Jotbody is dedicated to offering nanobody discovery CRO services and nanobody-based research reagents of outstanding quality to the global scientific community.

Jotbody (HK) Limited is a biotechnology company founded in 2020 by a group of passionate scientists and a globally recognized board of directors with well-documented experience in biotherapeutics development and entrepreneurship. With dual sites in Hong Kong and Shenzhen (China), Jotbody is part of the two well-established biotech ecosystems that provide modern co-working labs, spaces, and world-class equipment. We are positioned to rise to the needs of our customers for many years to come.

We envision a world where high-quality R&D can be broadly accessed and generate significant benefits for patients and healthcare payers worldwide and our goal is to speed up research and discovery by providing the highest quality nanobodies at an outstanding value and with excellent customer and technical support.

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.

Jotbody’s primary antibodies are designed to specifically target and bind to a wide range of protein targets.


Cat no. Product name Available sizes (µg) Reactivity Applications
JOT0001-1 anti-GFP VHH 50/100/250/1000/2000 Aequorea victoria ELISA, WB, IP
JOT0001-2 anti-GFP VHH, biotinylated 50/100/250/1000/2000 Aequorea victoria IF
JOT0001-3 anti-GFP VHH (Alexa Fluor® 647) 5/15/50 Aequorea victoria IF
JOT0001-4 anti-GFP VHH (Alexa Fluor® 488) 5/15/50 Aequorea victoria IF
JOT0001-5 anti-GFP VHH (Alexa Fluor® 568) 5/15/50 Aequorea victoria IF
JOT0002-5 anti-PD-L1 VHH 50/100/250/1000/2000 Human IHC, ELISA, WB, IF
JOT0002-5-1 anti-PD-L1 VHH (Alexa Fluor® 647) 5/15/50 Human IF
JOT0002-5-2 anti-PD-L1 VHH (Alexa Fluor® 488) 5/15/50 Human IF
JOT0002-5-3 anti-PD-L1 VHH (Alexa Fluor® 568) 5/15/50 Human IF
JOT0005-1 anti-hTNFR1 VHH 50/100/250/1000/2000 Human IHC, ELISA, WB, IF
JOT0007-1 anti-SARS-CoV-2 spike RBD VHH 50/100/250/1000/2000 SARS-CoV-2 ELISA
JOT0008-1 anti-Her2 VHH 50/100/250/1000/2000 Human IHC, IF
JOT0009-1 anti-EGFR VHH 50/100/250/1000/2000 Human IHC, ELISA, IF
JOT0052-1 anti-GFAP VHH 50/100/250/1000/2000 Human IHC, WB
JOT0076-1 anti-mCherry VHH 50/100/250/1000/2000 Discosoma sp. ELISA, WB, IF
JOT0121-1 anti-PCSK9 VHH 50/100/250/1000/2000 Human IHC, IF
JOT0200-1 Anti-GFP vNar 25/50/100/500/1000 Aequorea victoria ELISA, WB
JOT0200-2 Biparatopic Anti-GFP vNar 25/50/100/500/1000 Aequorea victoria ELISA, WB
JOT00058 anti-Vim VHH 50/100/250/1000/2000 Human ELISA
JOT0112-1 anti-P53 VHH 50/100/250/1000/2000 Human ELISA
JOT0125-1 anti-PCSK9 VHH antibody 50/100/250/1000/2000 Human ELISA
JOT0114 anti-VEGFR2 VHH antibody 50/100/250/1000/2000 Human ELISA

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.