The deduced 361-amino acid protein has a calculated molecular mass of 42.1 kD. Viperin contains an N-terminal leucine zipper motif and a domain associated with iron-sulfur cluster coordination. Viperin shares significant homology with Best5, which is expressed during rat osteoblast differentiation, and Vig1, which is induced in rainbow trout infected with a fish rhabdovirus. The N-terminal leucine zipper motifs display the least homology. Western blot analysis of IFNG-treated macrophages and transfected HeLa cells revealed a major band of 43 kD and a minor band of 35 kD.HCMV infection caused redistribution of the induced viperin from its normal endoplasmic reticulum association, first to the Golgi apparatus and then to cytoplasmic vacuoles containing gB and the HCMV structural protein pp28.

Human Radical S-adenosyl methionine domain-containing protein 2 (RSAD2) ELISA Kit employs a two-site sandwich ELISA to quantitate RSAD2 in samples. An antibody specific for RSAD2 has been pre-coated onto a microplate. Standards and samples are pipetted into the wells and anyRSAD2 present is bound by the immobilized antibody. After removing any unbound substances, a biotin-conjugated antibody specific for RSAD2 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 RSAD2 bound in the initial step. The color development is stopped and the intensity of the color is measured.

Human Radical S-adenosyl methionine domain-containing protein 2 (RSAD2) 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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