Related Experiment Video
Updated: Jan 19, 2026
Bacterial Expression and Purification of Human Matrix Metalloproteinase-3 using Affinity Chromatography
Published on: March 30, 2022
[Expression and purification of human amelogenin mature peptide in Escherichia coli]
Xue-Yang Zhang1, Jin-Cai Zhang, Hua Zhao
1Department of Periodontology, Guangdong Provincial Stomatological Hospital, Guangzhou 510280, China.
Objective:
To establish the expression and purification route for human amelogenin mature peptide in Escherichia coli and obtain the purified amelogenin (AMG) mature peptide.
Methods:
Recombined plasmid pGEX-4T-1-AMG was transformed to Escherichia coli BL21. After expression, AMG was purified with glutathione S-transferase fusion protein purification system (GSTrapFF) column.
Results:
Sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) and Western blotting hybridization results showed that 45,000 GST-AMG fusing protein and 19,000 target AMG mature peptide were obtained successfully.
Conclusions:
pGEX-4T-1-AMG-BL21 system is used successfully to express and purify human AMG mature peptide.
More Related Videos
10:01Directed Assembly of Elastin-like Proteins into defined Supramolecular Structures and Cargo Encapsulation In Vitro
Published on: April 8, 2020
07:08Efficient Mammalian Cell Expression and Single-step Purification of Extracellular Glycoproteins for Crystallization
Published on: December 23, 2015