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Recombinant Human ADH1C

Cat.No. : ADH1C-27094TH
Product Overview : Recombinant full length Human ADH1C with N terminal proprietary tag. Predicted MW 67.32 kDa.
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  • Gene Information
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Description : This gene encodes class I alcohol dehydrogenase, gamma subunit, which is a member of the alcohol dehydrogenase family. Members of this enzyme family metabolize a wide variety of substrates, including ethanol, retinol, other aliphatic alcohols, hydroxysteroids, and lipid peroxidation products. Class I alcohol dehydrogenase, consisting of several homo- and heterodimers of alpha, beta, and gamma subunits, exhibits high activity for ethanol oxidation and plays a major role in ethanol catabolism. Three genes encoding alpha, beta and gamma subunits are tandemly organized in a genomic segment as a gene cluster.
Protein length : 375 amino acids
Molecular Weight : 67.320kDa inclusive of tags
Source : Wheat germ
Form : Liquid
Purity : Proprietary Purification
Storage buffer : pH: 8.00Constituents:0.3% Glutathione, 0.79% Tris HCl
Storage : Shipped on dry ice. Upon delivery aliquot and store at -80oC. Avoid freeze / thaw cycles.
Sequences of amino acids : MSTAGKVIKCKAAVLWELKKPFSIEEVEVAPPKAHEVRIK MVAAGICRSDEHVVSGNLVTPLPVILGHEAAGIVESVGEG VTTVKPGDKVIPLFTPQCGKCRICKNPESNYCLKNDLGNP RGTLQDGTRRFTCSGKPIHHFVGVSTFSQYTVVDENAVAK IDAASPLEKVCLIGCGFSTGYGSAVKVAKVTPGSTCAVFG LGGVGLSVVMGCKAAGAARIIAVDINKDKFAKAKELGATE CINPQDYKKPIQEVLKEMTDGGVDFSFEVIGRLDTMMASL LCCHEACGTSVIVGVPPDSQNLSINPMLLLTGRTWKGAIF GGFKSKESVPKLVADFMAKKFSLDALITNILPFEKINEGF DLLRSGKSIRTVLTF
Sequence Similarities : Belongs to the zinc-containing alcohol dehydrogenase family.
Gene Name : ADH1C alcohol dehydrogenase 1C (class I), gamma polypeptide [ Homo sapiens ]
Official Symbol : ADH1C
Synonyms : ADH1C; alcohol dehydrogenase 1C (class I), gamma polypeptide; ADH3; alcohol dehydrogenase 1C;
Gene ID : 126
mRNA Refseq : NM_000669
Protein Refseq : NP_000660
MIM : 103730
Uniprot ID : P00326
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;
Function : alcohol dehydrogenase (NAD) activity; metal ion binding; nucleotide binding; oxidoreductase activity; zinc ion binding;

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)

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What are the structural features of ADH1C, and how do they relate to its enzymatic activity and substrate binding? 06/23/2022

The structural features of ADH1C, such as its active site and binding domains, are critical for its enzymatic activity and substrate recognition, enabling efficient alcohol oxidation.

How does the expression or activity of ADH1C change in response to pharmacological agents or environmental factors, and what are the implications for alcohol metabolism or therapy? 02/18/2021

Pharmacological agents or environmental factors can modulate ADH1C expression or activity, potentially influencing alcohol metabolism and providing avenues for therapeutic interventions or personalized medicine.

Can ADH1C metabolize other substrates apart from alcohol, and what are the implications for its broader metabolic role? 05/31/2020

ADH1C has the capacity to metabolize other substrates beyond alcohol, suggesting its involvement in broader metabolic pathways and potential metabolic interactions.

Are there any known genetic variations or polymorphisms in the ADH1C gene associated with differences in alcohol metabolism or susceptibility to alcohol-related disorders? 04/23/2020

Genetic variations or polymorphisms in the ADH1C gene have been associated with differences in alcohol metabolism and susceptibility to alcohol-related disorders, highlighting the impact of genotype on phenotype.

How does ADH1C expression or activity vary in different species or populations, and what are the underlying genetic and environmental factors influencing these variations? 04/07/2020

ADH1C 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.

What is the tissue-specific expression pattern of ADH1C, and how does it differ from other ADH isoforms in terms of its expression levels and distribution across organs and cell types? 10/13/2019

ADH1C 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.

How does ADH1C contribute to alcohol metabolism, and what is its catalytic efficiency and substrate specificity compared to other ADH isoforms? 07/13/2018

ADH1C plays a significant role in alcohol metabolism, showing specific catalytic efficiency and substrate specificity for the conversion of alcohol to acetaldehyde.

What are the regulatory mechanisms controlling ADH1C expression, and how do they respond to alcohol exposure or other metabolic factors? 12/29/2017

The expression of ADH1C is regulated by specific mechanisms, including transcriptional and post-transcriptional regulation, which can respond to alcohol exposure or metabolic factors such as hormonal signaling.

Are there any interacting proteins or partners of ADH1C that influence its function or localization? 12/17/2017

There may be interacting proteins or partners of ADH1C that influence its function or localization, potentially modulating its enzymatic activity or cellular processes.

What are the consequences of ADH1C deficiency or knockout in experimental models, and how does it affect alcohol metabolism and related phenotypes? 12/12/2017

ADH1C 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.

Customer Reviews (2)

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Reviews
04/03/2020

    Highly specific in recognizing and cleaving target substrates in protease assays.

    12/20/2018

      Provides efficient and accurate quantification of post-translational modifications in PTM studies.

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