ADH6 protein, expressed by E. coli , with tag free.

HY-P701926

	ADH4 Protein, Human ADH4; All-trans-retinol dehydrogenase [NAD(+)] ADH4; alcohol dehydrogenase 4; alcohol dehydrogenase class II pi chain	Human	E. coli
	ADH4 Protein, an enzyme, is involved in the metabolism of alcohol and other toxic compounds. Dysregulation of ADH4 Protein has been linked to alcohol-induced liver damage and susceptibility to certain diseases. Targeting ADH4 Protein may offer potential therapeutic interventions by modulating alcohol metabolism, protecting against liver damage, and reducing disease risk. ADH4 Protein, Human is the recombinant human-derived ADH4 protein, expressed by E. coli , with tag free.

HY-P701933

	ADH II Protein, Zymomonas mobilis subsp. mobilis adhB; alcohol dehydrogenase 2; alcohol dehydrogenase II; ADH II	Others	E. coli
	ADH II Protein, an iron-dependent alcohol dehydrogenase, is pivotal in converting pyruvate to ethanol. This enzymatic activity is essential for pathways involving ethanol formation, contributing to physiological processes in alcohol metabolism. Its iron dependency underscores intricate biochemical mechanisms, emphasizing ADH II's significance in producing ethanol from pyruvate within relevant biological contexts. ADH II Protein, Zymomonas mobilis subsp. mobilis is the recombinant ADH II protein, expressed by E. coli , with tag free.

HY-P701932

	ADH6 Protein, Human (GST) ADH6; alcohol dehydrogenase 6	Human	E. coli
	The ADH6 protein is considered an alcohol dehydrogenase and is critical in cellular metabolism. It catalyzes the NAD-dependent oxidation of primary alcohols to aldehydes and promotes the oxidation of secondary alcohols to ketones. ADH6 Protein, Human (GST) is the recombinant human-derived ADH6 protein, expressed by E. coli , with N-GST labeled tag.

HY-P701924

	ADH1A Protein, Human ADH1A; alcohol dehydrogenase 1A; alcohol dehydrogenase subunit alpha	Human	E. coli
	ADH1A Protein, recognized as alcohol dehydrogenase, is pivotal in cellular metabolism. It catalyzes the oxidation of both primary and secondary alcohols. Despite ethanol being a poor substrate, ADH1A's broad specificity underscores its importance in oxidizing diverse alcohols, maintaining cellular redox balance. The enzyme's versatility highlights its crucial role in alcohol-related metabolic pathways. ADH1A Protein, Human is the recombinant human-derived ADH1A protein, expressed by E. coli , with tag free.

HY-P701935

	ADH1C Protein, Human ADH1C; alcohol dehydrogenase 1C; alcohol dehydrogenase subunit gamma	Human	E. coli
	ADH1C Proteinas, an alcohol dehydrogenase, plays a pivotal role in ethanol catabolism, exhibiting heightened activity in ethanol oxidation. ADH1C Protein, Human is the recombinant human-derived ADH1C protein, expressed by E. coli , with tag free.

HY-P701927

	ADH4 Protein, Human (GST) ADH4; All-trans-retinol dehydrogenase [NAD(+)] ADH4; alcohol dehydrogenase 4; alcohol dehydrogenase class II pi chain	Human	E. coli
	ADH4 Protein, an enzyme, is involved in the metabolism of alcohol and other toxic compounds. Dysregulation of ADH4 Protein has been linked to alcohol-induced liver damage and susceptibility to certain diseases. Targeting ADH4 Protein may offer potential therapeutic interventions by modulating alcohol metabolism, protecting against liver damage, and reducing disease risk. ADH4 Protein, Human (GST) is the recombinant human-derived ADH4 protein, expressed by E. coli , with N-GST labeled tag.

HY-P701936

	ADH Protein, Sulfurisphaera tokodaii adh; NAD-dependent alcohol dehydrogenase	Others	E. coli
	ADH protein, active with primary alcohols, including methanol as a substrate, demonstrates specific enzymatic activity in alcohol metabolism. ADH Protein, Sulfurisphaera tokodaii is the recombinant ADH protein, expressed by E. coli , with tag free.

