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Recombinant Human ADH5 cell lysate

Cat.No. : ADH5-30HCL
  • Specification
  • Gene Information
  • Related Products
Description : This gene encodes a member of the alcohol dehydrogenase family. Members of this family metabolize a wide variety of substrates, including ethanol, retinol, other aliphatic alcohols, hydroxysteroids, and lipid peroxidation products. The encoded protein forms a homodimer. It has virtually no activity for ethanol oxidation, but exhibits high activity for oxidation of long-chain primary alcohols and for oxidation of S-hydroxymethyl-glutathione, a spontaneous adduct between formaldehyde and glutathione. This enzyme is an important component of cellular metabolism for the elimination of formaldehyde, a potent irritant and sensitizing agent that causes lacrymation, rhinitis, pharyngitis, and contact dermatitis. The human genome contains several non-transcribed pseudogenes related to this gene.
Species : Human
Size : 100 ul
Storage Buffer : 1X Sample Buffer (50 mM Tris-HCl, 2% SDS, 10% glycerol, 300 mM 2-mercaptoethanol, 0.01% Bromophenol blue)
Applications : Western Blot;
Gene Name : ADH5 alcohol dehydrogenase 5 (class III), chi polypeptide [ Homo sapiens ]
Official Symbol : ADH5
Synonyms : ADH5; alcohol dehydrogenase 5 (class III), chi polypeptide; FDH, formaldehyde dehydrogenase; alcohol dehydrogenase class-3; ADH 3; ADHX; formaldehyde dehydrogenase; alcohol dehydrogenase class-III; alcohol dehydrogenase class chi chain; S-(hydroxymethyl)glutathione dehydrogenase; glutathione-dependent formaldehyde dehydrogenase; alcohol dehydrogenase (class III), chi polypeptide; FDH; ADH-3; FALDH; GSNOR; GSH-FDH;
Gene ID : 128
mRNA Refseq : NM_000671
Protein Refseq : NP_000662
MIM : 103710
UniProt ID : P11766
Chromosome Location : 4q23
Pathway : Drug metabolism - cytochrome P450, organism-specific biosystem; Drug metabolism - cytochrome P450, conserved biosystem; Fatty acid metabolism, organism-specific biosystem; Fatty acid metabolism, conserved biosystem; Glycolysis / Gluconeogenesis, organism-specific biosystem; Glycolysis / Gluconeogenesis, conserved biosystem; Metabolic pathways, organism-specific biosystem;
Function : S-(hydroxymethyl)glutathione dehydrogenase activity; alcohol dehydrogenase (NAD) activity; electron carrier activity; fatty acid binding; formaldehyde dehydrogenase activity; metal ion binding; nucleotide binding; oxidoreductase activity; protein homodimerization 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 is the tissue-specific expression pattern of ADH5, and how is its expression regulated under normal physiological conditions and in response to specific stimuli? 03/07/2022

ADH5 exhibits a tissue-specific expression pattern, and its expression is regulated by various factors such as transcriptional control and signaling pathways.

Can ADH5 efficiently metabolize different alcohol substrates, and how does its substrate specificity compare to other ADH enzymes? 09/21/2021

ADH5 can efficiently metabolize different alcohol substrates, and its substrate specificity may differ from other ADH enzymes.

How does ADH5 expression and activity change in response to chronic alcohol exposure or alcohol withdrawal, and what are the molecular mechanisms underlying these changes? 09/03/2021

ADH5 expression and activity can be influenced by chronic alcohol exposure or withdrawal, and studying the underlying molecular mechanisms can shed light on alcohol-related effects.

Can the activity or function of ADH5 be modulated by pharmacological agents or environmental factors, and are there potential therapeutic implications? 08/17/2020

The activity or function of ADH5 can potentially be modulated by pharmacological agents or environmental factors, presenting potential therapeutic implications.

Are there any specific interacting proteins or cofactors that influence the activity or function of ADH5, and what are the underlying molecular mechanisms? 07/30/2020

Interacting proteins or cofactors can modulate the activity or function of ADH5, and investigating the molecular mechanisms involved can enhance our understanding of its regulation.

What are the enzymatic kinetics and catalytic properties of ADH5, and how do they contribute to its overall activity? 11/23/2019

The enzymatic kinetics and catalytic properties of ADH5 contribute to its overall activity and efficiency in alcohol metabolism.

Can ADH5 play a role in the metabolism of other endogenous compounds or xenobiotics, and if so, what are the implications for its broader physiological functions? 05/10/2019

ADH5 may have implications in the metabolism of other endogenous compounds or xenobiotics, suggesting its involvement in broader physiological functions.

Are there any known genetic variations or polymorphisms in the ADH5 gene associated with altered alcohol metabolism or susceptibility to alcohol-related disorders? 06/13/2018

Genetic variations or polymorphisms in the ADH5 gene may impact alcohol metabolism and susceptibility to alcohol-related disorders, emphasizing the role of genetic factors in its function.

What are the structural features of ADH5, and how do they contribute to its catalytic activity and binding affinity for alcohol? 02/08/2017

The structural features of ADH5 play a crucial role in its catalytic activity and binding affinity for alcohol, and understanding these features provides insights into its function.

What is the impact of ADH5 deficiency or overexpression on alcohol metabolism and its physiological consequences? 06/05/2016

Exploring the consequences of ADH5 deficiency or overexpression provides insights into its role in alcohol metabolism and its impact on physiological processes.

Customer Reviews (2)

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Reviews
07/29/2022

    Highly effective in stabilizing and enhancing the activity of enzymes in enzyme engineering.

    05/29/2016

      Demonstrates excellent resistance to aggregation and aggregation-prone conditions.

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