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ADH-6 TFA is a tripyridylamide compound. ADH-6 abrogates self-assembly of the aggregation-nucleating subdomain of mutant p53 DBD. ADH-6 TFA targets and dissociates mutant p53 aggregates in human cancer cells, which restores p53's transcriptional activity, leading to cell cycle arrest and apoptosis. ADH-6 TFA has the potential for the research of cancer diseases .
ADH-503 ((Z)-Leukadherin-1 choline) is an orally active and allosteric CD11b agonist. ADH-503 leads to the repolarization of tumor-associated macrophages, reduction in the number of tumor-infiltrating immunosuppressive myeloid cells, and enhances dendritic cell responses .
Argipressin (diacetate) (AVP (diacetate), also known as antidiuretic hormone (ADH)) is a 9 amino acid neuropeptide secreted by the posterior pituitary. Argipressin (diacetate) (AVP (diacetate)) can regulate the biological effects of fluid balance, osmolality and cardiovascular through three separate G-protein coupled receptors (GPCRs), namely Avpr1a (V1a), Avpr1b (V1b) and Avpr2 (V2). Argipressin (diacetate) (AVP (diacetate)) also have potentially important effects on centrally regulated metabolic processes .
ADH-6 is a tripyridylamide compound. ADH-6 abrogates self-assembly of the aggregation-nucleating subdomain of mutant p53 DBD. ADH-6 targets and dissociates mutant p53 aggregates in human cancer cells, which restores p53's transcriptional activity, leading to cell cycle arrest and apoptosis. ADH-6 has the potential for the research of cancer diseases[1].
ADH-353 can inhibit Aβ fibrillation and reduce Aβ-induced cytotoxicity in SH-SY5Y and N2a cells. ADH-353 can be used in Alzheimer's disease-related research .
ADH4 Human Pre-designed siRNA Set A contains three designed siRNAs for ADH4 gene (Human), as well as a negative control, a positive control, and a FAM-labeled negative control.
ADH5 Human Pre-designed siRNA Set A contains three designed siRNAs for ADH5 gene (Human), as well as a negative control, a positive control, and a FAM-labeled negative control.
Adh5 Mouse Pre-designed siRNA Set A contains three designed siRNAs for Adh5 gene (Mouse), as well as a negative control, a positive control, and a FAM-labeled negative control.
Adh5 Rat Pre-designed siRNA Set A contains three designed siRNAs for Adh5 gene (Rat), as well as a negative control, a positive control, and a FAM-labeled negative control.
ADH6 Human Pre-designed siRNA Set A contains three designed siRNAs for ADH6 gene (Human), as well as a negative control, a positive control, and a FAM-labeled negative control.
ADH7 Human Pre-designed siRNA Set A contains three designed siRNAs for ADH7 gene (Human), as well as a negative control, a positive control, and a FAM-labeled negative control.
ADH1A Human Pre-designed siRNA Set A contains three designed siRNAs for ADH1A gene (Human), as well as a negative control, a positive control, and a FAM-labeled negative control.
ADH1B Human Pre-designed siRNA Set A contains three designed siRNAs for ADH1B gene (Human), as well as a negative control, a positive control, and a FAM-labeled negative control.
ADH1C Human Pre-designed siRNA Set A contains three designed siRNAs for ADH1C gene (Human), as well as a negative control, a positive control, and a FAM-labeled negative control.
(Z)-Leukadherin-1 (ADH-503 free base) is an orally active and allosteric CD11b agonist. (Z)-Leukadherin-1 leads to the repolarization of tumor-associated macrophages, reduction in the number of tumor-infiltrating immunosuppressive myeloid cells, and enhances dendritic cell responses .
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 .
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 .
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 .
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 .
Argipressin (Arg8-vasopressin) (acetate) binds to the V1, V2, V3-vascular arginine vasopressin receptor, with a Kd value of 1.31 nM in A7r5 rat aortic smooth muscle cells for V1 .
Argipressin (diacetate) (AVP (diacetate), also known as antidiuretic hormone (ADH)) is a 9 amino acid neuropeptide secreted by the posterior pituitary. Argipressin (diacetate) (AVP (diacetate)) can regulate the biological effects of fluid balance, osmolality and cardiovascular through three separate G-protein coupled receptors (GPCRs), namely Avpr1a (V1a), Avpr1b (V1b) and Avpr2 (V2). Argipressin (diacetate) (AVP (diacetate)) also have potentially important effects on centrally regulated metabolic processes .
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) .
Argipressin (Arg8-vasopressin) (acetate) binds to the V1, V2, V3-vascular arginine vasopressin receptor, with a Kd value of 1.31 nM in A7r5 rat aortic smooth muscle cells for V1 .
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 .
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 .
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. The total length of ADH Protein, Geobacillus stearothermophilus is 338 a.a., .
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. The total length of ADH Protein, Geobacillus stearothermophilus (His, Strep) is 338 a.a., .
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. The total length of ADH Protein, Drosophila melanogaster is 255 a.a., .
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. The total length of ADH Protein, Sulfurisphaera tokodaii is 346 a.a., .
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. The total length of ADH Protein, Drosophila melanogaster (His, Strep) is 255 a.a., .
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. The total length of ADH-HT Protein, Geobacillus stearothermophilus is 338 a.a., .
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. The total length of ADH6 Protein, Human is 368 a.a., .
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. The total length of ADH Protein, Sulfurisphaera tokodaii (His, Strep) is 346 a.a., .
