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Essential Tool for Phage Display System - M13 Nano-Secondary Antibodies

M13 Nano-Secondary Antibody Solution | A Highly Sensitive Detection Tool for Phage Display Screening

In today's rapidly developing antibody drug and molecular diagnostics field, phage display technology has become a core platform for antibody discovery and optimization, and has been recognized with the Nobel Prize in Chemistry for its groundbreaking contributions to peptide screening and antibody engineering.

As one of the most mature display systems currently available, M13 phage is widely used in antibody library screening, affinity maturation, and biomolecular screening experiments, serving as a crucial "molecular screening engine" for modern biomedical research and development.

However, achieving high sensitivity, low background, and stable and reliable detection remains a key factor affecting experimental efficiency in the phage display screening process.


Phage Display Technology: An Accelerator for Biopharmaceutical Development 

Half of the 2018 Nobel Prize in Chemistry was awarded to George P. Smith and Sir Gregory P. Winter for their invention and application of phage display technology for peptides and antibodies. This groundbreaking technology has become a core tool in today's biopharmaceutical research and development for screening high-affinity therapeutic antibodies, recombinant proteins, and targeted peptides.

Based on the principle of "fusion of the coat protein and the exogenous gene," hundreds of millions of variant peptides or antibody fragments (such as ScFv, Fab, and VHH) are displayed on the phage surface. After multiple rounds of "adsorption-elution-amplification" enrichment (Panning), high-throughput identification using ELISA (enzyme-linked immunosorbent assay) is a crucial step in determining the success of the screening. In this process, high-performance M13-labeled antibodies (secondary antibodies) are indispensable "color-developing tools."

Essential Tool for Phage Display System - M13 Nano-Secondary Antibodies


M13 Phage: Mature System and Capsid Protein Deciphered

Of all display systems, the M13-based filamentous phage system is the most mature and widely used. M13 is a non-lytic (filamentous) virus that infects *E. coli*, its core being a circular single-stranded DNA (ssDNA) composed of over 6400 nucleotides.

Its capsid structure is intricate, composed of several key capsid proteins:

● P8 (major capsid protein): With approximately 2700 copies, it surrounds the virus. P8 display (multivalent display), due to its extremely high copy number, generates a strong affinity effect, making it ideal for screening peptide and short peptide libraries.

● P3 (minor capsid protein): Located at the phage terminal, it has only about 5 copies. P3 mediates the phage's adsorption to *E. coli* fimbriae. Due to their low copy number (low-value display), the P3 display system is commonly used for screening antibody libraries (such as ScFv and VHH), accurately reflecting the inherent affinity of the antibody and effectively avoiding false positives.

● P6, P7, and P9: These are also terminal minor proteins that play a role in viral assembly and specific display strategies.

Due to the unique biological characteristics of M13 phage, accurately and without steric hindrance capturing these capsid proteins under high background interference has become a major challenge for ELISA identification.

Essential Tool for Phage Display System - M13 Nano-Secondary Antibodies

 

AlpVHHs Innovative Recombinant Nanoantibodies: Breaking Through the Pain Points of Traditional Secondary Antibodies

As an innovative leader in high-throughput antibody development, AlpVHHs has successfully screened recombinant nanobodies with extremely high affinity (in the nanomolar nM range) for M13 phage capsid proteins (such as P8/P3) using its proprietary high-throughput yeast display platform.

Traditional animal-derived polyclonal secondary antibodies often face problems such as large batch-to-batch variability, high background signal, and steric hindrance due to large molecular weight. Our AlpVHHs series of recombinant secondary antibodies perfectly solves these research pain points.


M13-HRP Direct-Label Antibody | Making Phage Detection Simpler and More Efficient

Targeting the most critical ELISA detection step in phage display experiments, we have developed a high-performance M13-HRP direct-label antibody, significantly improving screening efficiency and detection reliability:

● Ultra-high sensitivity detection: Effectively identifies M13 phage signals, reducing the risk of false negatives

● HRP direct-label design: Simplifies the experimental process, reduces operational steps, and improves experimental efficiency

● High specificity binding: Accurately identifies M13 phage with lower background and a better signal-to-noise ratio

● Stable batch consistency: The recombinant expression system ensures a long-term stable supply

Essential Tool for Phage Display System - M13 Nano-Secondary Antibodies


One-Stop Solution for Phage Display

From antibody screening to detection validation, AlpVHHs provides a complete toolchain:

Phage display screening system construction

● M13-HRP antibody for rapid ELISA detection

● AlpVHHs nanobodies for subsequent high-affinity molecule development

This integrated solution significantly improves screening efficiency, experimental stability, and result reproducibility, helping research and biopharmaceutical teams accelerate project progress.


Why Choose AlpVHHs Recombinant Antilbody?

Essential Tool for Phage Display System - M13 Nano-Secondary Antibodies

● Strict Verification: Multiple validations ensure high specificity, high affinity (nM level), and clear application. This ensures accurate experiments.

● Stable Supply: Clear antibody sequences enable the construction of stable recombinant expression cell lines, minimizing batch-to-batch variability and ensuring robust experiments.

● Multiple Options: Clear VHH and Fab sequences enable chimeric expression with Fc fragments from different species, facilitating experimental design and supporting custom antibody development .

● Ethical Considerations: Recombinant expression is performed in serum-free, chemically defined culture medium, eliminating the presence of any animal-derived components.


Driving Phage Display into an Era of High Efficiency

With the rapid development of antibody drugs and molecular diagnostics, phage display technology is becoming a core infrastructure for new drug development.

AlpVHHs will continue to focus on the development of nanobodies and phage display tools, providing the global scientific research and biopharmaceutical industry with higher-performance, more stable, and easier-to-use molecular tool solutions.

Code

Description

Applications

Size

052-201-004

Anti-M13 Bacteriophage, AlpHcAbs® Rabbit antibody(Biotin)

ELISA

100ug

052-201-005

Anti- M13 Bacteriophage, AlpHcAbs® Rabbit antibody(HRP)

ELISA

100ug

052-201-001

Anti-M13 Bacteriophage, AlpHcAbs® Rabbit antibody

ELISA

100ug

052-201-007

Anti-M13 Bacteriophage, AlpHcAbs® Rabbit antibody(iFlour488)

ELISA,Flow Cyt

100ug

052-201-009

Anti-M13 Bacteriophage, AlpHcAbs® Rabbit antibody(iFlour647)

ELISA,Flow Cyt

100ug

052-101-010

Anti-M13 Bacteriophage, AlpSdAbs® VHH(PE)

Flow Cyt

0.1mL