Related Experiment Video

Updated: Jun 1, 2026

Non-chromatographic Purification of Recombinant Elastin-like Polypeptides and their Fusions with Peptides and Proteins from Escherichia coli
07:35

Non-chromatographic Purification of Recombinant Elastin-like Polypeptides and their Fusions with Peptides and Proteins from Escherichia coli

Published on: June 9, 2014

An improved nonchromatographic method for the purification of recombinant proteins using elastin-like

Dongming Lan1, Guangrui Huang, Hongwei Shao

  • 1State Key Laboratory of Biocontrol, Guangdong Province Key Laboratory of Therapeutic Functional Genes, College of Life Sciences, Sun Yat-sen University, Guangdong 510275, People's Republic of China.

Analytical Biochemistry
|May 24, 2011
PubMed

More Related Videos

Efficient Purification of Elastin-Like Polypeptides (ELPs) from E. coli Using an Organic Solvent-based Extraction and Precipitation Method06:30

Efficient Purification of Elastin-Like Polypeptides (ELPs) from E. coli Using an Organic Solvent-based Extraction and Precipitation Method

Published on: January 9, 2026

High-throughput Purification of Affinity-tagged Recombinant Proteins07:44

High-throughput Purification of Affinity-tagged Recombinant Proteins

Published on: August 26, 2012

Related Concept Videos

Tagging and Fusion Proteins01:24

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...