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. The total length of ADH-HT Protein, Geobacillus stearothermophilus (His, Strep) is 338 a.a., .
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. The total length of ADH6 Protein, Human (GST) is 368 a.a., .
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. The total length of ADH4 Protein, Human is 380 a.a., .
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. The total length of ADH4 Protein, Human (GST) is 380 a.a., .
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. The total length of ADH1A Protein, Human is 375 a.a., .
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. The total length of ADH4 Protein, Saccharomyces cerevisiae is 381 a.a., .
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. The total length of ADH1C Protein, Human is 374 a.a., .
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. The total length of ADH1A Protein, Human (His) is 375 a.a., .
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. The total length of ADH4 Protein, Saccharomyces cerevisiae (His, Strep) is 381 a.a., .
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. The total length of ADH II Protein, Zymomonas mobilis subsp. mobilis is 382 a.a., .
ADH2 Protein, Geobacillus thermodenitrificans is the recombinant ADH2, expressed by E. coli , with tag Free labeled tag. The total length of ADH2 Protein, Geobacillus thermodenitrificans is 386 a.a., .
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. The total length of ADH II Protein, Zymomonas mobilis subsp. mobilis (His, Strep) is 382 a.a., .
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. The total length of adhT Protein, Geobacillus stearothermophilus is 336 a.a., .
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.
ADH1 Protein, Geobacillus thermodenitrificans (His, Strep) is the recombinant ADH1, expressed by E. coli , with Strep, His labeled tag. The total length of ADH1 Protein, Geobacillus thermodenitrificans (His, Strep) is 394 a.a., .
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. The total length of adhT Protein, Geobacillus stearothermophilus (His, Strep) is 336 a.a., .
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.
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.
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. The total length of Alcohol dehydrogenase Protein, Lentilactobacillus curieae is 345 a.a., .
Aldehyde reductase Protein, Gluconobacter oxydans (His) is the recombinant Aldehyde reductase protein, expressed by E. coli , with N-6*His labeled tag. The total length of Aldehyde reductase Protein, Gluconobacter oxydans (His) is 385 a.a., .
The hemagglutinin HA1 protein is essential for attachment of virions to host cells by binding to sialic acid-containing receptors, inducing virion internalization via clathrin-dependent or clathrin- and caveolin-independent pathways. As a class I viral fusion protein, HA1 determines host range restriction and virulence, mediating fusion between the virion membrane and the endosomal membrane. HA/Hemagglutinin Protein, H10N7 (ADH96304, sf9, His) is the recombinant Virus-derived HA/Hemagglutinin protein, expressed by Sf9 insect cells , with C-His labeled tag.
The hemagglutinin HA1 protein is essential for attachment of virions to host cells by binding to sialic acid-containing receptors, inducing virion internalization via clathrin-dependent or clathrin- and caveolin-independent pathways.As a class I viral fusion protein, HA1 determines host range restriction and virulence, mediating fusion between the virion membrane and the endosomal membrane.HA1/Hemagglutinin Protein, H10N7 (ADH96304, HEK293, His) is the recombinant Virus-derived HA1/Hemagglutinin protein, expressed by HEK293 , with C-His labeled tag.
ADH5 Antibody (YA1998) is a rabbit-derived non-conjugated IgG antibody (Clone NO.: YA1998), targeting ADH5, with a predicted molecular weight of 40 kDa (observed band size: 40 kDa). ADH5 Antibody (YA1998) can be used for WB, IHC-P, IP experiment in human background.
Alcohol Dehydrogenase Antibody (YA1948) is a rabbit-derived non-conjugated IgG antibody (Clone NO.: YA1948), targeting Alcohol Dehydrogenase, with a predicted molecular weight of 40 kDa (observed band size: 40 kDa). Alcohol Dehydrogenase Antibody (YA1948) can be used for WB, IHC-P, ICC/IF experiment in human, mouse, rat background.
ADH4 Human Pre-designed siRNA Set A contains three designed siRNAs for ADH4 gene (Human), as well as a negative control, a positive control, and a FAM-labeled negative control.
ADH5 Human Pre-designed siRNA Set A contains three designed siRNAs for ADH5 gene (Human), as well as a negative control, a positive control, and a FAM-labeled negative control.
Adh5 Mouse Pre-designed siRNA Set A contains three designed siRNAs for Adh5 gene (Mouse), as well as a negative control, a positive control, and a FAM-labeled negative control.
Adh5 Rat Pre-designed siRNA Set A contains three designed siRNAs for Adh5 gene (Rat), as well as a negative control, a positive control, and a FAM-labeled negative control.
ADH6 Human Pre-designed siRNA Set A contains three designed siRNAs for ADH6 gene (Human), as well as a negative control, a positive control, and a FAM-labeled negative control.
ADH7 Human Pre-designed siRNA Set A contains three designed siRNAs for ADH7 gene (Human), as well as a negative control, a positive control, and a FAM-labeled negative control.
ADH1A Human Pre-designed siRNA Set A contains three designed siRNAs for ADH1A gene (Human), as well as a negative control, a positive control, and a FAM-labeled negative control.
ADH1B Human Pre-designed siRNA Set A contains three designed siRNAs for ADH1B gene (Human), as well as a negative control, a positive control, and a FAM-labeled negative control.
ADH1C Human Pre-designed siRNA Set A contains three designed siRNAs for ADH1C gene (Human), as well as a negative control, a positive control, and a FAM-labeled negative control.
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