アフコシル化抗体発現プラットフォーム アフコシル化抗体発現プラットフォーム

CHOK1-FUT8アフコシル化抗体の発現

CHOK1-FUT8 Afucosylated Antibody Expression
  • Fut8遺伝子ノックアウト細胞株
  • 高い収率と品質
  • カスタムサービス

サービス概要

アフコシル化抗体の生産のため、CHOK1-Fut8KO発現プラットフォームを新たに立ち上げました。当社のハイスループット・リコンビナント抗体発現プラットフォームと細胞培養技術との組み合わせ、研究および産業上のニーズに合わせてアフコシル化抗体を迅速に生産することができます。アフコシル化は、antibody-dependent cell-mediated cytotoxicity (ADCC)を著しく高めることが示されており、有効性を高めることにより標的療法の可能性を広げます。

アフコシル化抗体発現プラットフォーム Overview

高純度と低エンドトキシンレベル


ノックアウトされたFut8細胞株は、アフコシル化抗体の生産に適用されています。 Fut8は、α-1,6フコシルグリコシド結合の形成を触媒する酵素であり、したがって、アスパラギン酸に結合したN-アセチルグルコサミン部位へのフコースの付加を行います。1


フコースフリー宿主細胞CHOK1BN-Fut8KOは、抗体の特性評価と機能検証を行った後、工業生産に使用することができます。一般的なCHOK1BN細胞株と比較して、CHOK1BN-Fut8KOによって産生された抗体は、アフコシル化が達成されるだけでなく、発現量と品質の面でも一貫性が保たれます。

アフコシル化抗体発現プラットフォーム Overview

ハイライト

Fut8遺伝子ノックアウト細胞株

  • Fut8遺伝子ノックアウト細胞株を使用します。
  • 宿主細胞株はフコースが除去されていることを保証します。

高収量と高品質

  • 高純度とエンドトキシンレベルの低い抗体を製造します。

カスタムサービス

  • 抗体配列をご提供いただくだけで、抗体発現作業ができます。
  • 素早い出荷・納品

事例研究

  • 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

FAQs

  • 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

参考文献一覧

  • 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

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