Protein Directed Evolution

Protein directed evolution Library

In vitrodirected evolution of proteins is an artificially simulated natural evolution mechanism. It creates mutant protein that does not exist in nature or one that some of its enzyme properties are significantly enhanced by using modern molecular biology methods to create a large number of gene variants library and adopting sensitive directed selection strategy. Directed evolution has been widely used in the molecular modification of proteins and is considered as the most efficient method for producing proteins with improved or completely new properties.

Protein directed evolutionservice of Synbio Tech. provides a variety of methods to form gene mutation. Coordinatewith our leading screening techniques, we not only can create abundant gene diversities, but also can obtain the protein with required characteristics. Withmany years experience in protein and enzyme engineering research,scientists of Synbio Tech. willprovide professional, rapid, economic protein evolution services.

Service types of Protein Directed Evolution

1. Site-directed mutagenesis library: using synthetic biology methods to build proteins or regulate sequence site-directed mutagenesis library to form different mutants. It is a very effective way for scientists to conduct systematic research on protein characteristics, gene regulation and functions. Under the service of site-directed mutagenesis, Synbio Tech. can design, mutate and construct one or more amino acid sites that need to be mutated according to different needs. Each amino acid site can be mutated into anyoneof conventional 20 amino acidsin the light of research needs. What’s more, the proportion of each amino acid can be controlled accurately. The services include: scanning point mutation library, single point mutation, multi-point mutation, saturation mutation and conditional mutation, etc..
2. Random mutant library: the random mutation service platform developed by Synbio Tech. with the application of its own reagents and systems which can introduce nucleic acid mutation efficiently. It is capable of introducing random mutation to DNA sequence effectively and flexibly, and the mutation frequency can be controlled as1-10 mutation /kb.
3. Sequence combinationlibrary: the combination, splicing and construction of basic DNA expression elements (such as: promoters, UTRs, signal peptides and terminators) and different CDSs to form different sequences so as to express regulation combination. Researchers can reset different regulatory elements or genetic pathways according to their own designs to create new transcription units, biochemical pathways, genetic circuits, or engineering bacteria.
4. Non frame shift truncation library: an ideal tool for biologists to identify the smallest stable structure domain for crystallization and to determine the boundary amino acid residues that have important functions on proteins. The truncated mutations can also be obtained through the reduction of N- and C- end of the protein. Truncated library is more cost-effective in high throughput screening of peptides of different length and proteins compared to site-directed mutagenesis.

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