IP Library › Granted Patent US 12686702
Granted Patent B2
US 12686702 · App. 17/978,791 · Granted Jul 21, 2026

Methods for purifying antibodies

Inventors: Andre C. Dumetz (King of Prussia, PA); Kent E. Goklen (King of Prussia, PA); Nicholas E. Levy (King of Prussia, PA); Jessica Rachel Molek (King of Prussia, PA); Andrew S. Thomson (Collegeville, PA); Kenneth G. Yancey (Wayne, PA)
Assignee: GlaxoSmithKline Intellectual Property Development Limited
C07K1/22B01D15/3809B01D15/424C07K16/065
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Quick Facts
Patent No.
US 12686702
App. No.
17/978,791
Granted
Jul 21, 2026
Kind
B2
Abstract

The present invention relates to a method of purifying a recombinant polypeptide from Host Cell Proteins (HCP), the method comprising: (a) applying a solution comprising the recombinant polypeptide and HCP to a superantigen chromatography solid support, (b) washing the superantigen chromatography solid support with a wash buffer comprising caprylate and arginine; and (c) eluting the recombinant polypeptide from the superantigen chromatography solid support.

Claims (19)

1 . A method of purifying a recombinant polypeptide from Host Cell Proteins (HCP), the method comprising:

(a) applying a solution comprising the recombinant polypeptide and HCP to a superantigen chromatography solid support,

(b) washing the superantigen chromatography solid support with a wash buffer comprising about 100 mM to about 300 mM caprylate, about 0.75 M to about 1.5 M arginine, about 1 mM to about 500 mM Tris base and about 1 mM to about 500 mM acetic acid, wherein the pH of the wash buffer is about 7.5 to about 8.5; and

(c) eluting the recombinant polypeptide from the superantigen chromatography solid support,

wherein the superantigen chromatography solid support is a chromatography solid support having a superantigen immobilized therein, and wherein the superantigen is selected from the group consisting of Protein A, Protein G, and Protein L.

2 . The method according to claim 1 , wherein the wash buffer comprises about 100 mM caprylate.

3 . The method according to claim 1 , wherein the wash buffer comprises about 1.5 M about 1.1 M arginine.

4 . The method according to claim 1 , wherein the wash buffer further comprises about 0.5 M to about 1 M lysine.

5 . The method according to claim 1 , wherein the eluted recombinant polypeptide contains less than about 2% fragmented recombinant polypeptide.

6 . The method according to claim 1 , wherein the HCP is derived from a mammalian cell.

7 . The method according to claim 1 , wherein the HCP is phospholipase B-Like 2 protein.

8 . The method according to claim 1 , wherein the HCP is cathepsin L.

9 . The method according to claim 8 , wherein the purification of the recombinant polypeptide from cathepsin L is measured by a reduced cathepsin L activity in the eluate of step (c).

10 . The method according to claim 1 , wherein the recombinant polypeptide is a monoclonal antibody (mAb).

11 . The method according to claim 10 , wherein the mAb is an IgG1, or an IgG4.

12 . The method according to claim 1 , wherein the wash buffer does not contain sodium chloride.

13 . The method according to claim 1 , wherein the superantigen is Protein A.

14 . The method according to claim 1 , wherein after step (c) the amount of HCP is less than about 200 ng HCP/mg product.

15 . The method according to claim 1 , wherein the wash buffer comprises 55 mM Tris base, 45 mM acetic acid, 100 mM sodium caprylate, and 1.1 M arginine, and wherein the pH of the wash buffer is pH 7.5.