Creative Biolabs develops and commercializes a full range of integrated innovative services that are based on phage display technology. We have ...
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Many cellular activities are controlled by post-translational modifications, the study of which is hampered by the lack of specific reagents due in large part to their ubiquitous and non-immunogenic nature. Creative Biolabs has developed High-Affi™ technology, which offers antibody discovery services that specific for post-translational modifications on proteins.
Post-translational modifications are modifications that occur on proteins, catalyzed by enzymes, after its translation by ribosomes is complete. Post-translational modification refers to the addition of a functional group covalently to a protein as in phosphorylation and glycosylation. Protein post-translational modifications play a vital role in many cellular processes such as cellular differentiation, protein degradation, signaling and regulatory processes, regulation of gene expression, and protein-protein interactions. These modifications influence almost all aspects of normal cell biology and pathogenesis. Therefore, the identification and understanding of PTMs are critical in the study of both cell biology and the prevention and treatment of diseases.
Creative Biolabs provides specific antibody discovery services on a variety of post-translational modifications:
|Glycosylation||ISGylation||Tyrosine sulfation||Tyrosine nitration|
Fatty Acylation (N-Myristoylation,
Creative Biolabs employs phage display technology to support our post-translational modification specific antibody discovery.
Phage display platform for post-translational modification specific antibody discovery
Our staff scientists have extensive experience in the screening of phage display peptide, cDNA, and scFv/Fab libraries. In particular, by conducting library screening for 4 cycles, we normally get scFv/Fab antibodies of an affinity of 10-10 M.
In comparison with hybridoma technology, phage display technology offers greater advantages. Hybridoma-based monoclonal antibody technology can only generate a small number of binders against a particular immunogen at a time; whereas phage display technology can present the entire antibody repertoire (e.g. 1010) of an immunized animal, in which almost 10% of the antibodies are immunogen(s)-specific. With such a huge pool of potential binders, the chance is much better to use phage display technology to discover post-translational modification specific antibodies. In addition, it is hard to incorporate an enriching step that can selectively isolate antibodies of desired functionality by using hybridoma technology. In most cases, all the hybridoma clones are produced first and then validated one by one. In contrast, phage display technology allows various enriching strategies, post-translational modification specific antibodies can be enriched thus those without the desired functionality can be excluded from further validation. For example, antibody library screening can be done using the PTM-modified target to capture strong binders while using the unmodified controls to block/deplete cross-reactive binders. In particular, biopanning allows isolation of antibodies of the highest affinity from the immunized animals.
Jensen O N. (2006) “Interpreting the protein language using proteomics”. Nat Rev Mol Cell Biol, 7(6): 391-403.
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