Antibody Phage Display Introduction

The phage display library can be divided into two categories according to whether the conformation of the exogenous fused polypeptide is restricted.
By: ALPHA LIFETECH INC.
 
ALBANY, N.Y. - Nov. 6, 2023 - PRLog -- In recent years, phage display technology has developed rapidly, and it has a wide range of applications in the research fields of antibody epitopes, protein inhibitors and activators, enzyme-substrate specificity, protein folding, drug and vaccine design, gene expression regulation, and molecular recognition in the immune system. The so-called phage display is the method of molecular cloning to express the foreign nucleic acid fragment in the form of fusion protein on the surface of phage particles.

In general, phage display experiments can be summarized in two steps: a to build a library; b screening the library, firstly through artificial synthesis, cDNA method, DNase I random hydrolysis method to prepare a variety of nucleic acid fragments with different sequences, and then clone them in the carrier (bacteria or bacteria granules), and then infect or superinfect Escherichia coli to secrete phages with fusion expression of foreign fragments, collectively called library construction. Then immobilized target molecules were used to screen phages that were compatible with them. Phage display technology has two obvious advantages. One is that phage is easy to expand, and the other is that the amino acid sequence of foreign peptides or proteins expressed by fusion can be deduced by measuring the sequence of phage DNA. Phage display can be fused to express peptides, protein domains, and proteins, and the fused peptides displayed on the bacteria are called phage peptides.

Articles from Alpha Lifetech described detailed information about Ligand Phage Display Library and Substrate Phage Display Library. Please visit our website to learn more information: https://www.alphalifetech.com/article/Antibody-Phage-Disp...
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Source:ALPHA LIFETECH INC.
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