Recombinant Human ADH1A, His-tagged
| Cat.No. : | ADH1A-9416H |
| Product Overview : | Recombinant Human ADH1A protein, fused to His-tag, was expressed in E.coli and purified by Ni-sepharose. |
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| Description : | This gene encodes a member of the alcohol dehydrogenase family. The encoded protein is the alpha subunit of class I alcohol dehydrogenase, which consists of several homo- and heterodimers of alpha, beta and gamma subunits. Alcohol dehydrogenases catalyze the oxidation of alcohols to aldehydes. This gene is active in the liver in early fetal life but only weakly active in adult liver. This gene is found in a cluster with six additional alcohol dehydrogenase genes, including those encoding the beta and gamma subunits, on the long arm of chromosome 4. Mutations in this gene may contribute to variation in certain personality traits and substance dependence. |
| Source : | E.coli |
| Species : | Human |
| Tag : | His |
| Protein length : | 1-375a.a. |
| Storage : | The protein is stored in PBS buffer at -20℃. Avoid repeated freezing and thawing cycles. |
| Storage Buffer : | 1M PBS (58mM Na2HPO4,17mM NaH2PO4, 68mM NaCl, pH8. ) added with 300mM Imidazole and 0.7% Sarcosyl, 15%glycerol. |
| Gene Name : | ADH1A alcohol dehydrogenase 1A (class I), alpha polypeptide [ Homo sapiens ] |
| Official Symbol : | ADH1A |
| Synonyms : | ADH1A; alcohol dehydrogenase 1A (class I), alpha polypeptide; ADH1; alcohol dehydrogenase 1A; ADH, alpha subunit; aldehyde reductase; alcohol dehydrogenase subunit alpha; alcohol dehydrogenase 1 (class I), alpha polypeptide; |
| Gene ID : | 124 |
| mRNA Refseq : | NM_000667 |
| Protein Refseq : | NP_000658 |
| MIM : | 103700 |
| UniProt ID : | P07327 |
| Chromosome Location : | 4q23 |
| Pathway : | Biological oxidations, organism-specific biosystem; Drug metabolism - cytochrome P450, organism-specific biosystem; Drug metabolism - cytochrome P450, conserved biosystem; Ethanol oxidation, organism-specific biosystem; Fatty Acid Omega Oxidation, organism-specific biosystem; Fatty acid metabolism, organism-specific biosystem; Fatty acid metabolism, conserved biosystem; |
| Function : | alcohol dehydrogenase activity, zinc-dependent; metal ion binding; nucleotide binding; oxidoreductase activity; protein binding; zinc ion binding; |
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For Research Use Only. Not intended for any clinical use. No products from Creative BioMart may be resold, modified for resale or used to manufacture commercial products without prior written approval from Creative BioMart.
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Q&As (10)
Ask a questionThe expression of ADH1A is regulated by specific mechanisms, including transcriptional and post-transcriptional regulation, which can respond to alcohol exposure or metabolic factors such as hormonal signaling.
ADH1A requires specific cofactors or coenzymes, such as NAD+ or NADH, for its activity, serving as electron carriers and modulators of ADH1A function.
ADH1A plays a significant role in alcohol metabolism, showing specific catalytic efficiency and substrate specificity for the conversion of alcohol to acetaldehyde.
ADH1A deficiency or knockout in experimental models leads to altered alcohol metabolism and related phenotypes, such as decreased alcohol clearance and increased sensitivity to alcohol-induced effects.
ADH1A exhibits a tissue-specific expression pattern, with higher expression levels in certain organs such as the liver, and its distribution may differ from other ADH isoforms, reflecting functional specialization.
Genetic variations or polymorphisms in the ADH1A gene have been associated with differences in alcohol metabolism and susceptibility to alcohol-related disorders, highlighting the impact of genotype on phenotype.
Pharmacological agents or environmental factors can modulate ADH1A expression or activity, potentially influencing alcohol metabolism and providing avenues for therapeutic interventions or personalized medicine.
ADH1A has the capacity to metabolize other substrates beyond alcohol, suggesting its involvement in broader metabolic pathways and potential metabolic interactions.
ADH1A expression or activity may vary among different species or populations, influenced by genetic and environmental factors, contributing to inter-individual or inter-species differences in alcohol metabolism and tolerance.
The structural features of ADH1A, such as its active site and binding domains, are critical for its enzymatic activity and substrate recognition, enabling efficient alcohol oxidation.
Customer Reviews (2)
Write a reviewExhibits remarkable enzymatic activity under a wide range of pH conditions.
Provides reliable and consistent results in protein folding and unfolding studies.
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