Recombinant Antibody Expression
Recombinant Antibody Expression - Related Videos
03:38
A Method to Produce Recombinant Antibodies Against Metallopeptidase
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2025
This video demonstrates a procedure for the production of recombinant antibodies against metallopeptidase. Recombinant plasmids carrying genes for the antibody, green fluorescent protein, and antibiotic resistance are transfected into epithelial cells with lipofectamine. The transfected cells are selected and cultivated to generate recombinant antibodies.
12:55
Scalable High Throughput Selection From Phage-displayed Synthetic Antibody Libraries
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Cited by 33 •
2015
A method is described with visual accompaniment for conducting scalable, high throughput selections from phage-displayed combinatorial synthetic antibody libraries against hundreds of antigens simultaneously. Using this parallel approach, we have isolated antibody fragments that exhibit high affinity and specificity for diverse antigens that are functional in standard immunoassays.
12:18
Expression of Functional Recombinant Hemagglutinin and Neuraminidase Proteins from the Novel H7N9 Influenza Virus Using the Baculovirus Expression System
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Cited by 182 •
2013
Here we describe a way to express correctly folded and functional influenza virus surface antigens derived from the novel Chinese H7N9 virus in insect cells. The technique can be adapted to express ectodomains of any viral or cellular surface proteins.
09:46
Expression of Recombinant Proteins in the Methylotrophic Yeast Pichia pastoris
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Cited by 59 •
2010
The protocol describes protein expression using the methylotrophic yeast Pichia pastoris. The preparation of electrocompetent yeast cells, transformation of the vector with the gene of interest into P. pastoris and yeast DNA purification are also performed. Western blot analysis and protein purification build the last steps in this protein expression protocol.
07:50
Efficient Agroinfiltration of Plants for High-level Transient Expression of Recombinant Proteins
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Cited by 200 •
2013
Plants offer a novel system for the production of pharmaceutical proteins on a commercial scale that is more scalable, cost-efficient and safe than current expression paradigms. In this study, we report a simple and convenient, yet scalable approach to introduce target-gene containing Agrobacterium tumefaciens into plants for protein transient expression.
FAQs
The heavy- and light-chain genes provide paired instructions for producing the antibody molecule. After their introduction into a host cell, cellular transcription and translation generate the corresponding chains, which can assemble into a functional antibody. This genetic pairing connects a selected antibody sequence to a defined molecular product, supporting reproducible studies in immunology and infection research.
Sequence control makes the produced antibody defined and consistent across experiments. Investigators can preserve a selected molecular sequence and use it repeatedly when examining pathogen recognition, immune-marker detection, or treatment-oriented designs. The same control also provides a foundation for antibody engineering, allowing researchers to pursue improved specificity or other targeted properties without changing the starting antibody identity.
The host cell supplies the biological machinery required to turn introduced antibody genes into protein. It transcribes the heavy- and light-chain sequences, translates them into their respective chains, and supports their assembly into a functional antibody. In some expression systems, the assembled product is also secreted, which can provide access to the antibody outside the producing cell.
Several linked stages must proceed successfully: the antibody genes must be introduced into a suitable host, transcribed and translated, and the resulting heavy and light chains must assemble correctly. Secretion may follow assembly, but it is not universal. Because each stage contributes to the final product, expression results depend on coordinated gene activity, protein production, and molecular assembly.
A typical workflow begins with cloned sequences encoding the antibody heavy and light chains. Researchers introduce those sequences into a suitable host cell, allow the cell to transcribe and translate them, and then obtain the assembled antibody, which may be secreted. This sequence-to-product workflow provides a controlled route for generating material for subsequent immunology or infection studies.
Defined recombinant antibodies can recognize selected pathogens or immune markers and support standardized diagnostic assays. Because the antibody sequence is controlled, researchers can obtain a consistent reagent for repeated measurements rather than relying on an undefined production outcome. This reproducibility helps compare assay results across experiments and supports the development of tools for detecting infection-related targets.
They provide several complementary research uses: identifying pathogens, detecting immune markers, and neutralizing microbial targets. These activities allow investigators to examine host-pathogen interactions while using antibody molecules with controlled sequences. The same platform also supports development of engineered antibodies with improved specificity and targeted biologic potential, linking basic immune research with translational applications.