LEPREL1 belongs to a family of collagen prolyl hydroxylases required for proper collagen biosynthesis, folding, and assembly. The deduced 708-amino acid protein has an N-terminal signal peptide, 4 tetratricopeptide repeats, 4 CxxxC motifs, a central leucine zipper, a prolyl 4-hydroxylase-alpha domain, which contains an ATP/GTP-binding site, and a C-terminal endoplasmic reticulum (ER) retention motif (KDEL). LEPREL1 also has 3 potential N-glycosylation sites and putative glycosaminoglycan attachment sites. It shares 53% and 45% amino acid identity with LEPRE1 and LEPRE2, respectively. Northern blot analysis detected weak expression of a 3.4-kb transcript in most tissues examined, with higher levels in placenta and kidney. A 6.5-kb transcript was expressed abundantly in skeletal muscle and more weakly in heart.
Chicken Prolyl 3-hydroxylase 2 (LEPREL1) ELISA Kit employs a two-site sandwich ELISA to quantitate LEPREL1 in samples. An antibody specific for LEPREL1 has been pre-coated onto a microplate. Standards and samples are pipetted into the wells and anyLEPREL1 present is bound by the immobilized antibody. After removing any unbound substances, a biotin-conjugated antibody specific for LEPREL1 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 LEPREL1 bound in the initial step. The color development is stopped and the intensity of the color is measured.
Chicken Prolyl 3-hydroxylase 2 (LEPREL1) 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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