Creative BioMart has become leading manufacturer of protein products for life science research. One of our specialties is to develop unique immunoglobulin based chimeric fusion proteins utilizing cellular and molecular biology techniques.
Due to the nature of the antibody IgG-Fc, Fc fusion proteins play significant role in dimerization, in vivo half-life, receptor activation and ligand affinity. Considering many receptors are only bio-functional as dimeric form, a Fc fusion receptor protein can mimic the activated form and enhance its affinity to ligand. Besides, Fc domain also simplifies its detection (by western blot or ELISA) & purification (by protein A or protein G affinity chromatography) steps. Mammalian cell-specific glycosylation from the Fc domain of the protein also makes itself suitable for in vivo studies. If desired, the Fc domain can be cleaved by treatment with protease.
In the biopharmaceutical industry, as novel biological entities with potential for therapeutic activities, Fc-fusion proteins have become a class of biologic medicines for human disease. In some cases, these fusions are used as standalone therapeutic modalities; in others, they have provided alternatives when therapeutic monoclonal antibodies (mAbs) or other medications have failed to provide successful therapeutic results. There are several reasons that Fc domains have been chosen for fusion to polypeptides for therapeutic applications:
Creative BioMart helps scientists to develop recombinant Fc fusion proteins for research and pharmaceutical purposes.
The Fc options include but are not limited to:
|1||Gene synthesis plus codon optimization||1-2 weeks||
|2||Clone target gene into expression vector||1 week|
|3||Transfect competent cells with transfer vector||1week|
|4||Protein expression and purification||2-4 weeks|
|5||Optional services (secondary purification, endotoxin removal, protein labeling, activity assay, protein analysis, etc.)||1-2 weeks|
|6||Quality Control||<1 weeks|
Steven M. Chamow, et al. Therapeutic Fc-Fusion Proteins. ISBN: 978-3-527-33317-2. February 2014, Wiley-Blackwell. Page224 Figure 8.1
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