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Creative BioMart is a well-known expert who uses various protein domains as non-antibody scaffolds to produce synthetic binding proteins that have the ability to bind to molecules. With years of experience, we successfully designed zinc finger proteins based on non-antibody scaffolds to precisely meet customer requirements.
Zinc finger domain was originally coined to describe the finger-like appearance of a hypothesized structure from the African clawed frog (Xenopus laevis) transcription factor IIIA, and it has been found that it contains a variety of different protein structures in eukaryotic cells. Through gene sequencing, it was found that zinc finger proteins account for 2-3% of the entire human genome and are the most common DNA binding motif in human transcription factors. Zinc-finger proteins are related to a wide range of biological functions such as development, differentiation, and suppression of tumors. Each zinc-finger domain consists of twenty to thirty amino acid residues that have a special secondary structure stabilized by zinc ion bound to the Cys (C) and His (H) residues of the finger. Zinc finger has become the first choice for engineering design due to its small size, simple structure, and relatively simple interaction with DNA. In recent years, huge progress has been made in protein design and engineering based on zinc finger domains. Zinc finger nuclease and zinc finger transcription factor are the two most important applications realized so far.
Fig 1. Zinc Finger Modules and Binding Sites. (Sander JD, et al., 2007)
Zinc finger proteins have great potential as tools for gene regulation and genome modification, because they can locate functional domains at any position in any genome. As a leading service provider of protein engineering, Creative BioMart uses a variety of design strategies to redesign zinc finger domains (such as C2H2, C2HC, C4 ribbon, C4 GATA family, C6, C8, C3HC4 ring finger, and H2C2.) The sequence to create new zinc finger peptides/proteins provides valuable tools for biological research and gene therapy.
Cys(2)His(2) type zinc finger is one of the most common DNA binding motifs in eukaryotes. The simple mode of DNA recognition of Cys(2)His(2) type zinc finger domain is to design a new function protein provides an ideal scaffold. Based on Cys(2)His(2) zinc finger domain, Creative BioMart has established a mature artificial zinc finger protein design and synthesis platform, opening up the possibility of using engineered zinc finger-based factors as a new type of human therapy. For example, our redesigned Cys(2)His(2) zinc finger protein customizes its DNA binding properties by changing the secondary structure elements (ɑ-helix and β-sheet) of the domain, which increases the binding affinity by about 1000 times, realizing gene therapy the high binding affinity and fine specificity required by the application. In addition, we used computer modeling to design dimeric zinc finger proteins to bind predicted binding sites with high affinity and specificity. The DNA binding specificity of this fusion protein is mainly determined by the zinc fingers, and can be systematically changed by replacing the zinc fingers with variants of phage display selection.
Based on the protein engineering platform, we have successfully designed a variety of platforms for different applications to produce special proteins. We will work with you to develop the most appropriate strategy and provide the most meaningful data for your research for accelerating the research of life sciences. If you are interested in our services, please do not hesitate to contact us for more information.
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