Human aldehyde dehydrogenase 2,ALDH2 ELISA kit
- Known as:
- Human aldehyde dehydrogenase 2,ALDH2 Enzyme-linked immunosorbent assay test reagent
- Catalog number:
- 201-12-0722
- Product Quantity:
- USD
- Category:
- -
- Supplier:
- Sunredbio SunBT Sun red bio
- Gene target:
- Human aldehyde dehydrogenase 2 ALDH2 ELISA kit
Related genes to: Human aldehyde dehydrogenase 2,ALDH2 ELISA kit
- Gene:
- ALDH1A2 NIH gene
- Name:
- aldehyde dehydrogenase 1 family member A2
- Previous symbol:
- -
- Synonyms:
- RALDH2
- Chromosome:
- 15q21.3
- Locus Type:
- gene with protein product
- Date approved:
- 2001-03-30
- Date modifiied:
- 2018-05-03
- Gene:
- ALDH2 NIH gene
- Name:
- aldehyde dehydrogenase 2 family member
- Previous symbol:
- -
- Synonyms:
- -
- Chromosome:
- 12q24.12
- Locus Type:
- gene with protein product
- Date approved:
- 1986-01-01
- Date modifiied:
- 2018-05-03
Related products to: Human aldehyde dehydrogenase 2,ALDH2 ELISA kit
Related articles to: Human aldehyde dehydrogenase 2,ALDH2 ELISA kit
- ALDH1A family enzymes (ALDH1A1, ALDH1A2, and ALDH1A3) catalyze retinoic acid synthesis, and their dysregulation is linked to disease. Selective inhibitors of these enzymes have been tested in drug discovery programs and one such compound, WIN18,446, was found to irreversibly inhibit ALDH1A2. WIN18,446 is a reversible male contraceptive in humans and animals. The inhibition of spermatogenesis by WIN18,446 is thought to be due to inhibition of ALDH1A. However, the mechanism of irreversible inhibition of ALDH1A2 by WIN18,446 is not known. A crystal structure obtained after incubating ALDH1A2 with WIN18,446 revealed a WIN18,446-derived metabolite covalently adducted to the catalytic cysteine, C320. Inspection of this structure suggested that the observed adduct is unstable and may be a metabolic intermediate stabilized under crystallographic conditions. In the current work, we tested this hypothesis. We identified and characterized an aldehyde metabolite of WIN18,446, which we designated M-54. M-54 is likely the metabolite of the intermediate observed in the crystal structure. Using a range of proteomics techniques, we identified a WIN18,446-derived ALDH1A2 protein adduct of mass 292.07 Da on C319 of ALDH1A2. This adduct may result from the reaction of the crystal structure metabolic intermediate. Using the identified mass, we probed human liver samples from multiple donors and found WIN18,446 specific adducts on cysteines within the ALDH1A1 and ALDH2 active site regions. The current study provides new insight into the metabolism of WIN18,446 and the mechanism of inhibition of ALDH1A2. We also demonstrate a proteomics workflow for identifying and validating drug-protein adducts of unknown mass. - Source: PubMed
Publication date: 2026/06/08
Zelter AlexZhong GuoMaes MichalHoopmann Michael RRiffle MichaelJaschob DanielCarlson Ii Eddie ANelson Wendel LDalvie DeepakMoritz Robert LDavis Trisha NMacCoss Michael JIsoherranen Nina - Selective chemical probes are essential for dissecting biological pathways and advancing drug discovery, yet developing high-quality probes for targets such as the aldehyde dehydrogenase (ALDH) family remains challenging. Here, we present a novel integrated approach combining experimental quantitative high-throughput screening (qHTS) with advanced machine learning (ML) and pharmacophore (PH4) modeling to rapidly identify selective inhibitors across multiple ALDH isoforms. We screened ∼13,000 annotated compounds against biochemical and cellular assays. We then utilized the data set to build ML and PH4 models to virtually screen a larger set of 174,000 compounds to enhance the chemical diversity of hits. This approach led to the expansion of chemically diverse isoform-selective inhibitors that are potent in both biochemical and cell-based assays. Validation through cellular target engagement assays further confirmed the selective activity of these compounds, leading to the discovery of ALDH1A2, ALDH1A3, ALDH2, and ALDH3A1 chemical probe candidates. Remarkably, this was achieved by employing just a single iteration of quantitative structure-activity relationship (QSAR) and PH4 modeling for virtual screening. This combined and strategy not only enhances the discovery of biologically relevant chemical probe candidates but also significantly expands the chemical diversity accessible for probe development, establishing a new platform for the rapid and resource-efficient identification of chemical probes against the ALDH enzyme family. The data set generated, including hundreds of compounds thoroughly characterized across a spectrum of assays, is publicly available and can serve as a high-quality training set for future research initiatives and probe development efforts. - Source: PubMed
Publication date: 2025/09/25
