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AB124573

Recombinant Human ADH5 protein (His tag N-Terminus)

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(1 Publication)

Recombinant Human ADH5 protein (His tag N-Terminus) is a Human Full Length protein, in the 1 to 374 aa range, expressed in Escherichia coli, with >90%, suitable for SDS-PAGE, Mass Spec.

View Alternative Names

ADHX, FDH, ADH5, Alcohol dehydrogenase class-3, Alcohol dehydrogenase 5, Alcohol dehydrogenase class chi chain, Alcohol dehydrogenase class-III, Glutathione-dependent formaldehyde dehydrogenase, S-(hydroxymethyl)glutathione dehydrogenase, FALDH, GSH-FDH

1 Images
SDS-PAGE - Recombinant Human ADH5 protein (His tag N-Terminus) (AB124573)
  • SDS-PAGE

Unknown

SDS-PAGE - Recombinant Human ADH5 protein (His tag N-Terminus) (AB124573)

15% SDS-PAGE showing ab124573 at approximately 42.3kDa (3μg).

Key facts

Purity

>90% SDS-PAGE

Expression system

Escherichia coli

Tags

His tag N-Terminus

Applications

Mass Spec, SDS-PAGE

applications

Biologically active

No

Accession

P11766

Animal free

No

Carrier free

No

Species

Human

Storage buffer

pH: 7.5 Constituents: 20% Glycerol (glycerin, glycerine), 0.58% Sodium chloride, 0.32% Tris HCl, 0.02% (R*,R*)-1,4-Dimercaptobutan-2,3-diol

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>" }, "Mass Spec": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" } } }
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Sequence info

[{"sequence":"MGSSHHHHHHSSGLVPRGSHMGSHMANEVIKCKAAVAWEAGKPLSIEEIEVAPPKAHEVRIKIIATAVCHTDAYTLSGADPEGCFPVILGHEGAGIVESVGEGVTKLKAGDTVIPLYIPQCGECKFCLNPKTNLCQKIRVTQGKGLMPDGTSRFTCKGKTILHYMGTSTFSEYTVVADISVAKIDPLAPLDKVCLLGCGISTGYGAAVNTAKLEPGSVCAVFGLGGVGLAVIMGCKVAGASRIIGVDINKDKFARAKEFGATECINPQDFSKPIQEVLIEMTDGGVDYSFECIGNVKVMRAALEACHKGWGVSVVVGVAASGEEIATRPFQLVTGRTWKGTAFGGWKSVESVPKLVSEYMSKKIKVDEFVTHNLSFDEINKAFELMHSGKSIRTVVKI","proteinLength":"Full Length","predictedMolecularWeight":"42.3 kDa","actualMolecularWeight":null,"aminoAcidEnd":374,"aminoAcidStart":1,"nature":"Recombinant","expressionSystem":"Escherichia coli","accessionNumber":"P11766","tags":[{"tag":"His","terminus":"N-Terminus"}]}]
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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
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Supplementary information

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

ADH5 also known as alcohol dehydrogenase class-3 or glutathione-dependent formaldehyde dehydrogenase is an enzyme with a mass of approximately 42 kDa. It plays a role in alcohol metabolism specifically in the detoxification of formaldehyde. The protein is expressed in many tissues including the liver kidney and lung. ADH5 belongs to the alcohol dehydrogenase protein family and distinguishes itself by its ability to metabolize both aliphatic and aromatic compounds.
Biological function summary

Alcohol metabolism involves more than one enzyme and ADH5 functions within a network of metabolic reactions. This enzyme contributes to formaldehyde detoxification where it oxidizes formaldehyde to formic acid. The ADH5 enzyme operates in the cytosol and takes part in the catabolism of harmful aldehydes. Its action supports cellular protection reducing toxicity from chemical exposure and ensuring normal cellular metabolism.

Pathways

ADH5 plays significant roles in methanol and formaldehyde metabolic pathways. It acts alongside enzymes like alcohol dehydrogenase 1 (ADH1) and aldehyde dehydrogenase (ALDH) in processing formaldehyde into less toxic substances. In the methanol metabolism pathway interactions with ADH1 highlight its role in ethanol to acetaldehyde conversion. The pathway interactions emphasize its importance in reducing oxidative stress and preventing damage from reactive aldehydes.

ADH5's function aligns with conditions related to alcohol metabolism like formaldehyde sensitivity and methanol poisoning. Abnormal ADH5 activity can contribute to such conditions implicating oxidative stress responses. Associations also exist with other diseases related to aldehyde toxicity such as alcohol-related liver damage. Alongside ADH1 and ALDH ADH5 aids in maintaining homeostasis in cellular environments and disruptions can lead to pathological conditions.
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Specifications

Form

Liquid

Additional notes

ab124573 was purified using conventional chromatography techniques.

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General info

Function

Catalyzes the oxidation of long-chain primary alcohols and the oxidation of S-(hydroxymethyl) glutathione (PubMed : 8460164). Also oxidizes long chain omega-hydroxy fatty acids, such as 20-HETE, producing both the intermediate aldehyde, 20-oxoarachidonate and the end product, a dicarboxylic acid, (5Z,8Z,11Z,14Z)-eicosatetraenedioate (PubMed : 16081420). Class-III ADH is remarkably ineffective in oxidizing ethanol (PubMed : 8460164). Required for clearance of cellular formaldehyde, a cytotoxic and carcinogenic metabolite that induces DNA damage (PubMed : 33355142). Also acts as a S-nitroso-glutathione reductase by catalyzing the NADH-dependent reduction of S-nitrosoglutathione, thereby regulating protein S-nitrosylation (By similarity).

Sequence similarities

Belongs to the zinc-containing alcohol dehydrogenase family. Class-III subfamily.

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Product protocols

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Target data

Catalyzes the oxidation of long-chain primary alcohols and the oxidation of S-(hydroxymethyl) glutathione (PubMed : 8460164). Also oxidizes long chain omega-hydroxy fatty acids, such as 20-HETE, producing both the intermediate aldehyde, 20-oxoarachidonate and the end product, a dicarboxylic acid, (5Z,8Z,11Z,14Z)-eicosatetraenedioate (PubMed : 16081420). Class-III ADH is remarkably ineffective in oxidizing ethanol (PubMed : 8460164). Required for clearance of cellular formaldehyde, a cytotoxic and carcinogenic metabolite that induces DNA damage (PubMed : 33355142). Also acts as a S-nitroso-glutathione reductase by catalyzing the NADH-dependent reduction of S-nitrosoglutathione, thereby regulating protein S-nitrosylation (By similarity).
See full target information ADH5
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Publications (1)

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

Advanced science (Weinheim, Baden-Wurttemberg, Germany) 11:e2403894 PubMed38704696

2024

De-nitrosylation Coordinates Appressorium Function for Infection of the Rice Blast Fungus.

Applications

Unspecified application

Species

Unspecified reactive species

Hong Hu,Wenhui He,Zhiguang Qu,Xiang Dong,Zhiyong Ren,Mengyuan Qin,Hao Liu,Lu Zheng,Junbin Huang,Xiao-Lin Chen
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