HY-P702133

	ADH-HT Protein, Geobacillus stearothermophilus alcohol dehydrogenase; ADH-HT	Others	E. coli
	The ADH-HT protein is a thermophilic NAD(+)-dependent alcohol dehydrogenase that functions primarily as an alcohol dehydrogenase. This protein plays a vital role in ethanol metabolism by catalyzing the conversion of ethanol to acetaldehyde using NAD(+) as a cofactor in the process. ADH-HT Protein, Geobacillus stearothermophilus is the recombinant ADH-HT protein, expressed by E. coli , with tag free.

HY-P702139

	ADH Protein, Geobacillus stearothermophilus (His, StrepⅡ) adh; alcohol dehydrogenase; ADH	Others	E. coli
	ADH protein, active with primary alcohols, including methanol as a substrate, demonstrates specific enzymatic activity in alcohol metabolism. ADH Protein, Geobacillus stearothermophilus (His, Strep) is the recombinant ADH protein, expressed by E. coli , with N-Strep, N-6*His labeled tag.

HY-P701929

	ADH4 Protein, Saccharomyces cerevisiae (His, StrepⅡ) ADH4; alcohol dehydrogenase 4; alcohol dehydrogenase IV; ADHIV	Others	E. coli
	The ADH4 protein is a specific alcohol dehydrogenase that primarily functions as a mitochondrial formaldehyde dehydrogenase with a unique ethanol preference. It does not affect ethanol production and exhibits reduced activity on primary alcohols with four or more carbon atoms. ADH4 Protein, Saccharomyces cerevisiae (His, Strep) is the recombinant ADH4 protein, expressed by E. coli , with N-Strep, N-6*His labeled tag.

HY-P72071

	ADH1B Protein, Human (His-SUMO) ADH beta subunit; ADH1B; ADH1B_HUMAN; ADH2; alcohol dehydrogenase 1B; alcohol dehydrogenase 2 class I; beta polypeptide; alcohol dehydrogenase 2; alcohol dehydrogenase subunit beta; Aldehyde reductase; DKFZp686C06125; OTTHUMP00000220192	Human	E. coli
	ADH1B Protein, Human (His-SUMO) is an enzyme encoded by the ADH1B gene and is involved in the main ethanol metabolism pathway.

HY-P701925

	ADH1A Protein, Human (His) ADH1A; alcohol dehydrogenase 1A; alcohol dehydrogenase subunit alpha	Human	E. coli
	ADH1A Protein, recognized as alcohol dehydrogenase, is pivotal in cellular metabolism. It catalyzes the oxidation of both primary and secondary alcohols. Despite ethanol being a poor substrate, ADH1A's broad specificity underscores its importance in oxidizing diverse alcohols, maintaining cellular redox balance. The enzyme's versatility highlights its crucial role in alcohol-related metabolic pathways. ADH1A Protein, Human (His) is the recombinant human-derived ADH1A protein, expressed by E. coli , with N-6*His labeled tag.

HY-P701939

	ADH Protein, Drosophila melanogaster (His, StrepⅡ) Adh; alcohol dehydrogenase	Others	E. coli
	ADH Protein, Drosophila melanogaster (S2-I256) is a dimeric Zn-containing enzyme in the oxidoreductase family with acetaldehyde dehydrogenase and alcohol dehydrogenase activity, therefore, can oxidize primary and secondary alcohols. ADH Protein, Drosophila melanogaster (S2-I256) is E.coli-sourced and tag-free, the initiator methionine is naturally removed. ADH Protein, Drosophila melanogaster (His, Strep) is the recombinant ADH protein, expressed by E. coli , with N-Strep, N-6*His labeled tag.

HY-P701934

	ADH II Protein, Zymomonas mobilis subsp. mobilis (His, StrepⅡ) adhB; alcohol dehydrogenase 2; alcohol dehydrogenase II; ADH II	Others	E. coli
	ADH II Protein, an iron-dependent alcohol dehydrogenase, is pivotal in converting pyruvate to ethanol. This enzymatic activity is essential for pathways involving ethanol formation, contributing to physiological processes in alcohol metabolism. Its iron dependency underscores intricate biochemical mechanisms, emphasizing ADH II's significance in producing ethanol from pyruvate within relevant biological contexts. ADH II Protein, Zymomonas mobilis subsp. mobilis (His, Strep) is the recombinant ADH II protein, expressed by E. coli , with N-Strep, N-6*His labeled tag.

