Candy Swift's tracks: Recent Episodes
Candy Swift
Although single domain antibodies isolated from antibody libraries derived from gene synthesis and immunized or naïve animals generally exhibit reasonable affinity, it is often desirable to further increase their affinity. Quantitative library sorting by phage display or yeast surface display is used for improving the affinity of single domain antibodies. In particular, we have developed a proprietary DNA mutagenesis technique that is able to create a huge number (e.g. 1010) variants of the parental antibody with defined positions mutated.
http://www.creative-biolabs.com/Nanobody-Affinity-Maturation.html
Therapeutic proteins are proteins that are engineered in the laboratory for pharmaceutical use, including noncovalent binders, proteins that affect covalent bonds which are almost all enzymes, and albumin. Therapeutic proteins are highly effective in vivo and have revolutionized treatment of diseases. Protein therapeutics permits an individualized treatment approach by supporting a specifically targeted therapeutic process by compensating the deficiency of an essential protein.
http://www.creativebiolabs.net/therapeutic-proteins_47.htm
http://www.creative-biolabs.com/antibody-humanization.html
Humanization is important for reducing the immunogenicity of monoclonal antibodies derived from xenogeneic sources (commonly rodent) and for improving their activation of the human immune system. Since the development of the hybridoma technology, a large number of rodent monoclonal antibodies with specificity for antigens of therapeutic interest have been generated and characterized.
Reference: http://www.creative-biolabs.com/phage-display-service.html
Phage display is one of the most widely used laboratory technique for the study of protein-protein, protein-peptide and protein-DNA interactions. This technology is mainly based on the use of filamentous phage which is a kind of virus lives on Escherichia coli and has been proven as a powerful method to interrogate libraries containing millions or even billions of different peptides or proteins. Theoretically, phage display is an exogenous gene expression method which the gene encoding the interest protein is inserted into bacteriophage coat protein gene then displaying the interest protein on the phage surfaces, resulting in a connection between genotype and phenotype. Through DNA manipulation, numerous gene variants can be created and constructed as phage display library. To detect the interaction between displayed protein and those other molecules, phage display library can be screened to against other proteins, peptides or DNA sequences for selecting specific binders.
References: http://www.creative-biolabs.com/phage-display-service.html
Phage display is one of the most widely used laboratory technique for the study of protein-protein, protein-peptide and protein-DNA interactions. This technology is mainly based on the use of filamentous phage which is a kind of virus lives on Escherichia coli and has been proven as a powerful method to interrogate libraries containing millions or even billions of different peptides or proteins. Theoretically, phage display is an exogenous gene expression method which the gene encoding the interest protein is inserted into bacteriophage coat protein gene then displaying the interest protein on the phage surfaces, resulting in a connection between genotype and phenotype. Through DNA manipulation, numerous gene variants can be created and constructed as phage display library. To detect the interaction between displayed protein and those other molecules, phage display library can be screened to against other proteins, peptides or DNA sequences for selecting specific binders.
Reference: http://www.creative-biolabs.com/phage-display-service.html
Phage display is one of the most widely used laboratory technique for the study of protein-protein, protein-peptide and protein-DNA interactions. This technology is mainly based on the use of filamentous phage which is a kind of virus lives on Escherichia coli and has been proven as a powerful method to interrogate libraries containing millions or even billions of different peptides or proteins. Theoretically, phage display is an exogenous gene expression method which the gene encoding the interest protein is inserted into bacteriophage coat protein gene then displaying the interest protein on the phage surfaces, resulting in a connection between genotype and phenotype. Through DNA manipulation, numerous gene variants can be created and constructed as phage display library. To detect the interaction between displayed protein and those other molecules, phage display library can be screened to against other proteins, peptides or DNA sequences for selecting specific binders.
Reference: http://www.creative-biolabs.com/premade-phage-display-peptide-libraries.html
TriCo-16™ Phage Display Peptide Library
Type: pIII-fusion, True Phage Display
Format: 16-mer peptide library
Capacity: 2.60×1010
Trimer codons technology
Avoid stop and non-sense codon
Trimer codon for cysteine was excluded
TriCo-20™ Phage Display Peptide Library
Type: pIII-fusion, True Phage Display
Format: 20-mer peptide library
Capacity: 1.70×109
Trimer codons technology
Avoid stop and non-sense codon
Trimer codon for cysteine was excluded