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AB116934

Recombinant Human ADH1B protein

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(1 Publication)

Recombinant Human ADH1B protein is a Human Full Length protein, in the 1 to 375 aa range, expressed in Wheat germ, suitable for SDS-PAGE, ELISA, WB.

View Alternative Names

ADH2, ADH1B, All-trans-retinol dehydrogenase [NAD(+)] ADH1B, Alcohol dehydrogenase 1B, Alcohol dehydrogenase subunit beta

1 Images
SDS-PAGE - Recombinant Human ADH1B protein (AB116934)
  • SDS-PAGE

Unknown

SDS-PAGE - Recombinant Human ADH1B protein (AB116934)

12.5% SDS-PAGE stained with Coomassie Blue showing ab116934 at approximately 66.99 kDa.

Key facts

Expression system

Wheat germ

Tags

Tag free

Applications

ELISA, SDS-PAGE, WB

applications

Biologically active

No

Accession

P00325

Animal free

No

Carrier free

No

Species

Human

Storage buffer

pH: 8 Constituents: 0.79% Tris HCl, 0.3% Glutathione

storage-buffer

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Reactivity data

{ "title": "Reactivity Data", "filters": { "stats": ["", "Reactivity", "Dilution Info", "Notes"] }, "values": { "SDS-PAGE": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" }, "ELISA": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" }, "WB": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p>(Recombinant protein).</p>" } } }
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Sequence info

[{"sequence":"MSTAGKVIKCKAAVLWEVKKPFSIEDVEVAPPKAYEVRIKMVAVGICRTDDHVVSGNLVTPLPVILGHEAAGIVESVGEGVTTVKPGDKVIPLFTPQCGKCRVCKNPESNYCLKNDLGNPRGTLQDGTRRFTCRGKPIHHFLGTSTFSQYTVVDENAVAKIDAASPLEKVCLIGCGFSTGYGSAVNVAKVTPGSTCAVFGLGGVGLSAVMGCKAAGAARIIAVDINKDKFAKAKELGATECINPQDYKKPIQEVLKEMTDGGVDFSFEVIGRLDTMMASLLCCHEACGTSVIVGVPPASQNLSINPMLLLTGRTWKGAVYGGFKSKEGIPKLVADFMAKKFSLDALITHVLPFEKINEGFDLLHSGKSIRTVLTF","proteinLength":"Full Length","predictedMolecularWeight":"66.99 kDa","actualMolecularWeight":null,"aminoAcidEnd":375,"aminoAcidStart":1,"nature":"Recombinant","expressionSystem":"Wheat germ","accessionNumber":"P00325","tags":[]}]
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Properties and storage information

Shipped at conditions
Dry Ice
Appropriate short-term storage conditions
-80°C
Appropriate long-term storage conditions
-80°C
Aliquoting information
Upon delivery aliquot
Storage information
Avoid freeze / thaw cycle
False
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Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

The ADH1B protein also known as alcohol dehydrogenase 1B catalyzes the oxidation of alcohols to aldehydes. It plays a role in metabolic processes by enabling the conversion of ethanol to acetaldehyde. The mass of ADH1B is approximately 40 kDa. This enzyme is predominantly expressed in the liver where alcohol metabolism is an ongoing and critical function. ADH1B functions as a homodimer which means two identical subunits form the complete active enzyme.
Biological function summary

ADH1B contributes to ethanol metabolism which is important for the detoxification of alcohol in human body. The enzyme performs efficiently in metabolizing small alcohols. ADH1B does not work alone; it forms part of a larger enzyme complex. This complex also involves other alcohol dehydrogenases like ADH1A that operate in similar metabolic pathways. Together these enzymes maintain balance in alcohol and aldehyde levels in tissues.

Pathways

ADH1B is an important component of the alcohol metabolism and aldehyde metabolism pathways. It works closely with other proteins like aldehyde dehydrogenase (ALDH2) which process the acetaldehyde generated by ADH1B oxidation into acetic acid. This sequence of reactions not only aids in detoxification but also provides useful metabolic intermediates for further energy production. ADH1B interconnects with related enzymes supporting efficient regulation of metabolic flux.

The activity of ADH1B holds significance in conditions such as alcohol dependency and certain types of cancer. Genetic variations in the ADH1B gene can affect enzyme activity influencing alcohol processing speed and potential risk for addiction. Likewise altered ADH1B activity and expression levels have been linked to certain cancers particularly esophageal cancer. The relation between ADH1B and ALDH2 may also contribute to this disease risk highlighting important consequences of alcohol metabolism enzymes in human health.
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Specifications

Form

Liquid

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General info

Function

Catalyzes the NAD-dependent oxidation of all-trans-retinol and its derivatives such as all-trans-4-hydroxyretinol and may participate in retinoid metabolism (PubMed : 15369820, PubMed : 16787387). In vitro can also catalyze the NADH-dependent reduction of all-trans-retinal and its derivatives such as all-trans-4-oxoretinal (PubMed : 15369820, PubMed : 16787387). Catalyzes in the oxidative direction with higher efficiency (PubMed : 16787387). Has the same affinity for all-trans-4-hydroxyretinol and all-trans-4-oxoretinal (PubMed : 15369820).

Sequence similarities

Belongs to the zinc-containing alcohol dehydrogenase family.

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Product protocols

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Target data

Catalyzes the NAD-dependent oxidation of all-trans-retinol and its derivatives such as all-trans-4-hydroxyretinol and may participate in retinoid metabolism (PubMed : 15369820, PubMed : 16787387). In vitro can also catalyze the NADH-dependent reduction of all-trans-retinal and its derivatives such as all-trans-4-oxoretinal (PubMed : 15369820, PubMed : 16787387). Catalyzes in the oxidative direction with higher efficiency (PubMed : 16787387). Has the same affinity for all-trans-4-hydroxyretinol and all-trans-4-oxoretinal (PubMed : 15369820).
See full target information ADH1B
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Publications (1)

Recent publications for all applications. Explore the full list and refine your search

International journal of molecular sciences 22: PubMed34681731

2021

Mass Spectrometry-Based Proteomics Reveal Alcohol Dehydrogenase 1B as a Blood Biomarker Candidate to Monitor Acetaminophen-Induced Liver Injury.

Applications

Unspecified application

Species

Unspecified reactive species

Floriane Pailleux,Pauline Maes,Michel Jaquinod,Justine Barthelon,Marion Darnaud,Claire Lacoste,Yves Vandenbrouck,Benoît Gilquin,Mathilde Louwagie,Anne-Marie Hesse,Alexandra Kraut,Jérôme Garin,Vincent Leroy,Jean-Pierre Zarski,Christophe Bruley,Yohann Couté,Didier Samuel,Philippe Ichai,Jamila Faivre,Virginie Brun
View all publications
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