Recombinant Anti-cholera CTX VHH Single Domain Antibody (A9) (CAT#: PNBL-033)

Anti-cholera CTX VHH Single Domain Antibody is a recombinant protein produced in E. coli.


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  • Published Data
  • Datasheet
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  • COA

Figure 1 Specific binding of selected sdAb to cognate antigens.

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.

Goldman, E. R., Anderson, G. P., Liu, J. L., Delehanty, J. B., Sherwood, L. J., Osborn, L. E., ... & Hayhurst, A. (2006). Facile generation of heat-stable antiviral and antitoxin single domain antibodies from a semisynthetic llama library. Analytical chemistry, 78(24), 8245-8255.

Inhib

Figure 2 Ability of soluble toxins to inhibit binding of sdAb proteins to bead-immobilized toxins.

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.

Goldman, E. R., Anderson, G. P., Liu, J. L., Delehanty, J. B., Sherwood, L. J., Osborn, L. E., ... & Hayhurst, A. (2006). Facile generation of heat-stable antiviral and antitoxin single domain antibodies from a semisynthetic llama library. Analytical chemistry, 78(24), 8245-8255.

FuncS

Figure 3 Performance of sdAb as a reporter molecule in sandwich assays.

Figure 3 Performance of sdAb as a reporter molecule in sandwich assays.

Anti-CTX sdAb LCTA9 and rabbit anti-CTX as reporters in a sandwich assay. Goat anti-CTX was used as the capture.

Goldman, E. R., Anderson, G. P., Liu, J. L., Delehanty, J. B., Sherwood, L. J., Osborn, L. E., ... & Hayhurst, A. (2006). Facile generation of heat-stable antiviral and antitoxin single domain antibodies from a semisynthetic llama library. Analytical chemistry, 78(24), 8245-8255.


Specifications

  • Immunogen
  • Cholera toxin
  • Host Species
  • Llama
  • Derivation
  • Llama
  • Type
  • Llama VHH
  • Species Reactivity
  • Cholera
  • Clone
  • A9
  • Applications
  • Functional Assay, Inhibition

Product Property

  • Purity
  • >95% by SDS-PAGE and HPLC analysis
  • Storage
  • Store the antibody (in aliquots) at -20°C. Avoid repeated freezing and thawing of samples.

Applications

  • Application Notes
  • The antibody was validated for Functional Assay, Inhibition. For details, refer to Published Data.

Target

  • Alternative Names
  • Cholera toxin; CTX; choleragen; Ctx; CT

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.

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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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