Fusion Protein
Fusion Protein — A protein created by joining two or more genes that originally coded for separate proteins, used to express and purify recombinant peptides.
What Is a Fusion Protein?
A fusion protein is a chimeric molecule created by genetically joining a peptide sequence to a larger protein partner. Fusion partners improve peptide expression yield, solubility, purification (His-tag, GST), and in vivo half-life (Fc, albumin). The fusion partner is often removed by protease cleavage after purification.
Common Fusions
- His-tag: 6xHis enables IMAC purification on Ni-NTA. Small, rarely affects activity
- Fc fusion: IgG Fc domain extends half-life via FcRn recycling (dulaglutide = GLP-1-Fc)
- Albumin fusion: Albiglutide = GLP-1-albumin. Half-life extended to 5 days
- SUMO: Enhances solubility of aggregation-prone peptides in E. coli
Frequently Asked Questions
What is Fusion Protein?
A protein created by joining two or more genes that originally coded for separate proteins, used to express and purify recombinant peptides.
Why is Fusion Protein important in peptide research?
Fusion Protein is a fundamental concept in manufacturing as it relates to peptide science. It directly influences experimental design, compound characterization, and the reliability of research outcomes across biochemistry and molecular biology disciplines.
Authority Sources
- Fusion Protein on Wikipedia
- Search Fusion Protein on PubChem (NIH)
- Research articles on ScienceDirect