Rabbit Anti-VHH Antibody (CAT#: MOB-099CQ)

Lamtha, Thomanai, et al. "Generation of a nanobody against HER2 tyrosine kinase using phage display library screening for HER2-positive breast cancer therapy development." Protein Engineering, Design and Selection 34 (2021): gzab030. https://doi.org/10.1093/protein/gzab030

This study focuses on generating nanobodies targeting the HER2 tyrosine kinase domain, which is significant in HER2-positive breast cancer therapy. The research aimed to produce smaller, single-domain antibodies (nanobodies) to overcome limitations associated with conventional monoclonal antibodies, such as large size and resistance issues. Using phage display technology, the researchers identified three specific anti-HER2-TK nanobodies, with clone VHH17 showing the highest HER2 kinase inhibition activity. The study highlighted the potential of VHH17 as an effective therapeutic agent for treating HER2-positive breast cancer, demonstrating its ability to significantly decrease the viability of HER2-positive cancer cells.
Creative Biolabs played a crucial role in this research by providing essential reagents. Specifically, they supplied the rabbit anti-VHH antibody (Cat# MOB-099CQ) used in the ELISA binding affinity determination experiments. This reagent was vital for detecting the binding interactions between the selected nanobodies and HER2-TK, enabling the researchers to assess the specificity and efficacy of the nanobodies. The involvement of Creative Biolabs' products facilitated the detailed characterization and validation of the nanobody VHH17, which contributed significantly to the advancement of this therapeutic strategy for HER2-positive breast cancer.

Damman, Reinier, et al. "Development of in vitro-grown spheroids as a 3D tumor model system for solid-state NMR spectroscopy." Journal of Biomolecular NMR 74.8 (2020): 401-412. https://doi.org/10.1007/s10858-020-00328-8

This study explores the use of in vitro-grown spheroids as a three-dimensional tumor model system for solid-state NMR spectroscopy. Researchers investigated the hanging drop method to grow spheroids of uniform size and shape, suitable for studying solid tumors using solid-state NMR (ssNMR) spectroscopy. The findings revealed that these spheroids are stable under magic-angle-spinning conditions and exhibit significant metabolic differences compared to single cell preparations. Dynamic nuclear polarization (DNP)-supported ssNMR measurements demonstrated that even low concentrations of labeled nanobodies targeting EGFR (7D12) could be detected inside the spheroids. These results suggest that solid-state NMR can effectively examine proteins or other biomolecules within a 3D cellular microenvironment, offering potential applications in pharmacological research.
Creative Biolabs contributed significantly to this research by providing the rabbit-α-VHH antibody (Cat# MOB-099CQ) used for detecting 7D12. This antibody was crucial for the nanobody binding assay, which involved the detection of 7D12 binding to EGFR on A431 cells. The presence of this antibody enabled precise measurement of fluorescence intensity, helping to quantify the binding curve of 7D12. This contribution was essential for verifying the functionality and penetration of 7D12 into the spheroids, thereby facilitating detailed structural and functional studies of the proteins within the tumor model system.