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US 2016/0152668 A1Published application
Mutated Immunoglobulin-Binding Protein
AssigneeGE Healthcare Bio-Sciences AB
InventorSophia Hober
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AssigneeGE Healthcare Bio-Sciences AB
InventorSophia Hober
Estimating the term…
The present invention relates to an immunoglobulin-binding protein, wherein at least one asparagine residue has been mutated to an amino acid other than glutamine or aspartic acid, which mutation confers an increased chemical stability at pH-values of up to about 13-14 compared to the parental molecule. The protein can for example be derived from a protein capable of binding to other regions of the immunoglobulin molecule than the complementarity determining regions (CDR), such as protein A, and preferably the B-domain of Staphylococcal protein A. The invention also relates to a matrix for affinity separation, which comprises an immunoglobulin-binding protein as ligand coupled to a solid support, in which protein ligand at least one asparagine residue has been mutated to an amino acid other than glutamine.
A matrix for affinity chromatography, comprising a plurality of ligands coupled to a solid support, wherein the ligands comprise an immunoglobulin-binding protein, or multimer thereof, capable of binding to other regions of the immunoglobulin molecule than the complementarity determining regions (CDR), wherein at least the asparagine residue at position 6 or 11 of a parental immunoglobulin-binding protein defined by SEQ ID NO. 1 or 2 has been mutated to an amino acid other than glutamine, which mutation has conferred an increased chemical stability at alkaline pH-values compared to the parental molecule.
Dependencies are inferred from the claim text.