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Human PD-1 (nivolumab) antibody - Human IgG1, non-glycosylated
Non-glycosylated monoclonal human IgG1 antibody against human PD-1
Anti-hPD1-Ni-hIgG1NQ features a mutated constant region of the human IgG1 isotype and the variable region of nivolumab. Nivolumab is a fully human IgG4 (S228P) monoclonal antibody that contains an engineered hinge region mutation (S228P) designed to prevent exchange of IgG4 molecules. It targets the PD-1 receptor found on activated T cells, B cells, and myeloid cells. PD-1 negatively regulates T cell activation thereby preventing autoimmunity . However, under pathological conditions, cancer cells produce PD-L1 (programmed cell death 1 ligand 1), the agonist that binds and activates PD-1 enabling the cancer cells to evade the immune system. Nivolumab binds and blocks the activation of the PD-1 receptor, thereby resulting in the activation of T cells and cell‑mediated immune responses [2,3]. It has been approved by the FDA for the treatment of melanoma and squamous non-small cell lung cancer.
Anti-hPD1-Ni-hIgG1NQ contains a N-glycosylation mutation of the constant region of the human IgG1 where potential asparagine (N) glycosylation sites are substituted by glutamine (Q) residues resulting in the production of a non‑glycosylated antibody. Glycosylation of an antibody has no effect on antigen binding but is essential for Fc receptor-mediated activity . In non‑glycosylated antibodies the effector mechanisms mediated through the Fc receptors types (FcγRI, FcγRII, FcγRIII) and the C1q component of complement are severely compromised or ablated . It has been produced in CHO cells and purified by affinity chromatography with protein G.
Applications: Anti-hPD1-Ni-hIgG1NQ can be used with Anti-hPD1-Ni-hIgG1 to study the impact of effector functions.
- McDermott D. & Atkins M., 2013. PD-1 as a potential target in cancer therapy. Cancer Med. 2: 662–73.
- Wang C. et al., 2014. In vitro characterization of the anti-PD-1 antibody nivolumab, BMS- 936558, and in vivo toxicology in non-human primates..Cancer Immunol Res. 2:846-56.
- Gunturi A. & McDermott DF., 2015. Nivolumab for the treatment of cancer. Expert Opin Investig Drugs. 24:253-60.
- Arnold J. et al., 2007. The impact of glycosylation on the biological function and structure of human immunoglobulins. Annu Rev Immunol 25:21-50.
- Jefferis R., 2009. Glycosylation as a strategy to improve antibody-based therapeutics. Nat Rev Drug Discov. 8:226-34.
Specificity: Targets cells expressing human PD-1
Clonality: Monoclonal antibody
Isotype: Human IgG1
Source: CHO cells
Purity: Purified by affinity chromatography with protein G
- Binding of Anti-hPD1-Ni-hIgG1 to human PD-1 has been tested using flow cytometry.
- 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-hPD1-Ni-hIgG1NQ antibody, provided azide-free and lyophilizedBack to the top