|Application ||WB, IHC-P, FC, E|
|Calculated MW||39724 Da|
|Antigen Region||212-239 aa|
|Other Names||Alcohol dehydrogenase class-3, Alcohol dehydrogenase 5, Alcohol dehydrogenase class chi chain, Alcohol dehydrogenase class-III, Glutathione-dependent formaldehyde dehydrogenase, FALDH, FDH, GSH-FDH, 111-, S-(hydroxymethyl)glutathione dehydrogenase, ADH5 (HGNC:253), ADHX, FDH|
|Target/Specificity||This ADH5 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 212-239 amino acids from the Central region of human ADH5.|
|Format||Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is purified through a protein A column, followed by peptide affinity purification.|
|Storage||Maintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.|
|Precautions||ADH5 Antibody (Center) is for research use only and not for use in diagnostic or therapeutic procedures.|
|Function||Class-III ADH is remarkably ineffective in oxidizing ethanol, but it readily catalyzes the oxidation of long-chain primary alcohols and the oxidation of S-(hydroxymethyl) glutathione.|
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Provided below are standard protocols that you may find useful for product applications.
ADH5 is a member of the alcohol dehydrogenase family. Members of this family metabolize a wide variety of substrates, including ethanol, retinol, other aliphatic alcohols, hydroxysteroids, and lipid peroxidation products. This protein forms a homodimer. It has virtually no activity for ethanol oxidation, but exhibits high activity for oxidation of long-chain primary alcohols and for oxidation of S-hydroxymethyl-glutathione, a spontaneous adduct between formaldehyde and glutathione. This enzyme is an important component of cellular metabolism for the elimination of formaldehyde, a potent irritant and sensitizing agent that causes lacrymation, rhinitis, pharyngitis, and contact dermatitis.
Martins-de-Souza,D., et.al., Eur Arch Psychiatry Clin Neurosci 259 (3), 151-163 (2009)
Iborra,F.J., et.al., J. Histochem. Cytochem. 40 (12), 1865-1878 (1992)
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