Technical Data
A1331-05A
ADH5 (Alcohol Dehydrogenase Class-3, Alcohol Dehydrogenase Class-III, Alcohol Dehydrogenase 5, Alcohol Dehydrogenase Class chi Chain, S-(hydroxymethyl)glutathione Dehydrogenase, Glutathione-dependent Formaldehyde Dehydrogenase, GSH-FDH, FALDH, FDH, ADHX)
Description:
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.

Applications:
Suitable for use in ELISA and Western Blot. Other applications not tested.

Recommended Dilution:
ELISA: 1:1000
Western Blot: 1-3ug/ml
Optimal dilutions to be determined by the researcher.

Storage and Stability:
May be stored at 4C for short-term only. Aliquot to avoid repeated freezing and thawing. Store at -20C. Aliquots are stable for at least 12 months. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap.
TypeIsotypeCloneGrade
PabAffinity Purified
SizeStorageShippingSourceHost
100ug-20CBlue IceMouseGoat
Concentration:
~0.5mg/ml
Immunogen:
Synthetic peptide corresponding to C-KKIKVDEFVTHN, from mouse ADH5, at the internal region of the protein (NP_000662.3).
Purity:
Purified by immunoaffinity chromatography.
Form
Supplied as a liquid in Tris saline, 0.02% sodium azide, pH 7.3, 0.5% BSA.
Specificity:
Recognizes mouse ADH5. Species sequence homology: Bovine, canine, human, porcine and rat.
Intended for research use only. Not for use in human, therapeutic, or diagnostic applications.
1. Adinolfi A, Adinolfi M, Hopkinson DA. Immunological and biochemical characterization of the human alcohol dehydrogenase chi-ADH isozyme. Ann Hum Genet. 1984 Jan;48(Pt 1):1-10.