Fusion tags for recombinant protein expression and purification in structural and functional studies

Area of Science:

• Biochemistry
• Molecular Biology
• Structural Biology

Background:

• Protein purification is essential for biochemical, biophysical, and structural analyses.
• Native protein isolation often suffers from low yield and heterogeneity.
• Recombinant protein expression offers a scalable alternative for producing target proteins.

Purpose of the Study:

• To review commonly used fusion tags for recombinant protein expression and purification.
• To provide guidance on selecting fusion tags based on experimental requirements and target protein characteristics.
• To highlight the role of fusion tags in overcoming challenges in protein yield, solubility, stability, and recovery.

Main Methods:

• Overview of various fusion tag systems used in recombinant protein production.
• Discussion of strategies for optimizing fusion tag selection for specific experimental goals.
• Exploration of how fusion tags facilitate affinity-based purification and characterization.

Main Results:

• Fusion tags significantly improve expression levels and facilitate purification of recombinant proteins.
• Selected fusion tags can enhance protein solubility and stability.
• Fusion tags enable streamlined protein production for downstream structural and functional studies.

Conclusions:

• Fusion tags are indispensable tools for efficient recombinant protein expression and purification.
• Appropriate fusion tag selection expands research possibilities in protein science.
• Advances in fusion tag technology enhance the understanding of protein function and support therapeutic design.