Human epithelial discoidin domain- containing receptor (DDR1) gene encodes a tyrosine kinase that functions as cell surface receptor for fibrillar collagen and regulates cell attachment to the extracellular matrix, remodeling of the extracellular matrix, cell migration, differentiation, survival and cell proliferation. Collagen binding triggers a signaling pathway that involves SRC and leads to the activation of MAP kinases. Regulates remodeling of the extracellular matrix by up-regulation of the matrix metalloproteinases MMP2, MMP7 and MMP9, and thereby facilitates cell migration and wound healing. Required for normal blastocyst implantation during pregnancy, for normal mammary gland differentiation and normal lactation. It is also required for normal ear morphology and normal hearing. Expression of DDR1 protein is restricted to epithelial cells, particularly in the kidney, lung, gastrointestinal tract, and brain. In addition, it has been shown to be significantly overexpressed in several human tumors. DDR1 promotes smooth muscle cell migration, and thereby contributes to arterial wound healing. It also plays a role in tumor cell invasion.

Full-length extracellular domain of human DDR1 cDNA (21 – 417aa, Isoform-I, derived from BC070070) was constructed with codon optimization and expressed with a small T7-His-TEV cleavage site Tag (29aa) fusion at its N-terminal. This protein was expressed in E. coli as inclusion bodies. The final product was refolded using our unique “temperature shift inclusion body refolding” technology and chromatographically purified.

1. May be used for in vitro DDR1 mediated tumor cell angiogenesis & growth regulation study in MAP kinase pathways for various cells with this protein either as soluble factor or as coating matrix protein.

2. May be used for protein-protein interaction assay.

3. Potential biomarker protein for early clinical diagnosis of several cancers, such as ovarian cancer.

4. As immunogen for specific antibody production.