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Construction of Functional GFP-Neo Fusion Protein by Selection from a Peptide Library | Abstract
Cloning  & Transgenesis

Cloning & Transgenesis
Open Access

ISSN: 2168-9849

+443308089004

Abstract

Construction of Functional GFP-Neo Fusion Protein by Selection from a Peptide Library

Jiayou Zhang

Almost all retroviral vectors need to express more than one protein. One of the strategies to express multiple proteins is to construct a fusion protein that encodes two genes from a single reading frame. Since the interaction of two closely linked proteins resistance gene. This peptide library was then transformed into bacteria, and the transformed bacteria were selected for green fluorescence and antibiotic resistance. Several fusion proteins have been selected. When these fused genes are expressed by retroviral vectors, the GFP-Neo fusion proteins are also functional in eukaryotic cells. The fluorescence intensity of our fusion proteins is much greater than a commercial GFP fusion clone, although it is still less than the wild-type GFP. The isolation of a fusion protein described here can be modified and used to isolate other fusion proteins as long as selections for their functions are available.