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Non-fucosylated monoclonal human IgG1 antibody against human PD-L1
Anti-hPD-L1-hIgG1 features the constant region of the human IgG1 isotype and the variable region of atezolizumab. Atezolizumab (also known as MPDL3280A) is a fully humanized IgG1 (N298A) monoclonal antibody that targets the programmed cell death ligand 1 (PD-L1), a transmembrane protein over-expressed on tumor cells and tumor infiltrating immune cells, such as macrophages. PD-L1 binds to programmed cell death protein 1 (PD-1) on cytotoxic T cells, inhibiting the antitumor immune response . Atezolizumab blocks the interaction of PD-L1 with PD-1 and induces anti-tumor immune reactivation. Atezolizumab contains a modified Fc region designed to limit antibody-dependent cytotoxicity (ADCC) and complement-dependent cytotoxicity (CDC) [2, 3]. The mutation N298A eliminates its ability to bind to human Fcγ receptors. FDA has granted atezolizumab priority review for advanced bladder cancer.
Anti-hPD-L1-hIgG1fut is a non-fucosylated antibody. The absence of the fucose residue from the N-glycans of IgG-Fc results in dramatic enhancement of antibody-dependent cellular cytotoxicity (ADCC) without any detectable change in complement-dependent cytotoxicity (CDC) or antigen binding capability [4, 5].
Anti-hPD-L1-hIgG1fut was generated by recombinant DNA technology. It has been produced in CHO cells that are deficient for fucosylation and purified by affinity chromatography with protein G.
- McDermott D. & Atkins M. 2013. PD-1 as a potential target in cancer therapy. Cancer Med. 2(5): 662–673.
- Spigel D. et al., 2013. Clinical activity, safety, and biomarkers of MPDL3280A, an engineered PD-L1 antibody in patients with locally advanced or metastatic non-small cell lung cancer (NSCLC) [ASCO abstract 8008]. J Clin Oncol. 31(15)(suppl).
- Herbst RS. et al., 2014. Predictive correlates of response to the anti-PD-L1 antibody MPDL3280A in cancer patients. Nature. 515(7528):563-7.
- Yamane-Ohnuki N. & Satoh M., 2009. Production of therapeutic antibodies with controlled fucosylation.corresponding MAbs. 1(3): 230–236.
- Mizushima T., 2011. Structural basis for improved efficacy of therapeutic antibodies on defucosylation of their Fc glycans. Genes Cells. 16(11): 1071–1080.
Specificity: Targets cells expressing human and mouse PD-L1
Clonality: Monoclonal antibody
Isotype: Human IgG1
Source: CHO cells
Purity: Purified by affinity chromatography with protein G
- Binding of Anti-hPD-L1-hIgG1fut to hPD-L1 has been validated using flow cytometry in EL4 cells expressing membrane-bound human PD-L1.
- ADCC has been tested using CD16-expressing Jurkat-NFAT reporter cells.
- The complete sequence of this antibody has been verified.
- The absence of bacterial contamination (e.g. lipoproteins and endotoxins) has been confirmed using HEK-Blue™ TLR2 and HEK-Blue™ TLR4 cells.
• 100 µg purified anti-hPD-L1-hIgG1fut antibody, provided azide-free and lyophilizedBack to the top