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.Immune Checkpoint Immunotherapy Cancer Immunotherapy Targeted Therapy
Product Name:
Mouse DDR2 Kinase/CD167b Recombinant Protein (RPES2334)
Measured by its ability to bind rat tail Collagen I in a functional ELISA.
Endotoxin:
<1.0 EU per µg of the protein as determined by the LAL method.
Protein Construction:
A DNA sequence encoding the extracellular domain of mouse DDR2 (NP_072075.2) (Met 1-Arg 399) was expressed, with a polyhistidine tag at the C-terminus.
Purity:
> 95 % as determined by SDS-PAGE
Mol Mass:
44 kDa
AP Mol Mass:
80-90 kDa
Formulation:
Lyophilized from sterile PBS, pH 7.4
Shipping:
This product is provided as lyophilized powder which is shipped with ice packs.
Stability and Storage:
Lyophilized proteins are stable for up to 12 months when stored at -20 to -80°C. Reconstituted protein solution can be stored at 4-8°C for 2-7 days. Aliquots of reconstituted samples are stable at < -20°C for 3 months.
