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Related Experiment Video

Updated: Jul 11, 2026

Transmembrane Domain Oligomerization Propensity determined by ToxR Assay

Transmembrane Domain Oligomerization Propensity determined by ToxR Assay

Published on: May 26, 2011

[PTD-hEGF fusion protein--gene expression and function analysis].

Qing-Wen Zhi¹, Shu-Hao Wang, Feng-Ying Zhang

¹Institute of Pharmacology and Toxicology, Academy of Military Medical Sciences, Beijing 100850, China.

Sheng Wu Gong Cheng Xue Bao = Chinese Journal of Biotechnology

|September 8, 2007

Summary

Researchers engineered a membrane-permeable human epidermal growth factor (hEGF) using a PTD-hEGF fusion protein. This genetically modified protein significantly enhanced HEK-293 cell proliferation and growth in vitro.

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Area of Science:

Biotechnology
Molecular Biology
Cell Biology

Background:

Human epidermal growth factor (hEGF) is crucial for cell growth.
Enhancing hEGF's membrane permeability can improve its therapeutic potential.
Developing efficient production methods for modified growth factors is essential.

Purpose of the Study:

To construct and express a membrane-permeable PTD-hEGF fusion protein.
To purify and characterize the expressed fusion protein.
To evaluate the biological activity of the PTD-hEGF fusion protein on cell proliferation.

Main Methods:

Construction of a pPTD-hEGF prokaryotic expression vector.
Transformation into E. coli BL 21 (DE3) and induction with IPTG.
Purification using Ni2+-NTA affinity chromatography and analysis by SDS-PAGE and MALDI-TOF-MS.

Main Results:

Successfully produced PTD-hEGF fusion protein as inclusion bodies with 40% yield.
Purified protein showed a single band at 16 kD via SDS-PAGE.
MALDI-TOF-MS confirmed the amino acid sequence.
PTD-hEGF significantly promoted HEK-293 cell proliferation and growth in vitro.

Conclusions:

A novel membrane-permeable PTD-hEGF fusion protein was successfully produced and purified.
The engineered PTD-hEGF demonstrates enhanced biological activity, promoting cell proliferation.
This provides a promising strategy for developing improved growth factor therapeutics.