Recombinant Mouse Antibody (N1G9) is capable of binding to NP (4-hydroxy-3-nitrophenyl)acetate).
Figure 1 NP-binding IgM Abs possess cross-reactivity to analogs of the original antigen.
(A) Binding of IgG mAbs to NP 26-BSA (open bars) and DNP 26-BSA (closed bars). IgG mAbs with different Ka values to NPs, namely, N1G9 (Ka = 5 × 10 5 M −1 ), B2 (Ka = 3.4 × 10 6 M −1 ), and E11 (Ka = 10 8 M −1 ), were used. (B) Binding of IgM mAbs to NP 26-BSA (open bars) and DNP 26-BSA (closed bars). Recombinant IgM mAbs whose V-D-J genes were from N1G9, B2 and E11 (N1G9-, B2-and E11-IgM, respectively) were used. (C) Binding of IgM mAbs secreted by hybridomas (1A350, 1A8, and 1A86, respectively) to NP 26-BSA (open bars) and DNP 26-BSA (closed bars). (D) Binding of IgM mAbs performed as in (B) in the presence of the indicated concentrations of NP-Cap. (E) Binding of IgM Abs to NP 2-, NP 26-, and DNP 26-BSA in serum collected from an individual mouse (n = 3) at 1 week after primary immunization (primary 1w) and secondary immunization (secondary 1w). The serum was diluted 200-fold, and binding was measured by ELISA. *p < 0.05, **p < 0.01, and ***p < 0.001. Error bars indicates the s.d. Data are representative of three independent experiments per experiment (A-D) or four independent experiments with one mouse per experiment (C).
Tashiro, Y., Murakami, A., Hara, Y., Shimizu, T., Kubo, M., Goitsuka, R., ... & Azuma, T. (2018). High-affinity IgM+ memory B cells are defective in differentiation into IgM antibody-secreting cells by re-stimulation with a T cell-dependent antigen. Scientific reports, 8.
Cao, Fengqiang, et al. "Inside-out assembly of viral antigens for the enhanced vaccination." Signal transduction and targeted therapy 8.1 (2023): 189. https://doi.org/10.1038/s41392-023-01414-7
This research introduces an innovative "inside-out assembly" approach for enhanced vaccination against enveloped RNA viruses. The study developed a multi-layered aluminum hydroxide-stabilized emulsion (MASE) that reverses the natural viral packaging strategy by placing nucleocapsid protein (NP) on the outside of droplets while trapping the receptor-binding domain (RBD) inside. This reversed delivery sequence triggers potent type I interferon-mediated immune responses in advance, creating an immune-potentiated environment that subsequently boosts dendritic cell activation and lymph node engagement. When tested with both H1N1 influenza and SARS-CoV-2 antigens, this inside-out strategy significantly increased antibody secretion, memory T cell engagement, and Th1-biased immune responses, effectively reducing viral loads after lethal challenge.
Creative Biolabs contributed anti-NP antibodies that were essential for verifying the structural design of the vaccine formulation. These antibodies were used to confirm the proper spatial arrangement of antigens in the multi-layered structure through confocal imaging. This enabled researchers to visually validate that NP was indeed displayed on the surface while other antigens remained entrapped inside the nanocage, confirming the successful implementation of the inside-out strategy that formed the foundation of this study's enhanced immune response.
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• Increased sensitivity
• Confirmed specificity
• High repeatability
• Excellent batch-to-batch consistency
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CAT | Product Name | Application | Type |
---|---|---|---|
PFBW-094 | Mouse Anti-NP Recombinant Antibody (clone N1G9); Fab Fragment | WB, ELISA | Mouse Fab |
HPAB-0619-YJ-F(E) | Mouse Anti-NP Recombinant Antibody (clone 9T13); Fab Fragment | ELISA | Mouse Fab |
HPAB-0620-YJ-F(E) | Mouse Anti-NP Recombinant Antibody (clone 6T3); Fab Fragment | ELISA | Mouse Fab |
FAMAB-0071JF-F(E) | Mouse Anti-NP Recombinant Antibody (clone 1B236); Fab Fragment | WB, ELISA, FuncS | Mouse Fab |
FAMAB-0072JF-F(E) | Mouse Anti-NP Recombinant Antibody (clone 1A8); Fab Fragment | WB, ELISA, FuncS | Mouse Fab |
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