Anti-P. falciparum AMA1 Recombinant Antibody (14M-15) (CAT#: MRO-194CT)

Recombinant shark antibody specifically binds to Plasmodium falciparum AMA1, expressed in Chinese Hamster Ovary cells(CHO).


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ELISA

Figure 1 V(NAR) Library Design

Figure 1 V(NAR) Library Design

ELISA testing of affinity-purified VNAR proteins (14I-1, 14M-15, 12A-9) for cross-strain AMA1 binding. Data are represented as the mean ± standard error of triplicate experiments.

Henderson, K. A., Streltsov, V. A., Coley, A. M., Dolezal, O., Hudson, P. J., Batchelor, A. H., ... & Foley, M. (2007). Structure of an IgNAR-AMA1 complex: targeting a conserved hydrophobic cleft broadens malarial strain recognition. Structure, 15(11), 1452-1466.

SPR

Figure 2 Affinity maturation of V(NAR) 12Y-2 by error-prone PCR.

Figure 2 Affinity maturation of V(NAR) 12Y-2 by error-prone PCR.

BIAcore sensorgrams comparing the binding of identical concentrations of the parental and mutant proteins to immobilized AMA1 at a constant flow rate of 5 ul/min with an injection volume of 35 ul.

Nuttall, S. D., Humberstone, K. S., Krishnan, U. V., Carmichael, J. A., Doughty, L., Hattarki, M., ... & Irving, R. A. (2004). Selection and affinity maturation of IgNAR variable domains targeting Plasmodium falciparum AMA1. PROTEINS: Structure, Function, and Bioinformatics, 55(1), 187-197.

SPR

Figure 3 The 12Y-2 triple-mutant shows parental affinity for AMA1.

Figure 3 The 12Y-2 triple-mutant shows parental affinity for AMA1.

BIAcore sensorgrams comparing the binding of identical concentrations of the parental (12Y-2), single mutant (14M-15), and triple mutant proteins to immobilized AMA1.

Nuttall, S. D., Humberstone, K. S., Krishnan, U. V., Carmichael, J. A., Doughty, L., Hattarki, M., ... & Irving, R. A. (2004). Selection and affinity maturation of IgNAR variable domains targeting Plasmodium falciparum AMA1. PROTEINS: Structure, Function, and Bioinformatics, 55(1), 187-197.

SPR

Figure 4 Tandem V(NAR)s in a single chain format

Figure 4 Tandem V(NAR)s in a single chain format

BIAcore sensorgrams comparing binding of proteins 12Y-2, 14M-15, and 15Q-1 to immobilised AMA1 protein.

Simmons, D. P., Abregu, F. A., Krishnan, U. V., Proll, D. F., Streltsov, V. A., Doughty, L., ... & Nuttall, S. D. (2006). Dimerisation strategies for shark IgNAR single domain antibody fragments. Journal of immunological methods, 315(1-2), 171-184.

ELISA

Figure 5 ELISA analysis of 12 14M-15 variants (12Y-2 with Pro90Leu) for binding to AMA1 and a control negative antigen.

Figure 5 ELISA analysis of 12 14M-15 variants (12Y-2 with Pro90Leu) for binding to AMA1 and a control negative antigen.

ELISA analysis of 12 14M-15 variants (12Y-2 with Pro90Leu) for binding to AMA1 and a control negative antigen. Comparative expression levels are also shown. The CDR1 analogous region (loop region 4) has been shuffled in the variants.

ELISA

Figure 6 ELISA analysis of 40 12Y-2 variants binding to AMA-1 and a control negative antigen.

Figure 6 ELISA analysis of 40 12Y-2 variants binding to AMA-1 and a control negative antigen.

ELISA analysis of 40 12Y-2 variants binding to AMA-1 and a control negative antigen.

SPR

Figure 7 Biosensor traces of purified 12Y-2 variant proteins 14M-15 and 22A-2. 22A-2 shows 2-fold enhanced affinity over 14M-15 (20-fold better affinity than 12Y-2).

Figure 7 Biosensor traces of purified 12Y-2 variant proteins 14M-15 and 22A-2. 22A-2 shows 2-fold enhanced affinity over 14M-15 (20-fold better affinity than 12Y-2).

Biosensor traces of purified 12Y-2 variant proteins 14M-15 and 22A-2. 22A-2 shows 2-fold enhanced affinity over 14M-15 (20-fold better affinity than 12Y-2).

ELISA

Figure 8 V(NAR) 14M-15 targets a variable region of P. falciparum AMA1.

Figure 8 V(NAR) 14M-15 targets a variable region of P. falciparum AMA1.

ELISA comparison of V(NAR) protein 14M-15 binding to AMA1 derived from P. falciparum strains W2MEF, HB3, D10, and 3D7. Binding to reduced and alkylated 3D7 (R&A) is also shown.

Nuttall, S. D., Humberstone, K. S., Krishnan, U. V., Carmichael, J. A., Doughty, L., Hattarki, M., ... & Irving, R. A. (2004). Selection and affinity maturation of IgNAR variable domains targeting Plasmodium falciparum AMA1. PROTEINS: Structure, Function, and Bioinformatics, 55(1), 187-197.

Inhib

Figure 9 Parasite Invasion Inhibition

Figure 9 Parasite Invasion Inhibition

Recombinant V(NAR) domains inhibit invasion of erythrocytes by P. falciparum 3D7 parasites. Data are represented as the mean ± standard error of quadruplicate experiments.

Henderson, K. A., Streltsov, V. A., Coley, A. M., Dolezal, O., Hudson, P. J., Batchelor, A. H., ... & Foley, M. (2007). Structure of an IgNAR-AMA1 complex: targeting a conserved hydrophobic cleft broadens malarial strain recognition. Structure, 15(11), 1452-1466.

Inhib

Figure 10 Parasite Invasion Inhibition

Figure 10 Parasite Invasion Inhibition

Recombinant V(NAR) domains inhibit invasion of erythrocytes by P. falciparum 3D7 parasites. Data are represented as the mean ± standard error of quadruplicate experiments,except for P. falciparum W2mef parasites.

Henderson, K. A., Streltsov, V. A., Coley, A. M., Dolezal, O., Hudson, P. J., Batchelor, A. H., ... & Foley, M. (2007). Structure of an IgNAR-AMA1 complex: targeting a conserved hydrophobic cleft broadens malarial strain recognition. Structure, 15(11), 1452-1466.

ELISA

Figure 11 V(NAR) Library Design

Figure 11 V(NAR) Library Design

ELISA testing of affinity-purified V(NAR) proteins (14I-1, 14M-15, 12A-9) for cross-strain AMA1 binding.

Henderson, K. A., Streltsov, V. A., Coley, A. M., Dolezal, O., Hudson, P. J., Batchelor, A. H., ... & Foley, M. (2007). Structure of an IgNAR-AMA1 complex: targeting a conserved hydrophobic cleft broadens malarial strain recognition. Structure, 15(11), 1452-1466.


Specifications

  • Host Species
  • Shark
  • Species Reactivity
  • P. falciparum
  • Clone
  • 14M-15
  • Applications
  • ELISA, SPR, Inhib

Applications

  • Application Notes
  • The antibody was validated for ELISA, Surface plasmon resonance, Inhibition. For details, refer to Published Data.

Target

  • Alternative Names
  • apical membrane antigen 1; AMA1; AMA-1; Plasmodium falciparum; P. falciparum; Pf83; RMA-1; RMA1

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 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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