Non-glycosylated monoclonal human IgG1 antibody against human CD20

Anti-hCD20-hIgG1NQ features the variable region of rituximab and a mutated constant region of the human IgG1 isotype.
Rituximab is a mouse/human chimeric monoclonal antibody that targets the CD20 antigen found on the surface of malignant and normal B lymphocytes. Binding of rituximab to CD20 results in cell destruction through different mechanisms including direct signaling of apoptosis, complement activation and cell-mediated cytotoxicity. Rituximab has been approved by the FDA for the treatment of various lymphoid malignancies, including B-cell non-Hodgkin's lymphoma and B-cell chronic lymphocytic leukemia.

Anti-hCD20-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 [1].
In non-glycosylated antibodies the effector mechanisms mediated through the Fc receptors types (FcgRI, FcgRII, FcgRIII) and the C1q component of complement are severely compromised or ablated [2].
Anti-hCD20-hIgG1NQ was generated by recombinant DNA technology. It has been produced in CHO cells and purified by affinity chromatography with protein G.


Clonality: Non-glycosylated Monoclonal antibody
Specificity: Targets cells expressing human CD20
Isotype: Human IgG1
Application :
Anti-hCD20-hIgG1NQ can be compared with anti-hCD20-hIgG1 to study the impact of effector functions.

Quality control
- The absence of bacterial contamination (e.g. endotoxins and peptidoglycans) is controlled using HEK-Blue™ TLR2 and HEK-Blue™ TLR4 cells.
- The recognition of human CD20 with this antibody is tested using flow cytometry.


100 µg purified anti-hCD20-hIgG1NQ antibody, provided azide-free and lyophilized.

Store lyophilized antibody at -20°C. Lyophilized product is stable for 1 year


1. Arnold J. et al., 2007. The impact of glycosylation on the biological function and structure of human immunoglobulins. Annu Rev Immunol 25:21-50.
2. Jefferis R., 2009. Glycosylation as a strategy to improve antibody-based therapeutics. Nat Rev Drug
Discov. 8(3):226-34.


Recent articles using InvivoGen Anti-hCD20-hIgG1NQ



Description Non-glycosylated monoclonal human IgG1 antibody against human CD20
Cat. Codehcd20-mab12
Unit Size100 µg
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Note that the sequence of available ORFs provided by InvivoGen can differ from a given reference Genbank record due to genetic variations and/or alternative splicing. Customers should verify that the version of a gene sold by InvivoGen is suitable for the customer needs.
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