Antibodies are essential tools in modern medicine and research, but not all antibodies are the same. VHH antibodies, also known as single-domain antibodies or nanobodies, are a type of antibody that offers several advantages over conventional antibodies.
VHH antibodies are derived from the immune system of camelids, which produce antibodies that are much smaller than those produced by humans or mice. VHH antibodies consist of a single domain, or variable region, that is capable of binding to specific antigens. This makes them ideal for a wide range of applications, including diagnostic tests, therapeutics, and research tools.
One key advantage of VHH antibodies is their small size. This allows them to penetrate tissues more effectively than larger antibodies, making them useful for targeting diseases that are difficult to reach with conventional therapies. Additionally, VHH antibodies are highly stable and can withstand harsh conditions, such as high temperatures or acidic environments, which makes them useful for a range of diagnostic and therapeutic applications.
At Biointron, we specialize in the production of high-quality recombinant VHH antibodies for research and diagnostic purposes. Our team of experts uses state-of-the-art technologies to generate VHH antibodies that are highly specific and sensitive to their target antigens. Whether you need custom VHH antibody production or off-the-shelf options, we have the expertise to deliver the right solution for your needs.
To learn more about our VHH antibody services, visit our website or contact us today.
Antibodies are versatile molecules that perform a range of effector functions, many of which engage different arms of the immune system. Their modes of action extend beyond simple antigen binding, enabling the activation of various immune mechanisms that lead to pathogen neutralization and clearance. These functions include blocking molecular interactions, activating the complement system, and linking the humoral immune response to cellular immune responses via Fc receptor engagement.
In today’s competitive biotech landscape, intellectual property (IP) protection has become an essential pillar in fostering innovation and collaboration across drug discovery and development. By offering clear IP terms and no royalty fees,pharmaceutical companies and research institutes
In addition to isotypes and subtypes, antibodies exhibit genetic variation known as allotypes, which are polymorphic epitopes on immunoglobulins. These allotypic differences arise from allelic variations in immunoglobulin genes, causing certain antibody subtypes to differ between individuals or ethnic groups. The presence of these polymorphic forms can influence immune responses, particularly when an individual is exposed to a non-self allotype, potentially triggering an anti-allotype immune reaction.
In mammals, antibodies are classified into five major isotypes: IgA, IgD, IgE, IgG, and IgM. Each isotype is defined by the heavy chain it contains: alpha (IgA), delta (IgD), epsilon (IgE), gamma (IgG), or mu (IgM). These structural differences in the heavy chains determine the antibody's function, tissue localization, and role in the immune response. Furthermore, antibody light chains fall into two classes—kappa and lambda—with kappa being more common, though both exhibit similar functions despite differences in sequence.
