IP Library Granted Patent US 11,124,539
Granted Patent B2
US 11,124,539 · App. 16/348,534 · Granted Sep 21, 2021

Chromatography resin, production and use thereof

Inventors: Johan William Ohman (Uppsala, SE); Mats Ander (Uppsala, SE); Therese Graner (Uppsala, SE); Anneli Jorsback (Uppsala, SE); Jinyu Zou (Uppsala, SE)
Assignee: Cytiva BioProcess R&D AB
C07K1/22B01D15/3828B01J20/24B01J20/285B01J20/286B01J20/321B01J20/3212B01J20/3217B01J20/3274B01J2220/52C07K2319/20C07K2319/92C07K2319/95
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Quick Facts
Patent No.
US 11,124,539
App. No.
16/348,534
Granted
Sep 21, 2021
Kind
B2
Abstract

The present invention relates to the field of chromatography and more specifically to producing protein affinity chromatography resins comprising affinity ligands based on a N-terminal fragment of a split intein, such as DnaE from Nostoc punctiforme , as well as methods for using the same. The N-terminal fragments are produced in inclusion bodies in bacterial cells.

Claims (18)

1. A method for production of an affinity chromatography resin comprising an N-terminal split intein fragment as an affinity ligand, comprising the following steps:

a) expression of an N-terminal split intein fragment, wherein the N-terminal split intein fragment comprises a sequence selected from SEQ ID NO:s 1-5 or a sequence having at least 95% homology therewith and an Alanine at the fourth position and a Serine at the thirty-first position, as insoluble protein in inclusion bodies in bacterial cells,

b) harvesting said inclusion bodies;

c) solubilizing said inclusion bodies and releasing expressed protein;

d) binding said protein on a solid support;

e) refolding said protein;

f) releasing said protein from the solid support; and

g) immobilizing said protein as ligands on a chromatography resin to form an affinity chromatography resin—wherein the ligand density on said chromatography resin is 5-10 mg ligand/ml resin.

2. The method according to claim 1 , wherein the N-terminal split intein fragment comprises a sequence selected from SEQ ID NO:s 1-5.

3. The method according to claim 1 , wherein said chromatography resin is selected from the group consisting of agarose, polystyrene, methacrylate and cellulose beads.

4. The method according to claim 1 , wherein the immobilization in step g) is by covalent attachment.

5. The method according to claim 1 , wherein said immobilization is preceded by concentration to a protein concentration between 5-30 mg/ml.

6. The method according to claim 1 , wherein the chromatography resin is packed in a column, fluidized bed, porous monolith or capillary bed.

7. The method according to claim 1 , comprising binding of the N-terminal fragment on an ion exchange column in step d).

8. The method according to claim 1 , wherein the N-terminal fragment is tagged, and the solid support in step d) is an IMAC column.

9. The method according to claim 1 , wherein said chromatography resin is agarose beads.

10. The method according to claim 1 , wherein the N-terminal fragment is poly-histidine tagged, and the solid support in step d) is an IMAC column.

11. The method according to claim 1 , wherein the N-terminal split intein fragment a sequence having at least 95% homology to one of SEQ ID NO:s 1-5, an Alanine at the fourth position, a Serine at the thirty-first position, and a Serine at the sixty-second position.

Assignments (2)
CHANGE OF NAME Recorded Oct 5, 2020
From: GE HEALTHCARE BIOPROCESS R&D AB
To: CYTIVA BIOPROCESS R&D AB
Reel/Frame 054299/0349 →
ASSIGNMENT OF ASSIGNOR'S INTEREST Recorded May 9, 2019
From: OHMAN, JOHAN; JORSBACK, ANNELI; ANDER, MATS; GRANER, THERESE; ZOU, JINYU
To: GE HEALTHCARE BIOPROCESS R&D AB
Reel/Frame 049124/0710 →