NeuroMab™ Anti-NGF Antibody, Clone E3
A functional antibody raised against Human, Rodent NGF.
- Host Species:
- Humanized
- Species Reactivity:
- Human; Rodent
- Applications:
- FC; ELISA; Block; Inhib; In Vitro; In Vivo; Antagonist
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Low Endotoxin < 1 EU/mg
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Research Use Only
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Figure 1 is a graph comparing the NGF blocking effect of various Fabs in the presence of human NGF 0.04 ng/ml.
Elimination is measured using an antibody-dependent cellular cytotoxicity assay ("ADCC").
Figure 2 is a graph showing rest pain evaluated 24 hours after surgery, showing that treatment with 0.02 mg/kg, 0.1 mg/kg, 0.6 mg/kg, and 1 mg/kg of anti-NGF E3 antibody reduced pain. "*" indicates a statistically significant difference (p < 0.5) from the negative control.
Elimination is measured using an antibody-dependent cellular cytotoxicity assay ("ADCC").
Figure 3 is a graph showing the results of BIAcore analysis of human NGF binding affinity of E3 (Fab) antibody (referred to as "Fab 3E"). E3 binds to human NGF with a KD of about 0.07 nM (kon about 6.0 x 105 M-1 s-1, koff about 4.2 x 10-5 s-1).
Elimination is measured using an antibody-dependent cellular cytotoxicity assay ("ADCC").
Figure 4 is a graph showing that E3 antibody blocks the interaction of NGF with its receptors trkA and p75.
Axis corresponds to concentration of 3E antibody (Fab) and Y axis corresponds to NGF binding (percentage of maximal UR). Increasing concentrations of Fab E3 blocked the interaction of NGF with p75 and trkA, as indicated by a decrease in signal (measured in UR). When the concentration of E3 antibody (Fab) was equal to that of NGF, no NGF binding was observed (indicated by zero signal).
Figure 5 is a graph showing the capacities of Antibody E3 (solid triangles; referred to as "3E"), Antibody 911 (solid circles) at different concentrations (20, 4, 0.8, 0.16, 0.032, 0.0064, 0.00128, and 0.0 nM) and The trkA receptor immunoadhesin (shaded squares; designated 'trkA-Fc') inhibits NGF-dependent survival of trigeminal neurons E13.5.
Axis corresponds to concentration of 3E antibody (Fab) and Y axis corresponds to NGF binding (percentage of maximal UR). Increasing concentrations of Fab E3 blocked the interaction of NGF with p75 and trkA, as indicated by a decrease in signal (measured in UR). When the concentration of E3 antibody (Fab) was equal to that of NGF, no NGF binding was observed (indicated by zero signal).
Figure 6 is a graph showing the nociceptive response of arthritic rats (rheumatoid arthritis model) after administration of anti-NGF antibodies (E3 and 911) on D14 and D19.
Axis corresponds to concentration of 3E antibody (Fab) and Y axis corresponds to NGF binding (percentage of maximal UR). Increasing concentrations of Fab E3 blocked the interaction of NGF with p75 and trkA, as indicated by a decrease in signal (measured in UR). When the concentration of E3 antibody (Fab) was equal to that of NGF, no NGF binding was observed (indicated by zero signal).
Figure 7 is a graph showing the effect of anti-NGF antibody on body weight of arthritic rats (rheumatoid arthritis model) after administration of anti-NGF antibody on D14 and D19.
Axis corresponds to concentration of 3E antibody (Fab) and Y axis corresponds to NGF binding (percentage of maximal UR). Increasing concentrations of Fab E3 blocked the interaction of NGF with p75 and trkA, as indicated by a decrease in signal (measured in UR). When the concentration of E3 antibody (Fab) was equal to that of NGF, no NGF binding was observed (indicated by zero signal).
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