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Creative Biolabs
Product

NeuroMab™ Anti-SEZ6 BBB Shuttle Antibody, Clone NR26P

[CAT#: NRZP-1022-ZP2433]

Host Species:
Mouse
Species Reactivity:
Human; Cynomolgus Monkey
Applications:
FC; IHC; In Vitro; In Vivo

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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; Cynomolgus Monkey

Clonality

Monoclonal

Host Species

Mouse

Clone Number

NR26P

Applications

FC; IHC; In Vitro; In Vivo
Product Properties

Storage

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

Research Use Only

For research use only
Target

Target

SEZ6

Official Name

SEZ6

Full Name

Seizure Related 6 Homolog

Alternative Names

Seizure Related 6 Homolog; Seizure Related 6 Homolog (Mouse); Seizure Protein 6 Homolog; HSEZ-6; BSRPC; SEZ-6;
Product Pictures
FuncS

Fig.1 show the detection by flow cytometry of the expression of the SEZ6 protein in NTX tumor cells using various anti-SEZ6 antibodies.

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.2 shows the results of an in vitro destruction assay using anti-SEZ6 ADC in HEK293 cells that overexpress SEZ6.

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.3 shows the effect of anti-SEZ6 ADC on the in vivo growth of SCLC (LU86) and LCNEC (Lu50) tumors.

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.4 represents the ability of conjugated humanized anti-SEZ6 antibodies to retard the growth in vivo of four SCLC tumors (LU80, LU64, LU111 and LU117) and achieve lasting remission in immunosuppressed mice.

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.5 represents the ability of conjugated humanized anti-SEZ6 antibodies to retard the growth in vivo of four SCLC tumors (LU80, LU64, LU111 and LU117) and achieve lasting remission in immunosuppressed mice.

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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