Polyclonal Single Domain Antibody (SdAb) Generation Service

Camelid IgG Introduction Strategies Antigen-Specific Polyclonal Camelid Antibody Polyclonal Heavy Chain Only Antibody Polyclonal VHH Case Study Published Data FAQ Resources

Creative Biolabs has long-term devoted to the development and application of VHHs. Based on our advanced platforms and extensive experience, our scientists are confident in offering suitable polyclonal VHH generation services to meet your specific requirements.

Camelid IgG Introduction

Different from any other known antibodies, the camelid IgG antibodies consist of three subclasses. Therefore, IgG1 is composed of conventional antibodies, while IgG2 and IgG3 lack light chains and consist of dimers of short heavy chains characterized by a normal Fc region without a CH1 domain. Compared with conventional antibodies, IgG2 and IgG3 antibodies (also known as heavy chain only antibodies), as well as their antigen-binding domain (VHH), present great advantages due to their small size. According to the different species, the IgG isotype can be further divided into:

Llama/Alpaca: IgG1a, IgG1b, IgG2b, IgG2c, IgG3.

Camel: IgG1a, IgG1b, IgG2a, IgG2c, IgG3.

Comprehensive Strategies for Camelid Polyclonal Antibody Generation

Taking advantage of our deep understanding of camelid antibodies, Creative Biolabs can offer three elaborate stages to satisfy your various demands for camelid polyclonal antibody generation, which can let you obtain the real polyclonal single domain antibody.

Starting with a properly designed antigen and immunization strategy, the favorable immune response is expected to be triggered in 70 days. The blood will be collected after the confirmation of titration ELISA for further purification processes. Our scientists can tailor three strategies according to the different demands of final deliverables.

Generation of Antigen-Specific Polyclonal Camelid Antibody

The antigen-specific affinity purification will be employed as the main process, in which the antigen of interest will be coated to the column and then we will perform the purification for a few rounds. For polyclonal antibody purification, it is essential to avoid the co-purification of non-specific immunoglobulins. This approach can contribute to obtaining almost all antibodies (full-length format with different isotypes) that can recognize the antigen. It is also a foundation for the other two strategies.

Generation of Polyclonal Heavy Chain Only Antibody

The classic Protein A and Protein G columns will be employed in this strategy. With this subsequent purification process, our scientists can properly separate the isotype of obtained antigen-specific pAbs and also eliminate some unwanted binders. This approach can meet your demands for generating heavy chain only pAbs or pAbs with specific IgG isotypes (IgG1, IgG2, or IgG3).

Generation of Polyclonal Single Domain Antibody

For the demands of purified polyclonal single domain antibodies (VHH only), our scientists can also achieve such purpose by integrating a properly designed digestion strategy. Going through a series of digestion, washing, and elution steps, polyclonal single domain antibodies can be finally obtained from either IgG2 or IgG3.

Creative Biolabs is a leading service provider that focuses on VHH generation and development. We have accomplished a series of camelid polyclonal antibody generation projects for our customers all over the world. If you are interested in our service, please do not hesitate to contact us for more details.

Published Data

Polyclonal HCAbs and Proteins Derived from Camels Exhibit Considerable Anti-HCV Effects

Fig. 1 Dilution-based Evaluation of HCV Peptide Binding Affinity in Camel and Human IgGs.Fig. 1 Dilution-based Evaluation of HCV Peptide Binding Affinity in Camel and Human IgGs.1,2

The study sought to investigate the antiviral activity of proteins extracted from camel milk against the Hepatitis C Virus (HCV). The researchers evaluated the anti-HCV effects of purified camel naïve polyclonal IgGs (including Heavy-chain antibodies, HCAbs), α-lactalbumin, lactoferrin, and casein derived from camel milk using peripheral blood mononuclear cells (PBMCs), and Huh7.5 cell lines. This experiment displayed in Fig.1 was designed to test the reactivity of camel and human immunoglobulin G (IgG) against HCV peptides. It was revealed that camel IgGs and lactoferrin demonstrated a notable capacity to recognize HCV peptides and effectively inhibited HCV entry into cells, whereas human IgGs, α-lactalbumin, and casein exhibited little reactivity and did not demonstrate inhibitory effects, indicating the specific recognition ability of camel IgGs for HCV. This article suggests that specific proteins derived from camel milk like polyclonal HCAbs may serve as promising candidates for the development of novel anti-HCV therapies.

References

  1. El-Fakharany, Esmail M., et al. "Anti-infectivity of camel polyclonal antibodies against hepatitis C virus in Huh7. 5 hepatoma." Virology journal 9 (2012): 1-9.
  2. under Open Access license CC BY 2.0, without modification.

FAQ

1. What are polyclonal VHHs?
Polyclonal VHHs are VHH mixtures that identify numerous epitopes on the same antigen or separate antigens, whereas monoclonal VHHs are produced from a single B-cell clone and recognize just one epitope. Polyclonal VHH antibodies are produced by immunizing camelids, such as llamas or alpacas, providing a broader and more effective identification of the target, which makes them helpful in a variety of biotechnological and therapeutic applications.
2. What are the benefits of using polyclonal VHHs over monoclonal VHHs?
Polyclonal VHHs identify numerous epitopes on an antigen with strong and comprehensive binding, while monoclonal VHHs are derived from a single B-cell clone and target just a single epitope. Multiple epitope identification can be useful for polyclonal VHHs in situations requiring high antigen variability or more thorough epitope coverage. However, monoclonal VHHs are less significant for use in complex biological circumstances than polyclonal VHHs since they only bind to a single epitope.
3. What are the typical applications of polyclonal VHHs?
Owing to the multiple capacities to bind various epitopes with high affinity, polyclonal VHHs are widely used in several applications like diagnostic tests, therapies, and research. For laboratory use and diagnostic applications, they are effectively involved in immunohistochemistry, ELISA, Western blotting immunoprecipitation, and immunofluorescence studies to identify infections, biomarkers, and other relevant antigens in diagnosis and research settings. They are used in therapeutics for toxin neutralization, medication delivery, and cancer cell targeting.
4. What roles do polyclonal VHHs play in therapeutic applications?
Polyclonal VHHs help with therapeutic treatments by neutralizing pathogens across a broad spectrum and targeting several antigens at the same time. They are utilized to neutralize bacterial toxins, target cancer cells, combat viral infections, and function as medication transporters, leveraging their distinct features for greater therapeutic efficacy. They can be modified into multivalent formats to increase therapeutic efficacy or paired with drugs and toxins for targeted delivery, making them useful in the treatment of infections, cancer, and autoimmune illnesses.
5. What future advancements are expected in the field of polyclonal VHHs?
Future advancements in the field of polyclonal VHHs may include improved immunization and screening techniques, more sophisticated methods for analyzing and enhancing VHH diversity, and new applications in diagnostic and therapeutic areas. Innovations in synthetic biology and protein engineering could lead to the development of VHHs with improved properties and multifunctional capabilities.

Resources

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