Nanobodies, derived from camelids like alpacas and camels, are single-domain antibodies consisting of just the heavy-chain variable domain (VHH). At about one-tenth the size of traditional antibodies, they penetrate tissues more effectively and remain stable in tough conditions, making them ideal for cutting-edge scientific research.
Key Takeaways: Nanobodies are small, stable, and versatile tools for research, offering high specificity and cost-effective production for applications in oncology, immunology, and imaging.
Since the late 20th century, monoclonal antibodies have transformed oncology research, with widespread clinical adoption over the past decades. Yet, their large size, complex structure, and potential for immune reactions can limit their effectiveness, especially for reaching hidden molecular targets.
Discover how nanobodies compare to conventional antibodies, offering unique advantages for scientific research.
Feature | Conventional Antibodies | Nanobodies |
---|---|---|
Structure | 2 heavy chains + 2 light chains (Y-shaped) | Single heavy-chain variable domain (VHH) |
Molecular Weight | ~150 kDa | 12–15 kDa (10x smaller) |
Stability | Susceptible to high temperatures or extreme pH | Exhibiting higher thermal and pH tolerance than conventional antibodies [5] |
Penetration | Limited penetration into dense tissues | Improved tissue penetration, with studies demonstrating uptake in brain tissue via receptor-mediated mechanisms [3] |
Production | Requires mammalian cell culture, high cost | Produced in E. coli, often enabling lower production costs compared with mammalian expression [5] |
Thanks to their small size, high specificity, and robust stability, nanobodies are revolutionizing research in fields like oncology and immunology. These versatile tools are designed for scientific applications only. For Research Use Only (RUO).
Learn how nanobodies are advancing scientific discovery across multiple research fields.
Nanobodies are unlocking new possibilities in immuno-oncology by binding to immune checkpoints like PD-1/PD-L1 or CTLA-4 in preclinical studies. For Research Use Only (RUO).
Evidence: A bispecific VHH construct binding PD-1 and CTLA-4 shows strong potential in preclinical models [2].
The compact size of nanobodies enables high-resolution imaging in techniques like PET, SPECT, and optical imaging for tumor visualization research in preclinical models.
Evidence: Anti-PD-L1 nanobodies have been tested in preclinical imaging studies for cancer research [4].
Nanobodies are being explored for their ability to bind immune markers or cytokines in autoimmune disease models.
Evidence: A nanobody targeting IL-6R has shown promise in preclinical studies for rheumatoid arthritis research [6].
Nanobodies offer exciting potential for studying viral and bacterial proteins in preclinical infectious disease research.
Evidence: Anti-SARS-CoV-2 nanobodies targeting the spike protein demonstrated strong binding in preclinical models [7].
Explore the milestones achieved in nanobody research over the past decade.
Single-domain antibody–based approaches have progressed in preclinical and translational research literature, exploring their potential in immunology and imaging applications. This article is for scientific discussion only and does not promote prescription medicines. Check out the references below for more details.
Discover how abinScience supports global research with cutting-edge nanobody tools.
At abinScience, we’re passionate about empowering researchers with top-tier nanobody tools. Our extensive library fuels discoveries in virology, immunology, and more, offering reliable solutions for groundbreaking science.
Browse our nanobody products, tailored for research in oncology, infectious diseases, and beyond. All products are for Research Use Only (RUO).
