Naomi L Esmon

7011956, Mar 14, 2006

Sep 26, 2000

10/088021

Naomi L. Esmon - Oklahoma City OK, US

Oklahoma Medical Research Foundation - Oklahoma City OK

C12Q 1/56
G01N 33/86
G01N 33/92

435 13, 436 69, 436 71

An assay to assess thrombotic risk in which oxidized lipids comprising phospholipids are utilized as a membrane source in a clotting assay and the results compared to an assay in which unoxidized phospholipid is used as a membrane source in the presence and absence of activated protein C (“APC”). The assay can monitor for the presence of antibodies in the patient which interfere specifically with the anticoagulant function of APC in an oxidation dependent or independent manner. This can indicate the propensity of the patient to experience episodes of vein thrombosis or arterial thrombosis.

62391011, May 29, 2001

Jan 31, 1991

7/648900

Charles T. Esmon - Oklahoma City OK
Naomi L. Esmon - Oklahoma City OK
Deborah J. Stearns - Tokyo, JP
Shinichiro Kurosawa - Tokyo, JP

Oklahoma Medical Research Foundation - Oklahoma City OK

C07K 14745
A61K 3836
C12N 1512

514 8

Small, buffer soluble polypeptides having amino acid structures corresponding to residues 234-486, 310-486, and 407-486, of thrombomodulin and functionally equivalent analogs thereof inhibiting the clotting activity of thrombin and increasing protein C activation. The polypeptides can be coated onto the surface of articles adapted for contacting mammalian blood to render the surface non-thrombogenic. In pharmaceutical compositions, the polypeptides act as a natural anticoagulant.

53366107, Aug 9, 1994

Nov 30, 1992

7/982832

Charles T. Esmon - Oklahoma City OK
Naomi L. Esmon - Oklahoma City OK

Oklahoma Medical Research Foundation - Oklahoma City OK

C12N 948
C07K 320
C07K 1528

435212

A Ca. sup. 2+ dependent monoclonal antibody that specifically binds to a specific twelve peptide sequence (E D Q V D P R L I D G K) in the activation region of the Protein C. The antibody does not bind to Activated Protein C and can be used to inhibit activation of Protein C by thrombin-thrombomodulin. The antibody can be isolated from cell culture or ascites fluid in large quantities by affinity chromatography with mild conditions using the peptide bound to an immobilized substrate. The antibody has a number of specific uses in isolation and characterization of Protein C and as a model for the design of Ca. sup. 2+ dependent antibodies for the isolation of other proteins, as a diagnostic, and as a therapeutic to prevent activation of Protein C. The Protein C can be naturally produced or produced by expression of the recombinant gene. Advantages of the antibody in purification of Protein C include the specificity for Protein C and not Activated Protein C, and the unique Ca. sup.

52022536, Apr 13, 1993

Jul 12, 1991

7/730040

Charles T. Esmon - Oklahoma City OK
Naomi L. Esmon - Oklahoma City OK

Oklahoma Medical Research Foundation - Oklahoma City OK

C12N 520
C12N 1502
C07K 1528
C07K 320

43524027

A Ca. sup. 2+ dependent monoclonal antibody that specifically binds to a specific twelve peptide sequence (E D Q V D P R L I D G K) in the activation region of the Protein C. The antibody does not bind to Activated Protein C and can be used to inhibit activation of Protein C by thrombin-thrombomodulin. The antibody can be isolated from cell culture or ascites fluid in large quantities by affinity chromatography with mild conditions using the peptide bound to an immobilized substrate. The antibody has a number of specific uses in isolation and characterization of Protein C and as a model for the design of Ca. sup. 2+ dependent antibodies for the isolation of other proteins, as a diagnostic, and as a therapeutic to prevent activation of Protein C. The Protein C can be naturally produced or produced by expression of the recombinant gene. Advantages of the antibody in purification of Protein C include the specificity for Protein C and not Activated Protein C, and the unique Ca. sup.