Phage display is a selection technique in which a peptide or protein is fused with a bacteriophage coat protein and displayed on the surface of a virion. This technology was first described by George P. Smith in 1985, when he demonstrated the display of peptides on filamentous phage by fusing the peptide of interest to gene III of filamentous phage. Phage-displayed random peptide libraries enable functional access to the peptides and provide a physical link between phenotype (the displayed peptide) and genotype (the encoding DNA); these libraries lend themselves to a screening process in which binding clones are separated from nonbinding clones by affinity purification.

　　Peptides binding to individual targets can be identified by affinity selection (called biopanning). For biopanning, a display library is incubated with an immobilized target, followed by extensive washing to remove nonreacting phages. Binders are usually eluted using acid or high salt and are enriched by amplification in the appropriate host cells. Three to five rounds of biopanning are usually performed in order to obtain targets that bind with high affinity. The primary structure of the peptide can then be determined by sequencing the DNA of individual clones. Using this approach, it is easy to identify peptides that bind specifically to target molecules.

　　Empowered by extensive experience and well-established phage display technique platform, KS-V now brings out a comprehensive list of premade peptide libraries for various research programs. Over years, we have integrated multiple peptide libraries with varied lengths and properties to satisfy all kinds of applications.These random peptide libraries with such great quality and diversity can make excellent tools for peptide agent discovery.

　　Besides, we also provide featured service of custom peptide library construction and screening service. KS-V have earned great reputation from our clients for superior peptide library products & custom services.