Catalog No. | Product Name |
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HY286013 | Anti-Human CD340/ERBB2/HER2 Nanobody (SAA0836) |
HF004013 | Anti-Human EGFR/ERBB1/HER1 Nanobody (SAA0792) |
HY546023 | Anti-Human CD66e/CEA/CEACAM5 Nanobody (SAA0837) |
HY196023 | Anti-Human MET/c-Met/HGFR Nanobody (SAA1308) |
HY036013 | Anti-Human CD71/TFRC Nanobody (SAA1205) |
HY464013 | Anti-Human CD49e/ITGA5 Nanobody (SAA1304) |
HC546013 | Anti-Human CDH17/Cadherin-17 Nanobody (SAA0804) |
HY389013 | Anti-Human KRT19/CK19 Nanobody (SAA1367) |
Catalog No. | Product Name |
---|---|
JN074013 | Anti-Vibrio cholerae ctxB/Cholera Toxin Subunit B Nanobody (A9) |
JN989013 | Anti-P. gingivalis PorM Nanobody (Nb01) |
JN847013 | Anti-P. gingivalis fimA/Fimbrillin Antibody (123-123-10) (Antibody) |
JN080013 | Anti-Vibrio cholerae higB-2 Nanobody (SAA0850) |
Catalog No. | Product Name |
---|---|
HF875013 | Anti-Human CRP Nanobody (SAA1358) |
HY328013 | Anti-Human IL6 Nanobody (SAA0798) |
HY583013 | Anti-Human CD126/IL6R/IL-6RA Nanobody (SAA1278) |
HY185013 | Anti-Human SERPINE1/PAI-1 Nanobody (SAA0793) |
HY312013 | Anti-Human CCL3/MIP-1-alpha Nanobody (SAA1270) |
Catalog No. | Product Name |
---|---|
MB613013 | Anti-Mouse CD223/LAG3 Nanobody (SAA0767) |
MT188013 | Anti-Mouse CD282/TLR2 Nanobody (SAA0821) |
HB259013 | Anti-Human CXCR7/ACKR3 Nanobody (SAA0795) |
HB871013 | Anti-Human MC4R Nanobody (SAA0796) |
HX947013 | Anti-Human PTH1R Nanobody (SAA0797) |
HY411013 | Anti-Human Albumin/HSA Nanobody (SAA0807) |
HW680013 | Anti-Human MAGEB1 Nanobody (SAA0834) |
HY313013 | Anti-Human CFTR Nanobody (SAA0794) |
HY411033 | Anti-Human ALB Nanobody (SAA1019) |
HY348013 | Anti-Human CAT/Catalase Nanobody (SAA1202) |
HY392013 | Anti-Human CD230/PRNP Nanobody (SAA0883) |
HY057013 | Anti-Human CD3E Nanobody (SAA1330) |
HY353013 | Anti-Human CD221/IGF1R Nanobody (SAA1314) |
HY068013 | Anti-Human CHRM2 Nanobody (SAA1214) |
HY550053 | Anti-Human VIM/Vimentin Nanobody (SAA1226) |
HY302013 | Anti-Human CD7 Nanobody (SAA1260) |
HY484013 | Anti-Human FURIN Nanobody (SAA1180) |
HY342013 | Anti-Human C4b Nanobody (SAA0908) |
HY342023 | Anti-Human C4b Nanobody (SAA0907) |
Connect with us to explore how our nanobody tools can support your research.
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Explore the scientific foundation behind nanobody research.
[1] Ruiz-López, E., et al. (2022). Nanobodies targeting ABCC3 for immunotargeted applications in glioblastoma research. Scientific Reports, 12, 22613.
[2] Zeng, X., et al. (2024). Binding properties of a bispecific nanobody targeting PD-1 and CTLA-4 in preclinical studies. Oncogene, 43, 1234–1245.
[3] Zheng, F., Pang, Y., Li, L., et al. (2022). Applications of nanobodies in brain disease research. Frontiers in Immunology, 13, 978513.
[4] Yang, E. Y., et al. (2020). Nanobody probes targeting immune checkpoints for immuno-oncology and imaging research. Frontiers in Oncology, 10, 1182.
[5] Biochempeg. (2023). Nanobodies - Current Status and Prospects.
[6] Phase II study of an anti–IL-6 receptor nanobody in rheumatoid arthritis research. ClinicalTrials.gov, NCT02309359.
[7] Huo, J., et al. (2020). Nanobodies targeting SARS-CoV-2 spike RBD and their binding in preclinical studies. Nature Structural & Molecular Biology, 27, 846–854.
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