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Creative Biolabs

NeuroMab™ Anti-NGF BBB Shuttle Antibody,Clone NR1963P

[CAT#: NRZP-1022-ZP2426]

Host Species:
Mouse
Species Reactivity:
Human; Rodent
Applications:
FC; ELISA; Block; Inhib; In Vitro; In Vivo; Antagonist

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Product Overview

Description

Brain uptake of therapeutic antibodies is severely limited by their size. To achieve enhanced BBB crossing, Creative Biolabs developed a BBB shuttle antibody platform by utilizing the endogenous macromolecule transportation pathway, known as receptor-mediated transcytosis (RMT). The engineered antibody-based carrier is believed to significantly to increase the macromolecule brain entry to combat CNS diseases.
Notes: The BBB antibody is made-to order and available in a customized format. Please don't hesitate contact us for more details.

Species Reactivity

Human; Rodent

Clonality

Monoclonal

Host Species

Mouse

Clone Number

NR1963P

Applications

FC; ELISA; Block; Inhib; In Vitro; In Vivo; Antagonist

Relevant Diseases

Alzheimer's Disease; Parkinson's Disease; Huntington's Disease; Multiple Sclerosis
Product Properties

Storage

Store at -20°C. Do not aliquot the antibody.

Research Use Only

For research use only
Target

Target

NGF

Official Name

NGF

Full Name

Nerve Growth Factor

Alternative Names

Nerve Growth Factor; Nerve Growth Factor (Beta Polypeptide); Beta-NGF; NGFB; Nerve Growth Factor; Beta Subunit; Beta-Nerve Growth Factor; HSAN5;
Product Pictures
Block

Fig.1 is a graph comparing the effect of blocking NGF of various Fab in the presence of human NGF 0.04 ng / ml.

The X axis corresponds to the concentration of 3E antibody (Fab) and the Y axis corresponds to NGF binding (percentage of maximum UR). Increased concentrations of Fab E3 blocked the interaction of NGF with both p75 and trkA, as shown by signal reduction (measured in UR). When the concentration of E3 antibody (Fab) was equalized with the concentration of NGF, no NGF binding was observed (as shown by a zero signal).

BIAcore

Fig.2 is a graph showing the results of BIAcore analysis of human NGF binding affinity of mouse antibody 911 (Fab). Mouse antibody 911 bound NGF with a KD of 3.7 nM, koff of 8.4 x 10-5 s-1 and kon of 2.2 x 104 Ms-1.

The X axis corresponds to the concentration of 3E antibody (Fab) and the Y axis corresponds to NGF binding (percentage of maximum UR). Increased concentrations of Fab E3 blocked the interaction of NGF with both p75 and trkA, as shown by signal reduction (measured in UR). When the concentration of E3 antibody (Fab) was equalized with the concentration of NGF, no NGF binding was observed (as shown by a zero signal).

BIAcore

Fig.3 is a graph showing the results of BIAcore analysis of the human NGF binding affinity of the E3 (Fab) antibody (called "Fab 3E"). E3 was linked to human NGF with a KD of approximately 0.07 nM (and with a kon of approximately 6.0 x 105 M-1 s-1 and a koff of approximately 4.2 x 10-5 s-1).

The X axis corresponds to the concentration of 3E antibody (Fab) and the Y axis corresponds to NGF binding (percentage of maximum UR). Increased concentrations of Fab E3 blocked the interaction of NGF with both p75 and trkA, as shown by signal reduction (measured in UR). When the concentration of E3 antibody (Fab) was equalized with the concentration of NGF, no NGF binding was observed (as shown by a zero signal).

Block

Fig.4 is a graph representsing that the E3 antibody blocks the interaction of NGF with its receptors, trkA and p75.

The X axis corresponds to the concentration of 3E antibody (Fab) and the Y axis corresponds to NGF binding (percentage of maximum UR). Increased concentrations of Fab E3 blocked the interaction of NGF with both p75 and trkA, as shown by signal reduction (measured in UR). When the concentration of E3 antibody (Fab) was equalized with the concentration of NGF, no NGF binding was observed (as shown by a zero signal).

Inhib

Fig.5 is a graph that representss the capacity of various concentrations (20, 4, 0.8, 0.16, 0.032, 0.0064, 0.00128 and 0.0 nM) of antibody E3 (solid triangles; called “ 3E ”), antibody 911 (solid circles) and a trkA receptor immunoadhesin (shaded squares; called“ trkA-Fc) to inhibit NGF-dependent survival of trigeminal neurons E13.5.

The X axis corresponds to the concentration of 3E antibody (Fab) and the Y axis corresponds to NGF binding (percentage of maximum UR). Increased concentrations of Fab E3 blocked the interaction of NGF with both p75 and trkA, as shown by signal reduction (measured in UR). When the concentration of E3 antibody (Fab) was equalized with the concentration of NGF, no NGF binding was observed (as shown by a zero signal).

FuncS

Fig.6 It is a graph that demonstrates the nociceptive response in arthritic rats (rheumatoid arthritis model) after administration of anti-NGF antibodies (E3 and 911) in D14 and D19.

The X axis corresponds to the concentration of 3E antibody (Fab) and the Y axis corresponds to NGF binding (percentage of maximum UR). Increased concentrations of Fab E3 blocked the interaction of NGF with both p75 and trkA, as shown by signal reduction (measured in UR). When the concentration of E3 antibody (Fab) was equalized with the concentration of NGF, no NGF binding was observed (as shown by a zero signal).

FuncS

Fig.7 It is a graph that demonstrates the effects of anti-NGF antibodies on body weight in arthritis in rats (rheumatoid arthritis model) after administration of anti-NGF antibodies in D14 and D19.

The X axis corresponds to the concentration of 3E antibody (Fab) and the Y axis corresponds to NGF binding (percentage of maximum UR). Increased concentrations of Fab E3 blocked the interaction of NGF with both p75 and trkA, as shown by signal reduction (measured in UR). When the concentration of E3 antibody (Fab) was equalized with the concentration of NGF, no NGF binding was observed (as shown by a zero signal).

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