The deduced 418-amino acid human protein contains a signal sequence, followed by a VA domain, 2 fibronectin type III (F3) repeats, and a short pro/arg-rich C terminus. The VA domain has a putative metal ion-dependent adhesion site (MIDAS) motif and 2 potential O-linked glycosylation sites, and each F3 domain has a putative N-glycosylation site. Human WARP shares 79% amino acid identity with mouse Warp. RT-PCR of mRNA from various mouse tissues and cell lines detected Warp expression only in chondrocytes. Northern blot analysis confirmed expression of Warp in chondrocytes isolated from newborn mouse rib cartilage. Western blot analysis of transfected human embryonic kidney cells detected a 48-kD protein in both cell layer and media fractions.
Mouse Von Willebrand factor A domain-containing protein 1 (VWA1) ELISA Kit employs a two-site sandwich ELISA to quantitate VWA1 in samples. An antibody specific for VWA1 has been pre-coated onto a microplate. Standards and samples are pipetted into the wells and anyVWA1 present is bound by the immobilized antibody. After removing any unbound substances, a biotin-conjugated antibody specific for VWA1 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 VWA1 bound in the initial step. The color development is stopped and the intensity of the color is measured.
Mouse Von Willebrand factor A domain-containing protein 1 (VWA1) 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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