|Datasheet||Specific References||Reviews||Related Products||Protocols|
|RP11-572K18.1, MIG20a, NTRKR3, TKT, TYRO10|
|A DNA sequence encoding the extracellular domain (Met 1-Arg 399) of human DDR2 precursor (NP_001014796.1) was expressed with the fused Fc region of human IgG1 at the C-terminus.|
|In general, recombinant proteins are provided as lyophilized powder which are shipped at ambient temperature.|
Bulk packages of recombinant proteins are provided as frozen liquid. They are shipped out with blue ice unless customers require otherwise.
|> 95 % as determined by SDS-PAGE|
|Measured by its binding ability in a functional ELISA. Immobilized Rat tail Collagen I at 10 μg/ml can bind recombinant human DDR2-Fc Chimera with a linear range of 2.5-80 ng/ml. Scatchard analysis showed the affinity constant (Kd) of recombinant human DDR2-Fc Chimera bound to rat tail collagen I was 6.8 nM .|
|< 1.0 EU per μg of the protein as determined by the LAL method|
|Samples are stable for up to twelve months from date of receipt at -70℃|
|The recombinant human DDR2/Fc is a disulfide-linked homodimeric protein. The reduced monomer consists of 616 amino acids and has a calculated molecular mass of 69.4 kDa. Due to glycosylation, rhDDR2/Fc monomer migrates as an approximately 87 kDa protein in SDS-PAGE under reducing conditions.|
|Lyophilized from sterile PBS, pH 7.4|
1. Normally 5 % - 8 % trehalose and mannitol are added as protectants before lyophilization. Specific concentrations are included in the hardcopy of COA.
2. Please contact us for any concerns or special requirements.
|Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.|
|A hardcopy of COA with reconstitution instruction is sent along with the products. Please refer to it for detailed information.|
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.