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SRP6083

Sigma-Aldrich

ALDH2 human

recombinant, expressed in E. coli, ≥90% (SDS-PAGE)

Synonyme(s) :

ALDH class 2, ALDH-E2, ALDHI, ALDM, Aldehyde dehydrogenase, mitochondrial

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About This Item

Code UNSPSC :
12352200
Nomenclature NACRES :
NA.32

Source biologique

human

Produit recombinant

expressed in E. coli

Pureté

≥90% (SDS-PAGE)

Forme

liquid

Poids mol.

54.5 kDa

Conditionnement

pkg of 100 μg

Numéro d'accès NCBI

Conditions d'expédition

dry ice

Température de stockage

−70°C

Informations sur le gène

human ... ALDH2(217)

Description générale

ALDH2 (Aldehyde dehydrogenase 2 family) belongs to the aldehyde dehydrogenase family which catalyze the chemical transformation from acetaldehyde to acetic acid and is the second enzyme of the major oxidative pathway of alcohol metabolism. There are two major liver isoforms of this enzyme, cytosolic and mitochondrial, and they can be also distinguished by their electrophoretic mobilities, kinetic properties, and subcellular localizations. ALDH2 has been shown to interact with GroEL.
ALDH2 (Aldehyde dehydrogenase 2 family) belongs to the aldehyde dehydrogenase family. There are two major liver isoforms of liver aldehyde dehydrogenase, cytosolic (ALDH1) and mitochondrial (ALDH2), and they can be distinguished by their electrophoretic mobilities, kinetic properties, and subcellular localizations.
The ALDH2 gene is mapped to human chromosome 12q24.12.

Actions biochimiques/physiologiques

Aldehyde dehydrogenases catalyze the chemical transformation from acetaldehyde to acetic acid and ALDH2 (Aldehyde dehydrogenase 2 family) is the major enzyme of the oxidative pathway of alcohol metabolism. Overexpression of ALDH2 inhibits cell injury induced by acetaldehyde and prevents activation of stress signals.
It is actively involved in the metabolism of both endogenous and exogenous substances.

Forme physique

1 mg/mL solution in 20 mM Tris-HCl buffer (pH 7.5) containing 1 mM DTT, 1 mM EDTA and 10% glycerol.

Notes préparatoires

Centrifuge the vial prior to opening.

Autres remarques

MSAAATQAVP APNQQPEVFC NQIFINNEWH DAVSRKTFPT VNPSTGEVIC QVAEGDKEDV DKAVKAARAA FQLGSPWRRM DASHRGRLLN RLADLIERDR TYLAALETLD NGKPYVISYL VDLDMVLKCL RYYAGWADKY HGKTIPIDGD FFSYTRHEPV GVCGQIIPWN FPLLMQAWKL GPALATGNVV VMKVAEQTPL TALYVANLIK EAGFPPGVVN IVPGFGPTAG AAIASHEDVD KVAFTGSTEI GRVIQVAAGS SNLKRVTLEL GGKSPNIIMS DADMDWAVEQ AHFALFFNQG QCCCAGSRTF VQEDIYDEFV ERSVARAKSR VVGNPFDSKT EQGPQVDETQ FKKILGYINT GKQEGAKLLC GGGIAADRGY FIQPTVFGDV QDGMTIAKEE IFGPVMQILK FKTIEEVVGR ANNSTYGLAA AVFTKDLDKA NYLSQALQAG TVWVNCYDVF GAQSPFGGYK MSGSGRELGE YGLQAYTEVK TVTVKVPQKN S

Pictogrammes

Exclamation mark

Mention d'avertissement

Warning

Mentions de danger

Classification des risques

Eye Irrit. 2

Code de la classe de stockage

11 - Combustible Solids

Classe de danger pour l'eau (WGK)

WGK 3

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable


Certificats d'analyse (COA)

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Consulter la Bibliothèque de documents

Significant association between decreased ALDH2 activity and increased sensitivity to genotoxic effects in workers occupationally exposed to styrene.
Weng Z, et al.
Oncotarget, 7(25), 38224-38224 (2016)
Aishwarya Nene et al.
Journal of biomedical science, 24(1), 3-3 (2017-01-07)
Mitochondrial aldehyde dehydrogenase 2 (ALDH2) is a key enzyme for the metabolism of many toxic aldehydes such as acetaldehyde, derived from alcohol drinking, and 4HNE, an oxidative stress-derived lipid peroxidation aldehyde. Post-translational enhancement of ALDH2 activity can be achieved by
Overexpression of aldehyde dehydrogenase-2 (ALDH2) transgene prevents acetaldehyde-induced cell injury in human umbilical vein endothelial cells: role of ERK and p38 mitogen-activated protein kinase.
Li SY
The Journal of Biological Chemistry, 279, 11244-11252 (2004)
Direct detection of usual and atypical alleles on the human aldehyde dehydrogenase-2 (ALDH2) locus
Hsu LC
American Journal of Human Genetics, 41, 996-1001 (1987)
Cloning of cDNAs for human aldehyde dehydrogenases 1 and 2.
Hsu LC
Proceedings of the National Academy of Sciences of the USA, 82, 3771-3775 (1985)

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