ImmunoFusion Proteins

ImmunoFusion Protein technology takes advantage of the modular structure and long circulating half-lives of human immunoglobulins (antibodies). Company scientists use recombinant DNA methods to covalently fuse therapeutic proteins to the Fc domains of human immunoglobulin gamma proteins (IgGs). IgGs are abundant proteins that have circulating half-lives of up to 21 days in humans. Company scientists have created several cytokine-immunoglobulin fusion proteins that possess the high potency and specificity of their parent cytokine molecules, and the long circulating half-life of the immunoglobulin domain. Our cytokine-immunoglobulin fusion proteins are expressed in mammalian cells as homodimers, covalently joined through disulfide bonds that form between cysteine residues present in the IgG-Fc domains. Dimerization of the fusion proteins increases their effective sizes and lengthens the time they circulate in the body. A number of immunofusion proteins have been approved for use in humans or are currently in human clinical trials. Existing data indicate that immunofusion proteins are safe and largely non-immunogenic in people, despite the fact that they are non-natural proteins.

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