Anti-Influenza A Virus H1N1 Hemagglutinin HA1 subunit Recombinant Antibody (MRO-240LC-VHH) (CAT#: MRO-240LC-VHH)
This product is a recombinant alpaca anti-influenza A virus H1N1 single domain antibody. R1a-G6 specifically binds to hemagglutinin HA1 subunit and can be potentially usd in the treatment of influenza virus infection.
We specialize in custom recombinant antibody production, offering seamless execution from provided sequences to high-quality antibody deliverables, ensuring optimal yield and purity.
Figure 1 Display of hemagglutinin on yeast and evaluation of binding of single domain antibodies.
FACS plots of seven HA specific single domain antibodies (sdAbs) R1a-F5, R1a-G6, R2b-E8, R2b-D9, R1a-A5, R1a-B6, R2a-G8 binding to yeast displayed HA0. Negative controls sdAb R1a-G2 and no sdAb control are shown. The vertical arrow indicates absence of binding.
Gaiotto, T., & Hufton, S. E. (2016). Cross-neutralising sdAbs bind to a conserved pocket in the hemagglutinin stem region identified using yeast display and deep mutational scanning. PloS one, 11(10), e0164296.
Figure 2 Specificity of single domain antibodies to different influenza antigen reference reagents.
ELISA comparing binding of purified VHH antibodies at 30 mg/ml against H1N1, seasonal H1N1 and H5N1.
Hufton, S. E., Risley, P., Ball, C. R., Major, D., Engelhardt, O. G., & Poole, S. (2014). The breadth of cross sub-type neutralisation activity of a single domain antibody to influenza hemagglutinin can be increased by antibody valency. PLoS One, 9(8), e103294.
Figure 3 Antibody affinity on recombinant HA by surface plasmon resonance.
Affinity on recombinant H1-HA, H1N1.
Hufton, S. E., Risley, P., Ball, C. R., Major, D., Engelhardt, O. G., & Poole, S. (2014). The breadth of cross sub-type neutralisation activity of a single domain antibody to influenza hemagglutinin can be increased by antibody valency. PLoS One, 9(8), e103294.
Figure 4 Characterisation of antibody epitopes.
ELISA showing reactivity of purified antibodies at 30 mg/ml to HA antigen standard H1N1 either treated with low pH or neutral pH.
Hufton, S. E., Risley, P., Ball, C. R., Major, D., Engelhardt, O. G., & Poole, S. (2014). The breadth of cross sub-type neutralisation activity of a single domain antibody to influenza hemagglutinin can be increased by antibody valency. PLoS One, 9(8), e103294.
Figure 5 Characterisation of antibody epitopes.
ELISA showing binding of phage displayed HA gene fragments to purified sdAbs.
Hufton, S. E., Risley, P., Ball, C. R., Major, D., Engelhardt, O. G., & Poole, S. (2014). The breadth of cross sub-type neutralisation activity of a single domain antibody to influenza hemagglutinin can be increased by antibody valency. PLoS One, 9(8), e103294.
Specifications
- Host Species
- Alpaca
- Derivation
- Phage display library
- Type
- Single domain antibody
- Specificity
- Influenza A virus H1N1
- Clone
- MRO-240LC-VHH
- Applications
- ELISA, SPR, FC
- Related Disease
- Influenza virus infections
Applications
- Application Notes
- The antibody was validated for ELISA, Surface plasmon resonance, Flow Cytometry. For details, refer to Published Data.
Target
Product Notes
This is a product of Creative Biolabs' Hi-Affi™ recombinant antibody portfolio, which has several benefits including:
• Increased sensitivity
• Confirmed specificity
• High repeatability
• Excellent batch-to-batch consistency
• Sustainable supply
• Animal-free production
See more details about Hi-Affi™ recombinant antibody benefits.
Downloads
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MRO-230LC-VHH | Anti-Influenza A Virus H1N1 Hemagglutinin HA1 subunit Recombinant Antibody (MRO-230LC-VHH) | ELISA, SPR | Single domain antibody |
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For Research Use Only. Not For Clinical Use.
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