Recombinant Mouse Leucine-rich repeat-containing protein 15（Lrrc15), partial (Active)

Lrrc15 is emerging as a critical marker of cancer-associated fibroblasts and a regulator of tumor-stromal interactions, making functional protein reagents essential for dissecting its role in the tumor microenvironment. This mammalian-expressed fragment spanning residues 22–536 captures the extracellular leucine-rich repeat domain and demonstrates quantifiable binding activity to an anti-LRRC15 antibody with an EC50 of 4.841–6.280 ng/mL in functional ELISA, confirming native epitope presentation suitable for antibody development and validation studies. The demonstrated binding capacity supports use in cell adhesion and migration assays where Lrrc15-mediated interactions govern fibroblast behavior, as well as in tumor metastasis research examining stromal contributions to cancer progression. With greater than 95% purity and endotoxin levels below 1.0 EU/μg, this protein meets the quality thresholds commonly required for cell-based functional assays and protein-protein interaction studies investigating Lrrc15 biology in cancer contexts.