Discovering New Solutions for Life Science

Nanobody reagents

Jotbody offers an extensive range of high-quality nanobodies from camelids (VHH) and sharks (vNAR). We use advanced technologies to produce the antigens and validate the nanobody through multiple applications and protein samples. These applications include precision medicine, molecular biology, imaging, analytical technique, and plate-based assay.

All our antibodies undergo extensive testing to ensure optimal specificity, sensitivity, and reproducibility, providing you with reliable results every time. Our nanobodies are a unique and powerful tool for detecting and quantifying a wide range of proteins.

If you’re looking for high-quality antibodies that meet the rigorous standards of scientific research, look no further than Jotbody. Browse through our catalog of thoroughly tested primary and secondary antibodies to find the perfect solution for your research needs.

Our exclusive shark platform

Conventional vertebrate immunoglobulins (Igs) are tetramers of two heavy and two light chains, in which the variable domains of each chain (VH and VL, respectively) assemble to form the antigen-binding site.

In 1993, Hamers-Casterman et al. discovered the presence of heavy-chain-only antibodies in the sera of camelid species. These heavy-chain-only antibodies are composed of two identical heavy chains, each comprising two constant domains (CH2 and CH3), a hinge region, and a variable VHH domain responsible for antigen recognition. Antigen binding by VHH domains is mediated by three complementarity-determining regions (CDRs): CDR1, CDR2, and CDR3.

Two years after the discovery of camelid heavy-chain-only antibodies, it was reported that sharks and other cartilaginous fish also produced heavy-chain-only antibodies called Ig new antigen receptors (IgNARs). IgNARs are composed of two identical heavy chains, each comprising five constant domains (CNAR1 – 5) and a variable vNAR domain responsible for antigen recognition. Antigen binding by vNAR domains is mediated by CDR1 and CDR3, as well as two small additional HV loops (HV2 and HV4). Additionally, vNARs belong to the Ig superfamily and accordingly, it has a ß-sandwich fold consisting of only eight strands.

Both VHHs and vNARs share several characteristics such as high stability and solubility, longer than average CDR3 loops, and the presence of non-canonical disulfide linkages sculpting the binding site.

While VHH domains have attracted great interest as biological drugs and proven to be successful in clinical trials, the engineering of vNAR domains for biomedical applications is at an early stage. Despite this, with a molecular mass of ~ 12 kDa, the vNAR domain is the smallest antibody-like antigen-binding domain in the animal kingdom known to date and it is abundantly clear that they present a singular molecular framework that can be exploited to develop reagents for scientific research, disease diagnosis, and/or therapeutic intervention:

• vNAR, evolutionarily distant from mammal VH domains, is best for detecting human antigens
• vNAR owns a peculiar paratope structure suitable for enriching the epitope diversity of antigens
• The high concentration of urea in the shark blood forges antibodies that are highly resistant at high pH, temperature, and organic solvent

The vNAR of IgNAR from several species of shark, including nurse shark and wobbegong shark, is a valid alternative to camelids-derived products. Unfortunately, the large size of shark species together with the impossibility of captivity, slow maturity, aggressive temper, and unpredictable behavior are the major issues hampering the success of vNAR-derived products.

To address these issues, we have established and validated a nanobody discovery platform using a local small shark species, the whitespotted bamboo shark, commonly kept as a home aquarium fish. This species is known for its docility and small size, allowing for large-scale husbandry and cost-effective production of superior nanobodies. In contrast, our competitors use larger shark species, such as nurse sharks, which are more challenging to work with. By utilizing the whitespotted bamboo shark, we have achieved a reduction in production costs.

At Jotbody, we are dedicated to the discovery of nanobodies. Our platform offers two distinct approaches to generating nanobodies: immunized and naïve libraries.

Here’s how each approach works:

Immunized Library Approach

Our immunized library approach involves generating a nanobody library from camelids or sharks that have been immunized with the target antigen. This approach is particularly useful when the antigen is well characterized and when a strong immune response is expected. With our immunization program in Australia, we optimize the protocol to ensure a robust and specific immune response. We then use high-throughput screening methods to identify nanobodies with the desired binding properties.

Naïve Library Approach

Our naïve library approach utilizes a diverse collection of nanobodies generated from an animal without prior exposure to the antigen of interest. This approach is particularly useful when the antigen is not well characterized or when the target is difficult to generate antibodies against. We use state-of-the-art screening techniques to identify nanobodies with high affinity and specificity toward the target antigen.

Our team of experts has extensive experience in immunized and naïve library approaches, and we work closely with our clients to determine which approach best suits their specific needs. We also offer customized solutions to meet the unique requirements of each project, including antibody engineering and optimization, as well as downstream applications such as imaging, diagnostics, and therapeutics.

Whether you are looking to generate nanobodies using immunized or naïve libraries or require customized solutions for your specific project, our team is here to help.