Human Prolyl 3-hydroxylase 2 (LEPREL1) ELISA Kit

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.