The original antibody was obtained by immunizing mice with soluble recombinant human DR5 protein
Conjugate
Unconjugated
Applications
Application Notes
ELISA, FuncS Each laboratory should determine an optimum working titer for use in its particular application. Other applications have not been tested but use in such assays should not necessarily be excluded.
General Notes
DR5-01 and DR5-05 are designed to induce apoptosis in cancer cells by targeting DR5, with potential applications in cancer therapy, particularly in tumor types with high DR5 expression levels. DR5-01 and DR5-05 have been reported that can bind to two distinct epitopes on DR5, enhancing their affinity and specificity to effectively induce apoptosis.
Images
Binding characteristics of DR5-01 and DR5-05. Binding of DR5-01 and DR5-05 to HCT 116 colorectal cancer (CRC) cells was measured by FC. *DR5-01 and DR5-05 were modified by adding an E430G hexamerization-enhancing mutation in the Fc domain to create Hx-DR5-01 and Hx-DR5-05.
Crossblock binding ELISA with immobilized Hx-DR5-01 (left graph) and immobilized Hx-DR5-05 (right graph) in the presence of ECD of DR5 and the indicated competing antibodies. Data show percentage inhibition of binding to DR5 and is the mean of triplicate samples. *DR5-01 and DR5-05 were modified by adding an E430G hexamerization-enhancing mutation in the Fc domain to create Hx-DR5-01 and Hx-DR5-05.
We offer labeled antibodies using our catalogue antibody products and a broad range of intensely fluorescent dyes and labels including HRP, biotin, ALP, Alexa Fluor® dyes, DyLight® Fluor dyes, R-phycoerythrin (R-PE), at scales from less than 100 μg up to 1 g of IgG antibody. Learn More
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Hi-Puri™ Anti-Human DR5 monoclonal antibody
Binding characteristics of DR5-01 and DR5-05. Binding of DR5-01 and DR5-05 to HCT 116 colorectal cancer (CRC) cells was measured by FC. *DR5-01 and DR5-05 were modified by adding an E430G hexamerization-enhancing mutation in the Fc domain to create Hx-DR5-01 and Hx-DR5-05.
Crossblock binding ELISA with immobilized Hx-DR5-01 (left graph) and immobilized Hx-DR5-05 (right graph) in the presence of ECD of DR5 and the indicated competing antibodies. Data show percentage inhibition of binding to DR5 and is the mean of triplicate samples. *DR5-01 and DR5-05 were modified by adding an E430G hexamerization-enhancing mutation in the Fc domain to create Hx-DR5-01 and Hx-DR5-05.
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