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Tagging and Fusion Proteins

Tagging and Fusion Proteins

Proteins are involved in several cellular processes and biochemical reactions. Analyzing a specific protein of interest requires it to be isolated from the other proteins in the cell. This is achieved by overexpressing the specific gene in a suitable host to produce large quantities of the target protein. A tag or label is recombined with the gene to produce a fusion protein containing the target protein and the tag. The tags on these fusion proteins can then be used for easy detection and...

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Related Experiment Video

Updated: Nov 16, 2025

Evaluation of the Interplay Between the Complement Protein C1q and Hyaluronic Acid in Promoting Cell Adhesion

Evaluation of the Interplay Between the Complement Protein C1q and Hyaluronic Acid in Promoting Cell Adhesion

Published on: June 15, 2019

Functional recombinant human complement C1q with different affinity tags.

Isabelle Bally¹, Sarah Ancelet¹, Jean-Baptiste Reiser¹

¹Univ. Grenoble Alpes, CEA, CNRS, IBS, F-38000 Grenoble, France.

Journal of Immunological Methods

|February 23, 2021

Summary

This summary is machine-generated.

Researchers created new versions of complement C1q protein with different tags. These tagged C1q variants maintain their ability to bind immune molecules and activate the complement system, offering valuable tools for further study.

Keywords:

Affinity tag C1q Complement Interaction properties Recombinant protein

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Orthogonal Protein Purification Facilitated by a Small Bispecific Affinity Tag

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Last Updated: Nov 16, 2025

Evaluation of the Interplay Between the Complement Protein C1q and Hyaluronic Acid in Promoting Cell Adhesion

Evaluation of the Interplay Between the Complement Protein C1q and Hyaluronic Acid in Promoting Cell Adhesion

Published on: June 15, 2019

High-resolution Melting PCR for Complement Receptor 1 Length Polymorphism Genotyping: An Innovative Tool for Alzheimer's Disease Gene Susceptibility Assessment

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Published on: July 18, 2017

Orthogonal Protein Purification Facilitated by a Small Bispecific Affinity Tag

Orthogonal Protein Purification Facilitated by a Small Bispecific Affinity Tag

Published on: January 16, 2012

Area of Science:

Immunology
Molecular Biology
Biochemistry

Background:

Complement C1q initiates the classical complement pathway by binding to pathogens and immune complexes.
C1q is a hexameric protein comprising three polypeptide chains (A, B, C) with distinct collagenous and globular domains.

Purpose of the Study:

To generate and characterize novel recombinant complement C1q variants with various affinity tags.
To assess the functionality of these tagged C1q variants in binding and complement activation.

Main Methods:

Production of recombinant C1q proteins in HEK 293-F cells with C-terminal or N-terminal FLAG, Myc, or 6-His tags.
Assessment of C1q variant binding affinities to IgM and C1r2-C1s2 tetramer via ELISA or similar assays.
Evaluation of C1q-mediated serum complement activation triggered by IgM.

Main Results:

Multiple recombinant C1q variants with FLAG, Myc, or 6-His tags were successfully produced.
All tested C1q variants, except the 6-His tagged protein, exhibited comparable yields and binding affinities to IgM and C1r2-C1s2.
The functional C1q variants effectively triggered IgM-mediated classical complement pathway activation.

Conclusions:

The newly generated recombinant C1q variants are functional and suitable for research.
These tagged C1q proteins serve as valuable tools for exploring the diverse roles of C1q in immunity.