Afucosylated Antibody Expression Afucosylated Antibody Expression

CHOK1-FUT8 Afucosylated
Antibody Expression

Antibody Production
  • Fut8 gene knock-out cell line
  • High Yield and Quality
  • Customized Services


Enhance The Efficacy of Your Antibodies with Our Powerful Platform.

Our newly launched CHOK1-Fut8KO expression platform for afucosylated antibodies. Combined with our high-throughput recombinant antibody expression platform and cell culture technology, afucosylated antibodies can be rapidly produced for your research and industrial needs. Afucosylation has been shown to significantly boost antibody-dependent cell-mediated cytotoxicity (ADCC), opening up a realm of possibilities for targeted therapies by increasing effectiveness.

Afucosylated Antibody Expression Overview

Antibodies with high purity and low endotoxin levels!

knocked-out Fut8 cell line is applied in producing afucosylated antibodies. Fut8 is an enzyme that catalyzes the formation of α-1,6 fucosyl glycosidic bonds, and thus the addition of fucose to asparagine-linked N-acetylglucosamine moieties.1

Biointron’s fucose-free host cell CHOK1BN-Fut8KO can be used for industrial production after antibody characterization and functional verification. Compared to the unmodified CHOK1BN cell line, the antibody produced by the modified cell line not only achieves afucosylation but also maintains consistency in terms of expression quantity and quality.

Afucosylated Antibody Expression Overview


Fut8 gene knock-out cell line

  • Fut8 gene knockout cell line is used
  • We guarantee the host cell line will have fucose removed

High Yield and Quality

  • Produce antibodies with high purity and low endotoxin levels

Customized Services

  • Simply provide your customized sequences and we will express your antibodies for you
  • Fast antibody delivery cycle for purified antibodies

Case Study

  • Case 1: Glycosylation Profiling
    sample C2193xxxx-1
    Deconvoluted mass spectrum of the full molecular weight for sample C2193xxxx-1
    sample C2193xxxx-2
    Deconvoluted mass spectrum of the full molecular weight for sample C2193xxxx-2
  • Case 2: Purity Verification of the Antibody Expressed by CHOK1BN-Fut8KO
    Purity verification of C2193xxxx-1
    Purity verification of C2193xxxx-1
    Purity verification of C2193xxxx-1: CHOK1BN
    Purity verification of C2193xxxx-2
    Purity verification of C2193xxxx-2
    Purity verification of C2193xxxx-2: CHOK1BN-Fut8KO
  • Case 3: Antibody ADCC ActivityBiacore affinity detection results
    ADCC testing results
    ADCC testing results
  • Case 4: Antibody Affinity Measuring
    Y3; B2258xxx2; 1:1 binding
    Y4; B2258xxx2; 1:1 binding
    Y3; B2258xxx3; 1:1 binding
    Y4; B2258xxx3; 1:1 binding
“The newest offering in our service catalog, Biointron’s CHOK1-FUT8 afucosylated antibody expression, is an exciting addition to our capabilities. Heavily researched, afucosylation will improve your antibody efficacy, and my seasoned team of scientists will make sure the end results go above and beyond expectations.”
Xinyi Zhang
Xinyi Zhang
Antibody Production Team


  • Why should you use afucosylated antibodies?

    Afucosylation has been demonstrated to increase the effectiveness of antibody-dependent cellular cytotoxicity (ADCC). ADCC is regulated by N-linked glycosylation in the Fc region of the antibody.

    Importantly, in therapeutic antibodies such as CD20, Her2, and EGFR, absence of core fucose on the Fc N-glycan enhances IgG1 Fc binding affinity to FcγRIIIa on immune effector cells such as natural killer cells. This results in increased ADCC activity, and thus can improve therapeutic efficacy.2

  • Why are CHO cells used?

    Chinese hamster ovary (CHO) cell lines are derived from the ovary of adult, female Chinese hamsters. CHO cells were first established in 1957 by T. Puck, and were subsequently multiplied and optimized in vitro, allowing it to be cultured indefinitely. The CHO-K1 cell line was derived as a subclone from that parental CHO cell line. They are typically the preferred host expression system for recombinant antibodies due to their advantages in producing complex therapeutics, manufacturing adaptability, and glycosylation features similar to human IgG.3

    However, the Fc domain of the anti-tumor antibody drugs produced by wild-type CHO cells carries fucose sugar residues on both of its two biantennary complex polysaccharide chains. The presence of fucose residues can hinder the binding between the antibody and Fc receptor, thereby affecting the antibody's ADCC activity and anti-cancer efficacy.

    Although YB2/0 hybridoma cells and plant cells can be used as alternatives to CHO cells for producing antibody molecules, they lack the stability and scalability advantages of CHO cells.

  • How is antibody-dependent cellular cytotoxicity triggered?

    ADCC causes the natural killer (NK) cells to release cytokines and cytolytic agents, eventually killing the target cell. This is triggered by the engagement of immune complexes with FcγRIIIa present on NK cells, when the Fc binds with the Fc-γ receptor. This binding is significantly influenced by N-glycans in the CH2 structural domain.2

  • What makes afucosylated antibodies different from recombinant antibodies?

    Afucosylated antibodies are monoclonal antibodies which have been modified. The N-glycan (oligosaccharide and sialylation) residues in the antibody’s Fc region do not have core fucose sugar units, which can increase the effector function of ADCC.

    Several factors, including cell line characteristics, process control parameters, and cell culture medium components, may affect glycosylation and, consequently, biological activity, efficacy, stability, immunogenicity, clearance rate, and ADCC.2


  • Ma, M., Fu, Y., Zhou, X., Guan, F., Wang, Y., & Li, X. (2019). Functional roles of fucosylated and O-glycosylated cadherins during carcinogenesis and metastasis. Cellular Signalling, 63, 109365.
  • Pereira, N. A., Chan, K. F., Lin, P. C., & Song, Z. (2018). The "less-is-more" in therapeutic antibodies: Afucosylated anti-cancer antibodies with enhanced antibody-dependent cellular cytotoxicity. mAbs, 10(5), 693–711.
  • Fischer, S., Handrick, R., & Otte, K. (2015). The art of CHO cell engineering: A comprehensive retrospect and future perspectives. Biotechnology Advances, 33(8), 1878-1896.

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