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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

Overview

Upgrading The Efficacy of Your Antibodies with Our Powerful Platform.


Afucosylation has proved to significantly enhance antibody-dependent cell-mediated cytotoxicity (ADCC). This antibody modification has opened up a realm of possibilities of upgraded effectiveness of immunotherapies that involve some types of immune effector cells.


Biointron is excited to introduce our newly launched CHOK1- Fut8KO expression platform for afucosylated antibodies. Integrated with our high-throughput recombinant antibody expression capability and cell line development expertise, afucosylated antibodies can be rapidly produced in Biointron to meet your research and industrial needs.

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 a-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

Highlights

Advanced Gene-Editing Technology

  • Our technology makes possible efficient Fut8 gene knockouts
  • We guarantee the fucose knockout in host cells

High Yield and Quality

  • Trusted, extensive experience in CHO stable cell line development for over 10 years
  • Large­ scale afucosylated antibody production is optional
  • Antibodies production of high purity and low endotoxin levels

Customized Sequence, Customized Expression

  • Simply provide your customized sequences and we will express your antibodies
  • Fast antibody products delivery
Speak to A Specialist

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: Afucosylated antibody ADCC Activity Increase
    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

FAQs

  • Why should you use afucosylated antibodies?

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

    herapeutic antibodies targeting CD20, Her2, and EGFR, etc, with the absence of core fucose on the Fe N-glycan, manifest enhanced Fc binding affinity to FcyRllla 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

Resources

References

  • 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. https://doi.org/10.1016/j.cellsig.2019.109365
  • 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. https://doi.org/10.1080/19420862.2018.1466767
  • 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. https://doi.org/10.1016/j.biotechadv.2015.10.015

Committed to Top-Quality Products

At Biointron, we are deeply committed to delivering top-quality products that surpass customer expectations. With every product we offer, we promise to provide unmatched quality, reliability, and satisfaction to our valued customers. Your trust in our brand fuels our passion for continuous improvement, ensuring that we consistently deliver nothing but the best.

Services & Products

HTP Recombinant
Antibody Production
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Protein Expression In
Mammalian system
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CHO-K1 Stable
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