The patent badge is an abbreviated version of the USPTO patent document. The patent badge does contain a link to the full patent document.

The patent badge is an abbreviated version of the USPTO patent document. The patent badge covers the following: Patent number, Date patent was issued, Date patent was filed, Title of the patent, Applicant, Inventor, Assignee, Attorney firm, Primary examiner, Assistant examiner, CPCs, and Abstract. The patent badge does contain a link to the full patent document (in Adobe Acrobat format, aka pdf). To download or print any patent click here.

Date of Patent:
Jul. 07, 2020

Filed:

Nov. 10, 2016
Applicant:

GE Healthcare Bioprocess R&d Ab, Uppsala, SE;

Inventors:

Annika Kristina Forss, Uppsala, SE;

Gustav Jose Rodrigo, Uppsala, SE;

Tomas Bjorkman, Uppsala, SE;

Jesper Ulf Hansson, Uppsala, SE;

Mats Ander, Uppsala, SE;

Assignee:
Attorney:
Primary Examiner:
Int. Cl.
CPC ...
C07K 1/22 (2006.01); B01D 15/00 (2006.01); C07K 16/12 (2006.01); C07K 17/10 (2006.01); B01J 20/286 (2006.01); C07K 14/31 (2006.01); C07K 16/06 (2006.01); B01J 20/32 (2006.01);
U.S. Cl.
CPC ...
C07K 1/22 (2013.01); B01D 15/00 (2013.01); B01J 20/286 (2013.01); B01J 20/3212 (2013.01); B01J 20/3274 (2013.01); C07K 14/31 (2013.01); C07K 16/065 (2013.01); C07K 16/1271 (2013.01); C07K 17/10 (2013.01); B01J 2220/52 (2013.01);
Abstract

The invention relates to a method of isolating an immunoglobulin, comprising the steps of: a) providing a separation matrix comprising multimers of immunoglobulin-binding alkali-stabilized Protein A domains covalently coupled to a porous support, b) contacting a liquid sample comprising an immunoglobulin with the separation matrix, c) washing said separation matrix with a washing liquid, d) eluting the immunoglobulin from the separation matrix with an elution liquid, and e) cleaning the separation matrix with a cleaning liquid, wherein the alkali-stabilized Protein A domains comprise mutants of a parental Fc-binding domain ofProtein A (SpA), as defined by, or having at least 80% such as at least 90%, 95% or 98% identity to, SEQ ID NO 51 or SEQ ID NO 52, wherein the amino acid residues at positions 13 and 44 of SEQ ID NO 51 or 52 are asparagines and wherein at least the asparagine residue at position 3 of SEQ ID NO 51 or 52 has been mutated to an amino acid selected from the group consisting of glutamic acid, lysine, tyrosine, threonine, phenylalanine, leucine, isoleucine, tryptophan, methionine, valine, alanine, histidine and arginine.


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