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ScFv-Fc Chimera Products

Introduction Service Fc Options Features

Introduction of ScFv-Fc Chimeras

scFv-Fc chimeras are fusion proteins that combine the single-chain variable fragment (scFv) of an antibody with the constant region (Fc) of an immunoglobulin. This design allows the scFv to retain its antigen-binding specificity while benefiting from the effector functions provided by the Fc region. This combination not only preserves essential Fc functions such as the modulation of immune responses but also enhances therapeutic efficacy, leading to its successful application in diverse fields like immunotherapy, radioimmunotherapy, and the targeted engagement of the receptor-binding domain of SARS-CoV-2, showcasing its versatility in combating infectious diseases and cancer. Creative Biolabs is thrilled to introduce our tailored scFv-Fc chimera products, meticulously crafted to meet your specific requirements! Our dedicated team of experts is committed to assisting you in developing custom scFv-Fc chimera solutions that will ensure the success of your project.

Left: A chimeric full-length antibody. Right: A single-chain Fv-Fc (scFv-Fc) fragment.Fig 1. A chimeric intact antibody (left) and single-chain Fv-Fc (scFv-Fc) fragment (right). 1

Our Services

Our recombinant antibody production service focuses on the creation of single-chain variable fragment-Fc (scFv-Fc) antibodies.

  • Optimization and Synthesis: We utilize proprietary expression vectors to optimize and synthesize the variable regions of antibodies (VH and VL) or scFv-Fc antibodies, ensuring efficient and reliable recombinant antibody expression.
  • Transient Production: We produce recombinant antibodies in mammalian cells using transient expression to enhance efficiency.
  • Purification: We purify the recombinant antibodies using Protein A and other necessary purification methods.

scFv-Fc constructs, made as a single protein, retain the specificity of the original antibody while offering advantages in terms of construction speed, production yield, and engineering flexibility compared to full IgG. Clients can choose between human IgG1-Fc or mouse IgG2a-Fc scaffolds for their scFv-Fc designs. The process involves linking VH and VL via a short peptide linker (10-25 amino acids) to create the final recombinant scFv-Fc construct.

Fc Options

These Fc options provide researchers and clinicians with a rich toolkit to tailor their applications in therapeutic development, diagnostic reagents, and biomarker applications to meet specific needs. The Fc fusion protein options cover a diverse range, including but not limited to:

Fc-types Functions
Human IgG Subtypes Human IgG1-Fc: Known for its strong antibody-dependent cellular cytotoxicity (ADCC) characteristics.
Human IgG2-Fc: Renowned for its ability to stimulate complement fixation and its role in polysaccharide antigen immune responses.
Human IgG3-Fc: Exhibits the highest complement activation capability, often associated with enhanced immune responses.
Human IgG4-Fc: Unique among the subtypes, it promotes immune tolerance and has a weaker complement activation capacity.
Mouse IgG Subtypes Mouse IgG1-Fc: Commonly used in therapeutic applications due to its favorable immunological characteristics.
Mouse IgG2a-Fc: Particularly effective in mediating opsonization and ADCC.
Mouse IgG2b-Fc: Known for its complement activation capabilities, primarily in certain mouse strains.
Mouse IgG2c-Fc: A less common subtype that can provide insights into immunology in mouse models.
Mouse IgG3-Fc: This subtype plays a unique role in immune responses and is often explored in allergy research.
Rat IgG Subtypes Rat IgG1-Fc: Commonly used in research and therapeutic contexts.
Rat IgG2a-Fc: Exhibits strong antigen recognition capabilities and has been documented for its role in immune response regulation.
Rat IgG2b-Fc: Helps in local inflammation but has traditionally been studied less.
Rat IgG2c-Fc: Although uncommon, it is important for understanding immunology in rat models.
Rabbit IgG-Fc A versatile option, widely employed in various experimental settings, providing valuable models for studying humoral immunity.
Canine IgG-Fc Increasingly used in veterinary medicine and comparative immunological research to better understand canine immune responses.

Key Features

The scFv-Fc fusion structure significantly enhances binding affinity, expression yield, and screening efficiency, making it more promising for applications in biotherapy. The advantages of the scFv-Fc fusion protein structure are as follows:

  • Improved Binding Affinity

The bivalent nature of the scFv-Fc fusion protein enhances binding to antigens compared to monovalent scFv. The Fc region stabilizes the interaction, mimicking the binding characteristics of full-length monoclonal antibodies (mAbs).

  • Higher Expression Yield

Using transient expression systems (such as HEK293 cells) can yield high quantities (10 mg to 100 mg or more per liter) in a short time frame (within a few days), making the production process of functional antibody fragments faster.

  • No Additional Purification Steps Required

The scFv-Fc fusion proteins are secreted into the culture supernatant, allowing for direct collection and analysis without extensive purification. This reduces the time and resources needed for validation.

  • Seamless Transfer Between Systems

The common SfiI restriction enzyme cleavage sites facilitate the cloning of scFv or VHH structures between phage display vectors and other expression systems, providing flexibility for experimental design.

  • Functional Mimicry of IgG

The Fc region in the fusion protein helps mimic the functions of IgG antibodies, including antibody-dependent cellular cytotoxicity (ADCC) and complement-dependent cytotoxicity (CDC), further enhancing the therapeutic potential of the scFv-Fc structure.

  • Robust Transfection Systems

The ability to conduct transient transfections in small volumes (such as 24-well and 48-well plates) facilitates high-throughput validation across multiple clones, improving the efficiency of the screening process.

Let Creative Biolabs be your partner in innovation and success, as we transform your ideas into reality with our exceptional scFv-Fc chimera products! Reach out to us today to explore how we can assist you in advancing your research and achieving your scientific aspirations. For inquiries or to place an order, please feel free to contact us.

Reference
  1. Girgis, Mark D , et al. "Targeting CEA in Pancreas Cancer Xenografts with a Mutated scFv-Fc Antibody Fragment." EJNMMI Research 1.1(2011):24. Distributed under Open Access license CC BY 2.0, without modification.

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