Recombinant Human ALDH2
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Product specifications
| Category | Proteins and Peptides |
| Immunogen Target | 18-517 |
| Host | E.Coli |
| Origin | Human |
| Observed MW | 56.3 kDa |
| Expression | Recombinant |
| Purity | Greater than 80% by SDS-PAGE gel analyses |
| Purification | His tag |
| Size 1 | 50μg |
| Size 2 | 200μg |
| Size 3 | 1mg |
| Form | Lyophilized from a 0.2um filtered solution in PBS with 5% trehalose, pH7.4 |
| Tested Applications | Western Blot, ELISA |
| Buffer | Reconstitute with Sterile distilled water |
| Availability | 7 days |
| Storage | -20°C for 12 months as lyophilized;2-8°C for 1 month under sterile conditions after reconstitution |
| UniProt ID | P05091 |
| Alias | ALDH2,ALDM,ALDH class 2 |
| Background | Proteins ALDH2 |
| Status | RUO |
| Note | This product is for research use only. |
ALDH2 is a mitochondrial enzyme primarily responsible for the oxidation of acetaldehyde, a toxic intermediate produced during ethanol metabolism, into acetate. It plays a key role in alcohol detoxification, protecting cells from acetaldehyde-induced toxicity, which can lead to DNA damage, lipid peroxidation, and oxidative stress. ALDH2 also detoxifies reactive aldehydes generated during lipid peroxidation, such as 4-hydroxynonenal (4-HNE), and participates in mitochondrial redox balance. A common mutation in the ALDH2 gene, known as ALDH2*2, reduces enzymatic activity and is prevalent in East Asian populations, leading to alcohol intolerance, increased cancer risk (e.g., esophageal cancer), and cardiovascular diseases. ALDH2 is also protective against ischemic heart injury, as it reduces oxidative damage during cardiac stress. Its role in aldehyde detoxification and mitochondrial function highlights ALDH2 as a therapeutic target for alcohol-related diseases, cancer prevention, and cardiovascular disorders.
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This protein belongs to the aldehyde dehydrogenase family of proteins. Aldehyde dehydrogenase is the second enzyme of the major oxidative pathway of alcohol metabolism. Two major liver isoforms of aldehyde dehydrogenase, cytosolic and mitochondrial, can be distinguished by their electrophoretic mobilities, kinetic properties, and subcellular localizations. Most Caucasians have two major isozymes, while approximately 50% of East Asians have the cytosolic isozyme but not the mitochondrial isozyme. A remarkably higher frequency of acute alcohol intoxication among East Asians than among Caucasians could be related to the absence of a catalytically active form of the mitochondrial isozyme. The increased exposure to acetaldehyde in individuals with the catalytically inactive form may also confer greater susceptibility to many types of cancer. This gene encodes a mitochondrial isoform, which has a low Km for acetaldehydes, and is localized in mitochondrial matrix. Alternative splicing results in multiple transcript variants encoding distinct isoforms.
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