HY-P702823

	ADH5 Protein, Human ADH5; alcohol dehydrogenase class-3; alcohol dehydrogenase 5; alcohol dehydrogenase class chi chain; alcohol dehydrogenase class-III; Glutathione-dependent formaldehyde dehydrogenase; FALDH; FDH; GSH-FDH; S-(hydroxymethyl)glutathione dehydrogenase	Human	E. coli
	The ADH5 protein catalyzes the oxidation of long-chain primary alcohols and S-(hydroxymethyl) glutathione. It also oxidizes long-chain omega-hydroxy fatty acids, producing intermediate aldehydes and end products. However, it is ineffective in oxidizing ethanol. ADH5 is crucial for clearing cytotoxic formaldehyde, which causes DNA damage. ADH5 Protein, Human is the recombinant human-derived ADH5 protein, expressed by E. coli , with no tag.

HY-P701930

	ADH5 Protein, Human (His) ADH5; alcohol dehydrogenase class-3; alcohol dehydrogenase 5; alcohol dehydrogenase class chi chain; alcohol dehydrogenase class-III; Glutathione-dependent formaldehyde dehydrogenase; FALDH; FDH; GSH-FDH; S-(hydroxymethyl)glutathione dehydrogenase	Human	E. coli
	The ADH5 protein catalyzes the oxidation of long-chain primary alcohols and S-(hydroxymethyl) glutathione. It also oxidizes long-chain omega-hydroxy fatty acids, producing intermediate aldehydes and end products. However, it is ineffective in oxidizing ethanol. ADH5 is crucial for clearing cytotoxic formaldehyde, which causes DNA damage. ADH5 Protein, Human (His) is the recombinant human-derived ADH5 protein, expressed by E. coli , with N-His labeled tag.

HY-P703457

	ADH2 Protein, Geobacillus thermodenitrificans Long-chain-alcohol dehydrogenase 2; alcohol dehydrogenase 2; ADH2; Fatty alcohol oxidoreductase 2; adh2; Geobacillus thermodenitrificans (strain NG80-2); ADH2; Oxidoreductase; 1.1.1.192	Others	E. coli
	ADH2 Protein, Geobacillus thermodenitrificans is the recombinant ADH2, expressed by E. coli, with tag free labeled tag.

HY-P701938

	ADH Protein, Sulfurisphaera tokodaii (His, StrepⅡ) adh; NAD-dependent alcohol dehydrogenase	Others	E. coli
	ADH protein, active with primary alcohols, including methanol as a substrate, demonstrates specific enzymatic activity in alcohol metabolism. ADH Protein, Sulfurisphaera tokodaii (His, Strep) is the recombinant ADH protein, expressed by E. coli , with N-Strep, N-6*His labeled tag.

HY-P702134

	ADH-HT Protein, Geobacillus stearothermophilus (His, StrepⅡ) alcohol dehydrogenase; ADH-HT	Others	E. coli
	The ADH-HT protein is a thermophilic NAD(+)-dependent alcohol dehydrogenase that functions primarily as an alcohol dehydrogenase. This protein plays a vital role in ethanol metabolism by catalyzing the conversion of ethanol to acetaldehyde using NAD(+) as a cofactor in the process. ADH-HT Protein, Geobacillus stearothermophilus (His, Strep) is the recombinant ADH-HT protein, expressed by E. coli , with N-Strep, N-6*His labeled tag.

HY-P702140

	adhT Protein, Geobacillus stearothermophilus adhT; alcohol dehydrogenase; ADH-T	Others	E. coli
	adhT, a NAD(+)-dependent alcohol dehydrogenase, catalyzes the oxidation of alcohols, converting them to aldehydes or ketones while reducing NAD(+) to NADH. Its specificity enables participation in diverse metabolic pathways, contributing to alcohol breakdown and NADH regeneration. Integral to alcohol metabolism, adhT maintains cellular redox balance and energy homeostasis, crucial for processes like fermentation and energy production. adhT Protein, Geobacillus stearothermophilus is the recombinant adhT protein, expressed by E. coli , with tag free.