Yasgar AdamJain SankalpDavies MarissaDanchik CarinaNiehoff TaylorRan JingRai GaneshaYang Shyh-MingSimeonov AntonZakharov Alexey VMartinez Natalia J - Aldehyde dehydrogenase (ALDH) isoforms are widely used as biomarkers and potential drug targets in cancer research. Quantitation of ALDH enzymatic activity in biological samples often relies on the use of commercially available assays that are quite unspecific and do not discriminate between the various ALDH isoforms. The availability of highly purified recombinant ALDH isoforms allowed us to perform a full kinetic characterization of ALDH isoforms with fluorogenic substrates, BODIPY™-aminoacetaldehyde (BAAA), the ALDEFLUOR™ assay reagent, and two naphthaldedyde derivatives, 6-methoxy-2-naphthaldehyde (MONAL-62) and 7-methoxy-1-naphthaldehyde (MONAL-71). All ALDH1A isoforms were active to different extend with BAAA, while ALDH3A1 did not show any activity. Remarkable kinetic differences between ALDH1A1, ALDH1A2, ALDH1A3, ALDH2 and ALDH3A1 were observed with naphthaldehyde derivatives. Exquisite sensitivity was attained with MONAL-62 with a lower detection limit of 2 amol or 10 molecules of enzyme per microliter for ALDH1A1. The high substrate specificity of ALDH1A1 for MONAL-71 provides an alternative assay for the unambiguous identification of this isoform. Enzymatic properties of isoforms were accounted for by in silico simulations of substrate docking to the active site of ALDH structures. In addition to substrate specificity, inhibitor selectivity of each isoform, as assessed by incubation with DIMATE and ABD0171 inhibitors, provided additional information about isoform composition in low-activity samples isolated from cell extracts. The method was successfully applied to the detection of ALDH isoform activity in triple-negative breast cancer cells. - Source: PubMed
Publication date: 2025/06/18
Pequerul RaquelCovaleda DanielaSánchez-Vaca Andrés STorres LauraConstantinescu AndradaPerez-Alea MileidysParés XavierFarrés Jaume - Aldehyde dehydrogenases (ALDHs) constitute a group of enzymes that catalyze the oxidation of aldehydes to carboxylic acids. The human ALDH superfamily, including 19 different isoenzymes (ALDH1A1, ALDH1A2, ALDH1A3, AHDH1B1, ALDH1L1, ALDH1L2, ALDH2, ALDH3A1, ALDH3A2, ALDH3B1, ALDH3B2, ALDH4A1, ALDH5A1, ALDH6A1, ALDH7A1, ALDH8A1, ALDH9A1, ALDHA16A1, ALDH18A1), displays different key physiological and toxicological functions, with specific tissue expression and substrate specificity. Several studies have established that ALDH are interesting markers for the identification and quantification of human hematopoietic stem cells and cancer stem cells, notably leukemic stem cells. ALDH2 is the best-documented enzyme, in this family, as having an impact on hematology, particularly myeloid malignancies. ALDH2 mainly catalyzes the detoxification of toxic aldehydes (acetaldehyde, formaldehyde). For example, ALDH2 detoxifies formaldehyde, which is produced during the differentiation of hematopoietic progenitors. The trigger of alcohol dehydrogenase 5 (also known as formaldehyde dehydrogenase or S-nitrosoglutathione reductase, ADH5/FDH/GSNOR)/ALDH2 allows to eliminate formaldehyde and ensures normal hematopoiesis. Moreover, the ALDH2*2 variant allele is the most frequent ALDH2 variant, found in 35-45% of individuals of East Asian origin. It is associated with altered acetaldehyde metabolism and is involved in several hematological diseases (aplastic anemia, bone marrow failure, myelodysplastic syndrome). This review presents current knowledge of different members of the ALDH family and their involvement in normal and malignant hematopoiesis. Focus was brought to the ALDH2 isoenzyme in congenital (Fanconi anemia, Aplastic anemia, mental retardation, and dwarfism (AMeD) syndrome, and idiopathic aplastic anemia) and acquired (acute myeloid leukemia and myelodysplastic syndrome) hematological diseases. It also describes the possibilities of using ALDH as both a biomarker and therapeutic target, to identify and eradicate leukemic stem cells in malignant diseases. - Source: PubMed
Foucault AmélieHérault Olivier - Retinoic acid signaling pathway plays a role in regulating vertebrate development, cell differentiation, and homeostasis. As a key enzyme that catalyzes the oxidation of retinal to retinoic acid, aldehyde dehydrogenase 1 family member A2 (Aldh1a2) is involved in cardiac development, while whether it functions in heart diseases remains to be studied. In this study, we infected primary cardiomyocytes with adenovirus overexpressing (Ad-Aldh1a2) to explore the effects of overexpression on the biological function of cardiomyocytes. The results showed that the infection with Ad-Aldh1a2 realized the overexpression of in cardiomyocytes. Compared with the control group infected with Ad-GFP, the cardiomyocytes infected with Ad-Aldh1a2 showcased significantly increased size and up-regulated expression levels of the atrial natriuretic factor gene (), brain natriuretic peptide gene (), and βmyosin heavy chain (-). In addition, 5-ethynyl-2'-deoxyuridine (EdU) incorporation assay demonstrated that overexpression increased the proportion of cardiomyocytes with positive EdU signals and upregulated the expression levels of proliferation-related genes cyclin D2 () and budding uninhibited by benzimidazole 1 (). The above data indicated that overexpression of induced hypertrophic growth and proliferation of cardiomyocytes. This study provides a basis for further understanding the function of Aldh1a2 in heart diseases and developing therapies for heart diseases. - Source: PubMed
Liu HangLiu QiqiLi ZhenhuaYang XiaoWang Jian