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AB123147

Recombinant Human Alcohol Dehydrogenase protein (His tag N-Terminus)

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(1 Publication)

Recombinant Human Alcohol Dehydrogenase protein (His tag N-Terminus) is a Human Full Length protein, in the 1 to 375 aa range, expressed in Escherichia coli, with >90%, suitable for SDS-PAGE, Mass Spec.

View Alternative Names

ADH1, ADH1A, Alcohol dehydrogenase 1A, Alcohol dehydrogenase subunit alpha

1 Images
SDS-PAGE - Recombinant Human Alcohol Dehydrogenase protein (His tag N-Terminus) (AB123147)
  • SDS-PAGE

Unknown

SDS-PAGE - Recombinant Human Alcohol Dehydrogenase protein (His tag N-Terminus) (AB123147)

15% SDS PAGE, 3 µg of ab123147 loaded.

Key facts

Purity

>90% SDS-PAGE

Expression system

Escherichia coli

Tags

His tag N-Terminus

Applications

SDS-PAGE, Mass Spec

applications

Biologically active

No

Accession

P07327

Animal free

No

Carrier free

No

Species

Human

Storage buffer

pH: 8 Constituents: 10% Glycerol (glycerin, glycerine), 0.58% Sodium chloride, 0.32% Tris HCl, 0.02% (R*,R*)-1,4-Dimercaptobutan-2,3-diol

storage-buffer

Reactivity data

{ "title": "Reactivity Data", "filters": { "stats": ["", "Reactivity", "Dilution Info", "Notes"] }, "values": { "SDS-PAGE": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" }, "Mass Spec": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" } } }

Sequence info

[{"sequence":"MGSSHHHHHHSSGLVPRGSHMSTAGKVIKCKAAVLWELKKPFSIEEVEVAPPKAHEVRIKMVAVGICGTDDHVVSGTMVTPLPVILGHEAAGIVESVGEGVTTVKPGDKVIPLAIPQCGKCRICKNPESNYCLKNDVSNPQGTLQDGTSRFTCRRKPIHHFLGISTFSQYTVVDENAVAKIDAASPLEKVCLIGCGFSTGYGSAVNVAKVTPGSTCAVFGLGGVGLSAIMGCKAAGAARIIAVDINKDKFAKAKELGATECINPQDYKKPIQEVLKEMTDGGVDFSFEVIGRLDTMMASLLCCHEACGTSVIVGVPPDSQNLSMNPMLLLTGRTWKGAILGGFKSKECVPKLVADFMAKKFSLDALITHVLPFEKINEGFDLLHSGKSIRTILMF","proteinLength":"Full Length","predictedMolecularWeight":"42 kDa","actualMolecularWeight":null,"aminoAcidEnd":375,"aminoAcidStart":1,"nature":"Recombinant","expressionSystem":"Escherichia coli","accessionNumber":"P07327","tags":[{"tag":"His","terminus":"N-Terminus"}]}]

Properties and storage information

Shipped at conditions
Blue Ice
Appropriate short-term storage duration
1-2 weeks
Appropriate short-term storage conditions
+4°C
Appropriate long-term storage conditions
-20°C
Aliquoting information
Upon delivery aliquot
Storage information
Avoid freeze / thaw cycle
False

Supplementary information

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

Alcohol dehydrogenase (ADH) also known as aldehyde reductase is an enzyme that catalyzes the conversion of alcohols to aldehydes while reducing NAD+ to NADH. This enzyme's structure comprises approximately 40 kDa per subunit and it typically functions as a dimer. ADH is predominantly expressed in the liver where it plays a major role in alcohol metabolism. However its presence is also noted in other tissues such as the stomach lining and kidneys. The enzyme's activities are significant enough to be measured through various assays including ADH assay and alcohol dehydrogenase test highlighting its enzymatic kinetics.
Biological function summary

Alcohol dehydrogenase's role extends beyond simple alcohol metabolism. It participates in the body's detoxification processes. This enzyme is not part of a larger complex but can function alongside other dehydrogenases involved in metabolic processes. ADH's activity helps in managing blood alcohol levels by converting ethanol to acetaldehyde which is further processed by aldehyde dehydrogenase to acetate. The balance and efficiency of these reactions determine the rate and capacity of alcohol clearance from the body.

Pathways

Alcohol dehydrogenase significantly contributes to the alcohol metabolism pathway and the retinol metabolism pathway. It plays a role in converting retinol to retinal which is important for vision and cell growth. In these pathways ADH works closely with aldehyde dehydrogenase to ensure the continuation of the metabolic processes in the human body. The enzyme's function is also connected to the smooth operation of the cytochrome P450 system in the liver for comprehensive detoxification.

The activity of alcohol dehydrogenase links closely to conditions like alcoholism and liver disease. Variations in ADH enzyme activity can affect an individual's susceptibility to alcohol use disorder due to differences in alcohol metabolism rates. Additionally high acetaldehyde levels a product of the alcohol dehydrogenase reaction can contribute to liver damage leading to cirrhosis. This enzyme's relationship to aldehyde dehydrogenase is critical as the failure in converting acetaldehyde can exacerbate the toxic effects and contribute further to these disorders.

Specifications

Form

Liquid

Additional notes

ab123147 was purified using conventional chromatography.

General info

Function

Alcohol dehydrogenase (PubMed : 2738060). Oxidizes primary as well as secondary alcohols. Ethanol is a very poor substrate (PubMed : 2738060).

Sequence similarities

Belongs to the zinc-containing alcohol dehydrogenase family.

Product protocols

Target data

Alcohol dehydrogenase (PubMed : 2738060). Oxidizes primary as well as secondary alcohols. Ethanol is a very poor substrate (PubMed : 2738060).
See full target information ADH1A

Publications (1)

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

Biochemical pharmacology 167:27-32 PubMed30936015

2019

Human alcohol dehydrogenase 1 is an acceptor protein for polyADP-ribosylation.

Applications

Unspecified application

Species

Unspecified reactive species

Sachiko Yamashita,Masakazu Tanaka,Hiroto Nodono,Akiko Hamada,Takashi Hamada,Makoto Hasegawa,Yoshisuke Nishi,Joel Moss,Masanao Miwa
View all publications

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