HY-P703456

	ADH1 Protein, Geobacillus thermodenitrificans (His, Strep) Long-chain-alcohol dehydrogenase 1; alcohol dehydrogenase 1; ADH1; Fatty alcohol oxidoreductase 1; Glycerol dehydrogenase; 1.1.1.6; adh1; Geobacillus thermodenitrificans (strain NG80-2); ADH1; Oxidoreductase; 1.1.1.192	Others	E. coli
	ADH1 Protein, Geobacillus thermodenitrificans (His, Strep) is the recombinant ADH1, expressed by E. coli, with Strep, His labeled tag.

HY-P702141

	adhT Protein, Geobacillus stearothermophilus (His, StrepⅡ) adhT; alcohol dehydrogenase; ADH-T	Others	E. coli
	adhT, a NAD(+)-dependent alcohol dehydrogenase, catalyzes the oxidation of alcohols, converting them to aldehydes or ketones while reducing NAD(+) to NADH. Its specificity enables participation in diverse metabolic pathways, contributing to alcohol breakdown and NADH regeneration. Integral to alcohol metabolism, adhT maintains cellular redox balance and energy homeostasis, crucial for processes like fermentation and energy production. adhT Protein, Geobacillus stearothermophilus (His, Strep) is the recombinant adhT protein, expressed by E. coli , with N-Strep, N-6*His labeled tag.

HY-P702147

	Aldehyde reductase Protein, Gluconobacter oxydans (His) ADH; NADH-dependent iron-containing alcohol dehydrogenase	Others	E. coli
	Aldehyde reductase Protein, Gluconobacter oxydans (His) is the recombinant Aldehyde reductase protein, expressed by E. coli, with N-6*His labeled tag.

HY-P7473

	ADH7 Protein, Human (HEK293, His) rHuADH7, His; alcohol dehydrogenase class 4 mu, sigma chain; ADH-7	Human	HEK293
	ADH7 Protein, Human (HEK293, His) is human recombinant ADH7 with His tag at the C-terminus. ADH7 Protein, Human (HEK293, His) is expressed by Mammalian expression system and the target gene encoding Met1-Phe386 is expressed.

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HY-P82203

	Alcohol Dehydrogenase Antibody (YA1948) ADH; ADH1; ADH1A; Aldehyde reductase	WB, IHC-P, ICC/IF	Human, Mouse, Rat
	Alcohol Dehydrogenase Antibody (YA1948) is a Rabbit-derived and non-conjugated IgG monoclonal antibody, targeting to Alcohol Dehydrogenase.

HY-P86764

	ADH4 Antibody(YA6457) Ac1002 antibody; ADH 4 antibody; ADH-1 antibody; ADH-2 antibody; ADH2 antibody; Adh4 antibody; ADH4_HUMAN antibody; alcohol dehydrogenase 4 (class II) pi polypeptide antibody; alcohol dehydrogenase 4 antibody; alcohol dehydrogenase class II pi chain antibody; Ac1002 antibody; ADH 4 antibody; ADH-1 antibody; ADH-2 antibody; ADH2 antibody; Adh4 antibody; ADH4_HUMAN antibody; alcohol dehydrogenase 4 (class II) pi polypeptide antibody; alcohol dehydrogenase 4 antibody; alcohol dehydrogenase class II pi chain antibody; alcohol dehydrogenase pi isozyme ADH class II antibody; Aldehyde reductase antibody; Class II alcohol dehydrogenase 4 pi subunit antibody;	WB, IHC-P	Human
	ADH4 Antibody(YA6457) is a Rabbit-derived and non-conjugated IgG monoclonal antibody, targeting to ADH4.

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alcohol dehydrogenase (ADH)

Inhibitors & Agonists

Peptides

NaturalProducts

Recombinant Proteins

Antibodies

Natural
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