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Recombinant Human ADH4, His-tagged

Cat.No. : ADH4-3252H
Product Overview : Alcohol dehydrogenase 4 (ADH4)
  • Specification
  • Gene Information
  • Related Products
Description : This gene encodes class II alcohol dehydrogenase 4 pi 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 II alcohol dehydrogenase is a homodimer composed of 2 pi subunits. It exhibits a high activity for oxidation of long-chain aliphatic alcohols and aromatic alcohols and is less sensitive to pyrazole. This gene is localized to chromosome 4 in the cluster of alcohol dehydrogenase genes.
Source : E. Coli or Yeast
Species : Human
Tag : His
Form : This item requires custom production and lead time is between 5-9 weeks. We can custom produce according to your specifications.
Protein length : 380
Purity : >90%
Notes : Small volumes of ADH4 recombinant protein may occasionally become entrapped in the seal of the product vial during shipment and storage. If necessary, briefly centrifuge the vial on a tabletop centrifuge to dislodge any liquid in the container`s cap. Certain products may require to ship with dry ice.
Storage : Store at -20 degree C. For extended storage, store at -20 or -80 degree C.
Storage Buffer : PBS pH 7.4, 50% glycerol
Warning : This product is for research use only. Not for use in diagnostic or therapeutic procedures.
Gene Name : ADH4 alcohol dehydrogenase 4 (class II), pi polypeptide [ Homo sapiens ]
Official Symbol : ADH4
Synonyms : ADH4; alcohol dehydrogenase 4 (class II), pi polypeptide; alcohol dehydrogenase 4; ADH 2; aldehyde reductase; alcohol dehydrogenase class II pi chain; ADH-2;
Gene ID : 127
mRNA Refseq : NM_000670
Protein Refseq : NP_000661
MIM : 103740
UniProt ID : P08319
Chromosome Location : 4q22
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, organis
Function : NAD binding; NADPH:quinone reductase activity; alcohol dehydrogenase (NAD) activity; alcohol dehydrogenase activity, zinc-dependent; alditol:NADP+ 1-oxidoreductase activity; all-trans retinal binding; benzaldehyde dehydrogenase activity; metal ion binding; oxidoreductase activity; oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor; retinol binding; retinol dehydrogenase 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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Can ADH4 play a role in the metabolism of other endogenous compounds or xenobiotics, and if so, what are the implications for its broader physiological functions? 07/15/2021

ADH4 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 ADH4 gene associated with altered alcohol metabolism or susceptibility to alcohol-related disorders? 05/30/2021

Genetic variations or polymorphisms in the ADH4 gene may impact alcohol metabolism and susceptibility to alcohol-related disorders, emphasizing the role of genetic factors in its function.

What is the tissue-specific expression pattern of ADH4, and how is its expression regulated under normal physiological conditions and in response to specific stimuli? 04/10/2020

ADH4 exhibits a tissue-specific expression pattern, and its expression is regulated by various factors such as transcriptional control and signaling pathways.

What are the enzymatic kinetics and catalytic properties of ADH4, and how do they contribute to its overall activity? 02/06/2020

The enzymatic kinetics and catalytic properties of ADH4 contribute to its overall activity and efficiency in alcohol metabolism.

What is the impact of ADH4 deficiency or overexpression on alcohol metabolism and its physiological consequences? 05/15/2019

Exploring the consequences of ADH4 deficiency or overexpression provides insights into its role in alcohol metabolism and its impact on physiological processes.

Can ADH4 efficiently metabolize different alcohol substrates, and how does its substrate specificity compare to other ADH enzymes? 01/09/2019

ADH4 can efficiently metabolize different alcohol substrates, and its substrate specificity may differ from other ADH enzymes.

How does ADH4 expression and activity change in response to chronic alcohol exposure or alcohol withdrawal, and what are the molecular mechanisms underlying these changes? 07/07/2018

ADH4 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.

Are there any specific interacting proteins or cofactors that influence the activity or function of ADH4, and what are the underlying molecular mechanisms? 06/17/2018

Interacting proteins or cofactors can modulate the activity or function of ADH4, and investigating the molecular mechanisms involved can enhance our understanding of its regulation.

Can the activity or function of ADH4 be modulated by pharmacological agents or environmental factors, and are there potential therapeutic implications? 03/22/2018

The activity or function of ADH4 can potentially be modulated by pharmacological agents or environmental factors, presenting potential therapeutic implications.

What are the structural features of ADH4, and how do they contribute to its catalytic activity and binding affinity for alcohol? 07/09/2017

The structural features of ADH4 play a crucial role in its catalytic activity and binding affinity for alcohol, and understanding these features provides insights into its function.

Customer Reviews (2)

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Reviews
11/04/2018

    Shows exceptional specificity in binding to DNA or RNA in nucleic acid binding assays.

    05/14/2017

      Provides accurate and reliable quantification of protein isoforms in proteoforms analysis.

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