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US 2017/0080358 A1Published application
Mutated Immunoglobulin-Binding Protein
AssigneeGE Healthcare BioProcess R&D AB
InventorSophia Hober
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AssigneeGE Healthcare BioProcess R&D 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 two asparagine residues excluding asparagine 21 of a parental immunoglobulin-binding protein defined by SEQ ID NO. 1 or 2 have been mutated to the same or different amino acid residues selected from G, A, V, L, I, S, T, M, F, Y, W, E, R H, or K, which mutations have conferred an increased chemical stability at alkaline pH-values compared to the parental molecule.
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;
Dependencies are inferred from the claim text.