Human CD20 Antibody - Obinutuzumab Biosimilar

Non-fucosylated human IgG1 monoclonal antibody (mAb) against human CD20

Anti-hCD20-Ga-hIgG1fut is the biosimilar of the clinical antibody obinutuzumab. Anti-hCD20-Ga-hIgG1fut features the constant region (Fc) of a non-fucosylated (fut), human IgG1 isotype and the variable region of obinutuzumab. Obinutuzumab (formerly named afutuzumab or GA101) targets the human CD20 antigen found on the surface of normal and malignant B lymphocytes.

Obinutuzumab is a type II (second generation) non-fucosylated, fully humanized IgG1 monoclonal antibody with improved therapeutic efficacy compared with previously developed type I (first generation) anti-hCD20 mAbs, such as Rituximab and Ofatumumab. Obinutuzumab has been approved by the FDA to treat chronic lymphocytic leukemia [1-3].

The absence of fucose residues from the Fc N-glycans results in dramatic enhancement of antibody-dependent cellular cytotoxicity (ADCC) without any detectable change in complement-dependent cytotoxicity (CDC) or antigen-binding capability [4].

InvivoGen’s Anti-hCD20-Ga-hIgG1fut is generated by recombinant DNA technology, produced in Chinese hamster ovary (CHO) cells deficient for fucosylation, and purified by affinity chromatography (protein G).

More isotypes of this antibody are available and can be used for comparison of biological activities such as ADCC (see below or in the ' upon request' section).
InvivoGen also provides type I anti-hCD20 mAbs featuring the variable regions of Rituximab or Ofatumumab, with either native or engineered Fc region.

Read our review on Antibody Isotypes

References:

1. Gagez AL. & Cartron G., 2014. Obinutuzumab: a new class of anti-CD20 monoclonal antibody. Curr Opin Oncol. 26(5):484-91.
2. Smolej L., 2014. Targeted treatment for chronic lymphocytic leukemia: clinical potential of obinutuzumab. Pharmgenomics Pers Med. 8:1-7.
3. Winiarska M. et al., 2011. Molecular mechanisms of the antitumor effects of anti-CD20 antibodies. Front Biosci (Landmark Ed). 16:277-306. 4. Mizushima T., 2011. Structural basis for improved efficacy of therapeutic antibodies on defucosylation of their Fc glycans. Genes Cells. 16(11): 1071–1080.