Recombinant Human DDR2 Kinase/CD167b Protein (aa 422-855, His & GST Tag) (PKSH030420)
For research use only.
| Synonyms | CD167, MIG20a, NTRKR3, TKT, TYRO10 |
| Species | Human |
| Expression Host | Baculovirus-Insect Cells |
| Sequence | Arg422-Glu855 |
| Accession | Q16832 |
| Calculated Molecular Weight | 77.1 kDa |
| Observed Molecular Weight | 77 kDa |
| Tag | N-His-GST |
| Bio-activity | The specific activity was determined to be 8 nmol/min/mg using synthetic AXLtide peptide(CKKSRGDYMTMQIG) as substrate. |
| Purity | > 95 % as determined by reducing SDS-PAGE. |
| Endotoxin | < 1.0 EU per μg of the protein as determined by the LAL method. |
| Storage | Store at < -20°C, stable for 6 months. Please minimize freeze-thaw cycles. |
| Shipping | This product is provided as liquid. It is shipped at frozen temperature with blue ice/gel packs. Upon receipt, store it immediately at < - 20°C. |
| Formulation | Supplied as sterile solution of 20mM Tris, 500mM NaCl, pH 7.4, 10% glycerol |
| Reconstitution | Not Applicable |
| Background | Discoidin domain receptor 2 (DDR2) or CD167b (cluster of differentiation 167b) is a kind of protein tyrosine kinases associated with cell proliferation and tumor metastasis, and collagen, identified as a ligand for DDR2, up-regulates matrix metallloproteinase 1 (MMP-1) and MMP-2 expression in cellular matrix. DDR2/CD167b was found to recognise the triple-helical region of collagen X as well as the NC1 domain. Binding to the collagenous region was dependent on the triple-helical conformation. DDR2/CD167b autophosphorylation was induced by the collagen X triple-helical region but not the NC1 domain, indicating that the triple-helical region of collagen X contains a specific DDR2 binding site that is capable of receptor activation. DDR2/CD167b is induced during stellate cell activation and implicate the phosphorylated receptor as a mediator of MMP-2 release and growth stimulation in response to type I collagen. Moreover, type I collagen-dependent upregulation of DDR2/CD167b expression establishes a positive feedback loop in activated stellate cells, leading to further proliferation and enhanced invasive activity. |
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