This product is a recombinant Alpaca antibody that can recognize RTA. V1C7 binds epitope(s) associated with weaker toxin neutralizing activity. V1C7's interface with RTA is limited to α-helix D (residues 141–142, 145–146, 149, and 153) and α-helix E (residue 163), along with several additional interactions with loops e-d (residues 65–68), C-D (residue 138), D-E (residues 157–160), and F-G (residues 195, 197).
Figure 1 Neutralization capacity of V1C7 point mutants.
The two VHH point mutants at position 29 were compared against their parental VHHs in a Vero cell cytotoxicity assay. Ricin toxin-neutralizing activities associated with V1C7 versus V1C7 G29R.
Figure 2 Relative affinities of V1C7 (circles), V2B9 (squares), V2E8 (triangles), and V5C1 (inverted triangles) for ricin toxin, as determined by ELISA in which ricin was captured onto plastic surface by ASF.
Bazzoli, A., Vance, D. J., Rudolph, M. J., Rong, Y., Angalakurthi, S. K., Toth IV, R. T., ... & Mantis, N. J. (2017). Using homology modeling to interrogate binding affinity in neutralization of ricin toxin by a family of single domain antibodies. Proteins: Structure, Function, and Bioinformatics, 85(11), 1994-2008.
Figure 3 Relationships between VHH binding affinities and toxin-neutralizing activities.
Each color represents a family; each dot represents an individual VHH within that family. The downward slope of the lines suggests a relationship between KD and TNA within a clonal family.
Vance, D. J., Tremblay, J. M., Rong, Y., Angalakurthi, S. K., Volkin, D. B., Middaugh, C. R., ... & Mantis, N. J. (2017). High-resolution epitope positioning of a large collection of neutralizing and nonneutralizing single-domain antibodies on the enzymatic and binding subunits of ricin toxin. Clin. Vaccine Immunol., 24(12), e00236-17.
Figure 4 4 Validation of cross-competition ELISA as a strategy for epitope localization on RTA.
V1C7 were subjected to competition ELISAs with a panel of RTA-specific MAbs representing neutralizing clusters I to IV.
Vance, D. J., Tremblay, J. M., Rong, Y., Angalakurthi, S. K., Volkin, D. B., Middaugh, C. R., ... & Mantis, N. J. (2017). High-resolution epitope positioning of a large collection of neutralizing and nonneutralizing single-domain antibodies on the enzymatic and binding subunits of ricin toxin. Clin. Vaccine Immunol., 24(12), e00236-17.
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.
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CAT | Product Name | Application | Type |
---|---|---|---|
NABL-029 | Recombinant Anti-RTA VHH Single Domain Antibody | WB, IHC, FC, FuncS | Llama VHH |
PABC-567 | Recombinant Alpaca Anti-RTA Single Domain Antibody (PABC-567) | ELISA, FC, Neut | Alpaca VHH |
PABC-568 | Recombinant Llama Anti-RTA Single Domain Antibody (PABC-568) | ELISA, WB, Neut | Llama VHH |
PABC-570 | Recombinant Alpaca Anti-RTA Single Domain Antibody (PABC-570) | ELISA, FC, Neut | Alpaca VHH |
PABC-571 | Recombinant Alpaca Anti-RTA Single Domain Antibody (PABC-571) | ELISA, Neut | Alpaca VHH |
CAT | Product Name | Application | Type |
---|---|---|---|
PABJ-0018 | Camelid Anti-RTA Recombinant Antibody (clone V6A7) | ELISA, Inhib | Camelid VHH |
PABJ-0019 | Camelid Anti-RTA Recombinant Antibody (clone V6H8) | ELISA, Inhib | Camelid VHH |
PABJ-0020 | Camelid Anti-RTA Recombinant Antibody (clone V6D4) | ELISA, Inhib (weak) | Camelid VHH |
PABJ-0021 | Camelid Anti-RTA Recombinant Antibody (clone V2G10) | ELISA, Inhib | Camelid VHH |
PABJ-0022 | Camelid Anti-RTA Recombinant Antibody (clone V6A6) | ELISA, Inhib (weak) | Camelid VHH |
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For Research Use Only. Not For Clinical Use.
For research use only. Not intended for any clinical use. No products from Creative Biolabs may be resold, modified for resale or used to manufacture commercial products without prior written approval from Creative Biolabs.
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