IP Library Granted Patent US 12,398,387
Granted Patent B2
US 12,398,387 · App. 17/629,999 · Granted Aug 26, 2025

Compositions and methods for preparing factor Xa and derivatives

Inventor: Genmin Lu (South San Francisco, CA)
Assignee: Alexion Pharmaceuticals, Inc.
C12N9/6432C07K2319/31C07K2319/50
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Quick Facts
Patent No.
US 12,398,387
App. No.
17/629,999
Granted
Aug 26, 2025
Kind
B2
Abstract

The present disclosure relates to protein sequences which can be used to generate factor Xa proteins and derivatives thereof. The protein sequences include a factor Xa light chain portion, a heavy chain catalytic domain portion, and an activation peptide C-terminal to the heavy chain catalytic domain portion.

Claims (22)

1. A protein comprising the amino acid sequence of formula (I):

LC - L 1- HC - L 2- AP   (I),

wherein:

LC comprises the amino acid sequence that is at least 85% identical to the amino acid sequence of SEQ ID NO:13,

L1 is a peptide linker comprising a protease recognition site,

HC comprises the amino acid sequence that is at least 85% identical to the amino acid sequence of SEQ ID NO:11,

L2 is absent or is a peptide linker that cannot be processed by the protease recognizing the protease recognition site in L1, and

AP is an activation peptide comprising the amino acid sequence that is at least 90% identical to the amino acid sequence of SEQ ID NO: 12; and

wherein, when the L1 is processed by the protease, a two-chain polypeptide comprising the LC and the HC on separate chains is produced, and the two-chain polypeptide binds to a factor Xa (fXa) inhibitor.

2. The protein of claim 1 , wherein the protease is furin.

3. The protein of claim 1 , wherein the L1 comprises the amino acid sequence of RKR or RKRRKR (SEQ ID NO:7).

4. The protein of claim 1 , wherein the L2 is 0-50 amino acid residues in length.

5. The protein of claim 4 , wherein at least 50% of the amino acid residues of L2 is Gly or Ser.

6. The protein of claim 1 , wherein the activation peptide comprises a glycosylation site.

7. The protein of claim 1 , wherein the activation peptide comprises the amino acid sequence of SEQ ID NO: 12.

8. The protein of claim 1 , wherein the protein further comprises human serum albumin (HSA) at the N-terminus of the formula (I).

9. The protein of claim 8 , wherein the LC does not comprise amino acid residues 1-45 of SEQ ID NO:2.

10. The protein of claim 1 , wherein the produced two-chain polypeptide has reduced capacity to assemble into a prothrombin complex as compared to a wild-type fXa.

11. The protein of claim 1 , wherein the LC comprises the amino acid sequence that is at least 90% identical to the amino acid sequence of SEQ ID NO:6.

12. The protein of claim 1 , wherein the produced two-chain polypeptide has reduced catalytic activity as compared to a wild-type fXa.

13. The protein of claim 1 , wherein the HC comprises the amino acid sequence that is at least 90% identical to the amino acid sequence of SEQ ID NO:10.

14. The protein of claim 1 , wherein the HC comprises the amino acid sequence of SEQ ID NO:11.

Assignments (3)
ASSIGNMENT OF ASSIGNOR'S INTEREST Recorded Dec 9, 2024
From: LU, GENMIN
To: PORTOLA PHARMACEUTICALS, LLC
Reel/Frame 069529/0190 →
ASSIGNMENT OF ASSIGNOR'S INTEREST Recorded Dec 9, 2024
From: PORTOLA PHARMACEUTICALS, LLC
To: ALEXION PHARMACEUTICALS, INC.
Reel/Frame 069560/0735 →
CHANGE OF NAME Recorded Dec 9, 2024
From: PORTOLA PHARMACEUTICALS, INC.
To: PORTOLA PHARMACEUTICALS, LLC
Reel/Frame 069561/0097 →
Continuity (3)
Provisional Application 62990885 · Mar 17, 2020
Provisional Application 62884652 · Aug 8, 2019
Related Publication 20220251534A1 · Aug 11, 2022
References Cited (12)
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US 20170240879A1 · Lu et al. · 2017 [cited by applicant]
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WO WO2006128668A2 · 2006 [cited by applicant]
WO WO2009042962A2 · 2009 [cited by applicant]
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WO WO2017147522A1 · 2017 [cited by applicant]
International Search Report and Written Opinion dated Feb. 1, 2021 for PCT/US2020/045039. (16 pages). [cited by applicant]
European Search Report and Opinion dated Nov. 17, 2023 for EP Application No. 20851033.9. 9 pages. [cited by applicant]