IP Library › Granted Patent US 12,152,085
Granted Patent B2
US 12,152,085 · App. 17/739,691 · Granted Nov 26, 2024

Compositions and methods to regulate Renalase in the treatment of cancer

Inventors: Gary Desir (Woodbridge, CT); Abigail Hunt (Alameda, CA); Jessica O-Rear (Redwood City, CA); Peter Flynn (San Francisco, CA)
Assignee: Yale University
C07K16/40A61K39/39558C12Y106/03G01N33/573A61K2039/505C07K2317/34C07K2317/51C07K2317/515C07K2317/565C07K2317/73C07K2317/76C07K2317/92G01N2333/90209
View Patent ↗
Loading inventors, assignments & file history…
Monitor This Case
Get email alerts when status or documents change.
Order Certified Copies
Most orders are placed with the USPTO same day — all within 24 business hours.
Order via The Patent Place →
Pre-filled with this patent's details
Quick Facts
Patent No.
US 12,152,085
App. No.
17/739,691
Granted
Nov 26, 2024
Kind
B2
Abstract

The invention provides compositions and methods for binding and inhibiting renalase. In one embodiment, the renalase binding molecule inhibits renalase activity. Thus, in diseases and conditions where a reduction of renalase activity is beneficial, such inhibitory renalase binding molecules act as therapeutics.

Claims (11)

1. A composition comprising an isolated monoclonal antibody, wherein the antibody is selected from the group consisting of:

a) an antibody comprising the heavy chain CDR1 sequence of SEQ ID NO:27; the heavy chain CDR2 sequence of SEQ ID NO:28; the heavy chain CDR3 sequence of SEQ ID NO:29; the light chain CDR1 sequence of SEQ ID NO: 30; the light chain CDR2 sequence of SEQ ID NO:31; and the light chain CDR3 sequence of SEQ ID NO:32; and

b) an antibody comprising the heavy chain CDR1 sequence of SEQ ID NO:43; the heavy chain CDR2 sequence of SEQ ID NO:44; the heavy chain CDR3 sequence of SEQ ID NO:45; the light chain CDR1 sequence of SEQ ID NO: 46; the light chain CDR2 sequence of SEQ ID NO:47; and the light chain CDR3 sequence of SEQ ID NO:48.

2. The composition of claim 1 , wherein the antibody specifically binds to renalase with an affinity of at least 10 −6 M.

3. The composition of claim 1 , wherein the antibody is selected from the group consisting of an immunoconjugate, a defucosylated antibody, and a bispecific antibody.

4. The composition of claim 3 , wherein the immunoconjugate comprises a therapeutic agent or a detection moiety.

5. The composition of claim 1 , wherein the antibody is selected from the group consisting of a humanized antibody, a chimeric antibody, a fully human antibody, and an antibody mimetic.

6. The composition of claim 1 , wherein the antibody of a) comprises the heavy chain sequence as set forth in SEQ ID NO:25.

7. The composition of claim 1 , wherein the antibody of a) comprises the light chain sequence as set forth in SEQ ID NO:26.

8. The composition of claim 1 , wherein the antibody of b) comprises the heavy chain sequence as set forth in SEQ ID NO:41.

9. The composition of claim 1 , wherein the antibody of b) comprises the light chain sequence as set forth in SEQ ID NO:42.

Assignments (1)
ASSIGNMENT OF ASSIGNOR'S INTEREST Recorded Jul 12, 2023
From: DESIR, GARY; HUNT, ABIGAIL; O-REAR, JESSICA; FLYNN, PETER
To: YALE UNIVERSITY
Reel/Frame 064229/0944 →
Continuity (5)
Division 16847964 · Apr 14, 2020
Division 16295084 · Mar 7, 2019
Division 15321015
Provisional Application 62017487 · Jun 26, 2014
Related Publication 20220281996A1 · Sep 8, 2022