UNG encodes one of several uracil-DNA glycosylases. One important function of uracil-DNA glycosylases is to prevent mutagenesis by eliminating uracil from DNA molecules by cleaving the N-glycosylic bond and initiating the base-excision repair (BER) pathway. Uracil bases occur from cytosine deamination or misincorporation of dUMP residues. Alternative promoter usage and splicing of this gene leads to two different isoforms: the nuclear (UNG2) and mitochondrial (UNG1) isoforms of UNG result from alternative splicing and the use of alternative promoters. The UNG1 and UNG2 proteins contain different N-terminal sequences, but the downstream 269 amino acids are common and include a short region that binds replication protein A and a larger, compact catalytic domain.
Human Uracil-DNA glycosylase (UNG) ELISA Kit employs a two-site sandwich ELISA to quantitate UNG in samples. An antibody specific for UNG has been pre-coated onto a microplate. Standards and samples are pipetted into the wells and anyUNG present is bound by the immobilized antibody. After removing any unbound substances, a biotin-conjugated antibody specific for UNG is added to the wells. After washing, Streptavidin conjugated Horseradish Peroxidase (HRP) is added to the wells. Following a wash to remove any unbound avidin-enzyme reagent, a substrate solution is added to the wells and color develops in proportion to the amount of UNG bound in the initial step. The color development is stopped and the intensity of the color is measured.
Human Uracil-DNA glycosylase (UNG) ELISA Kit listed herein is for research use only and is not intended for use in human or clinical diagnosis. Suggested applications of our products are not recommendations to use our products in violation of any patent or as a license. We cannot be responsible for patent infringements or other violations that may occur with the use of this product.
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