Recombinant Protein Detection
Recombinant Protein Detection - Related Videos
09:00
Detection of Protein Ubiquitination
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Cited by 97 •
2009
Ubiquitination is a key posttranslational modification carried out by a set of three enzymes. Mutations of genes involved in this modification are associated with many different human diseases. Here, we describe protocols to detect protein ubiquitination in cultured cells in vivo and test tubes in vitro.
03:56
An In Vitro Recombinant Virus Reporter System for the Detection of Viral Infection
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2025
This video demonstrates an in vitro technique to detect hepatitis B virus (HBV) infection via a recombinant HBV reporter system. Upon infecting host cells, the recombinant viral genome expresses the luciferase reporter enzyme, which produces bioluminescence upon oxidizing its substrate — helping detect viral infection.
09:46
Expression of Recombinant Proteins in the Methylotrophic Yeast Pichia pastoris
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Cited by 57 •
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.
03:39
Generation of an Immunostimulatory Protein-Encoding Recombinant Measles Virus
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2026
Source: Heidbuechel, J. P., Engeland, C. E. Paramyxoviruses for Tumor-targeted Immunomodulation: Design and Evaluation Ex Vivo. J. Vis. Exp. (2019)This video demonstrates the generation of recombinant measles viruses using liposomes to deliver plasmids encoding the viral antigenome and essential helper proteins into producer cells. The transcribed and replicated RNA leads to the formation of viral particles expressing immunostimulatory and fluorescent reporter proteins. Fluorescence microscopy...
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
Detection can target a recombinant protein through antibody recognition of a specific epitope, binding of an affinity tag to a capture reagent, or size separation followed by immunoblotting. These approaches rely on different protein features, so the resulting evidence reflects whether the engineered product is recognized, captured, or resolved as an appropriately sized species during analysis.
An affinity tag provides a defined binding feature that a capture reagent can recognize. This gives researchers a way to identify the engineered product even when its natural properties are not the main basis of detection. In recombinant protein studies, tag-based recognition can therefore support evaluation of expression and purification alongside other detection strategies.
Enzyme-linked assays and fluorescence convert recognition of the target protein into a measurable signal. The initial interaction may involve an antibody, epitope, or affinity tag, while the linked enzyme or fluorescent feature provides the readout. Signal measurement allows researchers to assess whether the recombinant product is present and compare detection outcomes during an experiment.
A typical workflow begins with a genetically engineered construct expressed in host cells, followed by analysis of the resulting protein material. Researchers may apply antibody recognition, affinity capture, or size separation before immunoblotting, then use enzyme-linked or fluorescent signal generation for measurement. This sequence connects the engineered DNA construct with evidence about its protein product.
Researchers use this analysis to verify that a cloned gene is expressed in host cells and that its expected product is present. It also helps evaluate recombinant protein production, examine engineered constructs, and assess the effects of experimental treatments. These uses connect DNA-level manipulation with observable protein-level outcomes in genetics research.
The results can inform studies of gene function, protein localization, recombinant protein purification, and biotechnology applications. Detection also helps assess whether an engineered construct produces the intended protein and whether experimental treatment changes the detectable product. In this way, protein-level measurements add functional and application-focused context to genetic engineering experiments.