Anti-hPD1-Ni-hIgG1fut

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Human PD-1 (nivolumab) antibody - Human IgG1, non-fucosylated
Anti-hPD1-Ni-hIgG1fut

Anti-hPD1-Ni-hIgG1fut features the constant region of the human IgG1 isotype and the variable region of nivolumab. Nivolumab is a fully human IgG4 (S228P) monoclonal antibody that targets the programmed cell death 1 (PD-1) receptor found on activated T cells, B cells, and myeloid cells. Under normal physiological conditions, PD-1 negatively regulates T cell activation thereby preventing autoimmunity [1]. Under pathological conditions, cancer cells produce PD-L1 (programmed cell death 1 ligand 1), the agonist that binds and activates PD-1. Activated PD-1 enables 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]. This antibody contains an engineered hinge region mutation (S228P) designed to prevent exchange of IgG4 molecules. Nivolumab has been approved by the FDA for the treatment of melanoma and metastatic squamous non-small cell lung cancer (NSCLC). 

Anti-hPD1-Ni-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]. It has been produced in CHO cells that are deficient for fucosylation and purified by affinity chromatography with protein G.

References:

  1. McDermott D. & Atkins M., 2013. PD-1 as a potential target in cancer therapy. Cancer Med. 2: 662–73.
  2. 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.
  3. Gunturi A. & McDermott DF., 2015. Nivolumab for the treatment of cancer. Expert Opin Investig Drugs. 24:253-60.
  4. Yamane-Ohnuki N. & Satoh M., 2009. Production of therapeutic antibodies with controlled fucosylation.corresponding MAbs. 1(3): 230–236.
  5. Mizushima T., 2011. Structural basis for improved efficacy of therapeutic antibodies on defucosylation of their Fc glycans. Genes Cells. 16(11): 1071–1080

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