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. 2014 Feb 5;289(11):7935–7947. doi: 10.1074/jbc.M113.512780

FIGURE 1.

FIGURE 1.

Recombinant uPARAP and MR, but not PLA2R and DEC-205, bind collagens type I and IV. A, overview of domains in the full-length receptors belonging to the MR protein family and in soluble recombinant constructs. uPARAP, MR, PLA2R, and DEC-205 consist of a large ectodomain (including a Cys-rich domain, an FN-II domain, and 8–10 CTLDs), a transmembrane (TM) region, and a short cytoplasmic domain (Cyto). Soluble recombinant proteins (uPARAP D1–3, MR D1–3, PLA2R D1–3, DEC-205 D1–3) consist of the Cys-Rich domain, the FN-II domain, and the first CTLD fused to a protein-epitope tag. B, SDS-PAGE analysis and Coomassie Brilliant Blue staining of recombinant proteins (1.5 μg samples). The theoretical molecular masses are 53.3, 51.5, 54.6, and 50.5 kDa for uPARAP D1–3, MR D1–3, PLA2R D1–3, and DEC-205 D1–3, respectively. C, ELISA analysis of the binding of soluble recombinant protein (0, 1, 3, and 9 μg/ml) to immobilized, heat-denatured collagen type I (5 μg/ml, left panel) and IV (5 μg/ml, right panel). Recombinant protein binding was detected with an anti-tag mAb and a secondary HRP-coupled antibody. Error bars represent S.D. of duplicate samples.