Anti-cholera CTX VHH Single Domain Antibody is a recombinant protein produced in E. coli.
Figure 1 Specific binding of selected sdAb to cognate antigens.
Binding of CTX selected sdAb as determined by Luminex100. Curves are shown for binding of all anti-CTX sdAbs on CTX-coated beads, compiled from separate experiments. Binding to SEB- and ricin-coated control beads was negligible except for LCTC3. The ricin control is shown for both LCTC3 and LCTA9; the latter is representative of the other sdAb. Binding of LCTC3 to SEB-coated beads was essentially the same as on the ricin-coated beads and is not shown. Binding of LCTA9 to ricincoated beads was identical to the binding on SEB-coated beads and is representative of the traces found on control beads for LCTG3, LCTC11, and LCTG4. The majority of the curves on control beads have been omitted for clarity.
Figure 2 Ability of soluble toxins to inhibit binding of sdAb proteins to bead-immobilized toxins.
Increasing amounts of CTX were added to the toxin-coated bead set mixture prior to addition of the sdAb. After 15 min incubation to approach equilibrium, Ni-SA-PE (10 mg/L) was added to generate the signal. Then after an additional 30 min, inhibition of binding of sdAb to toxin-coated beads were assessed.
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