NeuroMab™ Anti-AQP4 BBB Shuttle Antibody(NRZP-1022-ZP3670)

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

Clonality

Monoclonal

Host Species

Mouse

Applications

WB; In Vitro; Block; In Vivo; ADCC; CDC

Relevant Diseases

Epilepsy; Stroke; Glioblastoma

Product Properties

Storage

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

Research Use Only

For research use only

Target

AQP4

Official Name

AQP4

Full Name

Aquaporin 4

Alternative Names

AQP4; Aquaporin 4

Product Pictures

FuncS

Figure 1 depicts differential binding of purified monoclonal NMO-IgG to M1 and M23 AQP4.

Representative fluorescence micrographs of rAb-53 and rAb-58 (green) binding as a function of concentration, and a reference AQP4 antibody (red).

FuncS

Figure 2 depicts differential binding of purified monoclonal NMO-IgG to M1 versus M23 AQP4.

Binding curves of rAb-53 (left), rAb-58 (middle) and rAb-186 (right) to M1 vs. M23 AQP4 (mean ± SE, n=5). The curve representation fits the single-point binding model.

FuncS

Figure 3 depicts the mechanism for increasing the binding affinity of NMO-IgG to array-assembled AQP4.

Prediction of bivalent versus monovalent binding mechanisms. AQP4 monomers (cylinders) are shown to assemble into tetramers (M1) or OAPs (M23). NMO-IgG (green) binds monovalently or bivalently to the (unknown) extracellular domain on AQP4.

FuncS

Figure 4 depicts the mechanism for increasing the binding affinity of NMO-IgG to array-assembled AQP4.

Relative M1-M23 binding of whole IgG or purified Fab fragments of mouse anti-Myc (left), rAb-53 (middle) and rAb-58 (right) at fixed concentrations (mean ± SE, n=5).

Publications