B lymphocytes from the immune animals and myeloma cells are fused to obtain hybridoma cells that can both express specific antibodies and proliferate indefinitely in vitro. The hybridoma cells with vigorous growth and high expression levels are selected through high-throughput screening and expanded in culture to produce monoclonal antibodies in large quantities.

We provide a diverse range of immunization methods (including nucleic acids, proteins, cells) and efficient hybridoma preparation and screening strategies, offering a comprehensive solution from gene sequence to hybridoma cell development and identification.

Recombinant antibody genes are fused into genome of phage's capsid protein, enabling the display of antibody fusion proteins on the surface of the phage, thus constructing a library. Through solid-phase selection, phages that bind to the antigen are screened, amplified by infecting a host, and subjected to the next round of selection. After 3-5 rounds of repetition, highly enriched phages expressing the target antibody with specificity are obtained. Monoclonal strains can be further screened using ELISA or FACS.

Our antibody library has a capacity of billions (10^11 pfu) using a two-step library construction method which ensures library diversity. Antibody libraries of various species (human, mouse, rabbit, alpaca, chicken, dog, monkey, etc.) and types (scFv, Fab, VHH, etc.) can be constructed.

High-throughput screening and localization of B cells expressing specific antibodies are achieved using a photonic system. The expressed sequences of these antibodies are then obtained through sequencing, enabling the rapid discovery of monoclonal antibodies.

We combine multiple PCR technologies and automated high-throughput flow cytometry screening systems to facilitate the development of high-throughput, efficient, stable, and specific antibodies.