Finetest Protein Recombinant Human ADH5

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FineTest Protein Recombinant Human ADH5 Catalogue No.: P4706 Synonyms: ADH 3, ADH5, ADHX, ADHX_HUMAN, Alcohol dehydrogenase (class III) chi polypeptide, Alcohol dehydrogenase 5, alcohol dehydrogenase 5 (class III) chi polypeptide, Alcohol dehydrogenase class 3, Alcohol dehydrogenase class chi chain, Alcohol dehydrogenase class III, Alcohol dehydrogenase class-3, Alcohol dehydrogenase class-III, class III alcohol dehydrogenase 5 chi subunit, FALDH, FDH Species: Human Uniprot ID: P11766 Expression Region: 1-374 Source: E.Coli Tags: His tag Molecular Weight: 41 kDa Purity: Greater than 95% by SDS-PAGE gel analyses Formulation: Lyophilized from a 0.2um filtered solution in PBS with 5% trehalose, pH7.4 Reconstitution: Sterile distilled water Storage: -20°C for 12 months as lyophilized; 2-8°C for 1 month under sterile conditions after reconstitution Wuhan Fine Biotech Co., Ltd. B9 Bld, High-Tech Medical Devices Park, No. 818 Gaoxin Ave.East Lake High-Tech Development Zone.Wuhan, Hubei, China (430206) Tel: (0086)027-87384275 Fax: (0086)027-87800889 www.fn-test.com FineTest Protein Image: Safety note: This product is intended for research and manufacturing uses only. It is not a diagnostic device. Product degradation will result from multiple freeze/thaw cycles. It is suggested that the antigen be stored in use size aliquots and thawed just prior to use. This material has been inactivated, however as with all biological materials, it should be handled as potentially infectious. The user assumes all responsibility for care, custody and control of the material, including its disposal, in accordance with all regulations. Wuhan Fine Biotech Co., Ltd. B9 Bld, High-Tech Medical Devices Park, No. 818 Gaoxin Ave.East Lake High-Tech Development Zone.Wuhan, Hubei, China (430206) Tel: (0086)027-87384275 Fax: (0086)027-87800889 www.fn-test.com.

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Dehydrogenase Gene of Entamoeba Histolytica
Proc. Nad. Acad. Sci. USA Vol. 89, pp. 10188-10192, November 1992 Medical Sciences Cloning and expression of an NADP+-dependent alcohol dehydrogenase gene of Entamoeba histolytica (amebiasis/protozoan parasite/fermentation/inhibitors) AJIT KUMAR*, PEI-SHEN SHENtt, STEVEN DESCOTEAUX*, JAN POHL§, GORDON BAILEYt, AND JOHN SAMUELSON*1II *Department of Tropical Public Health, Harvard School of Public Health, Boston, MA 02115; tDepartment of Biochemistry, Morehouse School of Medicine, Atlanta, GA 30310; §Microchemical Facility, Emory University, Atlanta, GA 30322; and 'Department of Pathology, New England Deaconess Hospital, Boston, MA 02215 Communicated by Elkan Blout, June 29, 1992 (receivedfor review May 1, 1992) ABSTRACT Ethanol is the major metabolic product of NAD(P)+ so that the reducing equivalents are regenerated glucose fermentation by the protozoan parasite Entmoeba (4-7). Both NADP+-dependent and NAD+-dependent alco- histolytica under the anaerobic conditions found in the lumen hol dehydrogenase (ADH) activities have been identified in of the colon. Here an internal peptide sequence determined E. histolytica trophozoites (4-7). The NADP+-dependent from a major 39-kDa amoeba protein isolated by isoeLtric ADH (EhADHi; EC 1.1.1.2) was found to be composed of focusing followed by SDS/PAGE was used to clone the gene for four -30-kDa subunits, prefer secondary alcohols to primary the E. histolytica NADP+-dependent alcohol dehydrogenase alcohols, and be inhibited by the substrate analogue pyrazole (EhADH1; EC 1.1.1.2). The EhADHi clone had an open (7). The amoeba NAD+-dependent ADH (EC 1.1.1.1) is not reading frame that was 360 amino acids long and encoded a well-characterized (4).
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The Failure of Two Major Formaldehyde Catabolism Enzymes (ADH5 and ALDH2) Leads to Partial Synthetic Lethality in C57BL/ 6 Mice Jun Nakamura1,2*, Darcy W
Nakamura et al. Genes and Environment (2020) 42:21 https://doi.org/10.1186/s41021-020-00160-4 SHORT REPORT Open Access The failure of two major formaldehyde catabolism enzymes (ADH5 and ALDH2) leads to partial synthetic lethality in C57BL/ 6 mice Jun Nakamura1,2*, Darcy W. Holley3, Toshihiro Kawamoto4 and Scott J. Bultman3 Abstract Background: Exogenous formaldehyde is classified by the IARC as a Category 1 known human carcinogen. Meanwhile, a significant amount of endogenous formaldehyde is produced in the human body; as such, formaldehyde-derived DNA and protein adducts have been detected in animals and humans in the absence of major exogenous formaldehyde exposure. However, the toxicological effects of endogenous formaldehyde on individuals with normal DNA damage repair functions are not well understood. In this study, we attempted to generate C57BL/6 mice deficient in both Adh5 and Aldh2, which encode two major enzymes that metabolize endogenous formaldehyde, in order to understand the effects of endogenous formaldehyde on mice with normal DNA repair function. Results: Due to deficiencies in both ADH5 and ALDH2, few mice survived past post-natal day 21. In fact, the survival of pups within the first few days after birth was significantly decreased. Remarkably, two Aldh2−/−/Adh5−/− mice survived for 25 days after birth, and we measured their total body weight and organ weights. The body weight of Aldh2−/−/Adh5−/− mice decreased significantly by almost 37% compared to the Aldh2−/−/Adh5+/− and Aldh2−/−/Adh5+/+ mice of the same litter. In addition, the absolute weight of each organ was also significantly reduced. Conclusion: Mice deficient in both formaldehyde-metabolizing enzymes ADH5 and ALDH2 were found to develop partial synthetic lethality and mortality shortly after birth.
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Age-Dependent Protein Abundance of Cytosolic Alcohol and Aldehyde Dehydrogenases in Human Liver S
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Computational Exploration of the Medium-Chain Dehydrogenase / Reductase Superfamily
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Anti-ADH5 Monoclonal Antibody, Clone FQS23996(C) (DCABH-6425) This Product Is for Research Use Only and Is Not Intended for Diagnostic Use
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32-2124: ADH5 Recombinant Protein Description Product Info
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