DETAILED ACTION
Notice of Pre-AIA or AIA Status
The present application, filed on or after March 16, 2013, is being examined under the first inventor to file provisions of the AIA .
Claim Status
Claims 1-4, 6-8, 12-18, 20, 23, 25, 27, 30, and 60 are pending under examination
Priority
This application is a 371 of PCT/IB2022/055391, filed 06/09/2022. This application claims priority to and the benefit of U.S. Provisional Application No. 63/208,929, filed June 9, 2021
Information Disclosure Statement
IDS submitted on 04/28/2025 and 05/15/2026 were reviewed.
The listing of references in the specification is not a proper information disclosure statement. 37 CFR 1.98(b) requires a list of all patents, publications, or other information submitted for consideration by the Office, and MPEP § 609.04(a) states, "the list may not be incorporated into the specification but must be submitted in a separate paper." Therefore, unless the references have been cited by the examiner on form PTO-892, they have not been considered.
Nucleotide and/or Amino Acid Sequence Disclosures
REQUIREMENTS FOR PATENT APPLICATIONS CONTAINING NUCLEOTIDE AND/OR AMINO ACID SEQUENCE DISCLOSURES
Items 1) and 2) provide general guidance related to requirements for sequence disclosures.
37 CFR 1.821(c) requires that patent applications which contain disclosures of nucleotide and/or amino acid sequences that fall within the definitions of 37 CFR 1.821(a) must contain a "Sequence Listing," as a separate part of the disclosure, which presents the nucleotide and/or amino acid sequences and associated information using the symbols and format in accordance with the requirements of 37 CFR 1.821 - 1.825. This "Sequence Listing" part of the disclosure may be submitted:
In accordance with 37 CFR 1.821(c)(1) via the USPTO patent electronic filing system (see Section I.1 of the Legal Framework for Patent Electronic System (https://www.uspto.gov/PatentLegalFramework), hereinafter "Legal Framework") as an ASCII text file, together with an incorporation-by-reference of the material in the ASCII text file in a separate paragraph of the specification as required by 37 CFR 1.823(b)(1) identifying:
the name of the ASCII text file;
ii) the date of creation; and
iii) the size of the ASCII text file in bytes;
In accordance with 37 CFR 1.821(c)(1) on read-only optical disc(s) as permitted by 37 CFR 1.52(e)(1)(ii), labeled according to 37 CFR 1.52(e)(5), with an incorporation-by-reference of the material in the ASCII text file according to 37 CFR 1.52(e)(8) and 37 CFR 1.823(b)(1) in a separate paragraph of the specification identifying:
the name of the ASCII text file;
the date of creation; and
the size of the ASCII text file in bytes;
In accordance with 37 CFR 1.821(c)(2) via the USPTO patent electronic filing system as a PDF file (not recommended); or
In accordance with 37 CFR 1.821(c)(3) on physical sheets of paper (not recommended).
When a “Sequence Listing” has been submitted as a PDF file as in 1(c) above (37 CFR 1.821(c)(2)) or on physical sheets of paper as in 1(d) above (37 CFR 1.821(c)(3)), 37 CFR 1.821(e)(1) requires a computer readable form (CRF) of the “Sequence Listing” in accordance with the requirements of 37 CFR 1.824.
If the "Sequence Listing" required by 37 CFR 1.821(c) is filed via the USPTO patent electronic filing system as a PDF, then 37 CFR 1.821(e)(1)(ii) or 1.821(e)(2)(ii) requires submission of a statement that the "Sequence Listing" content of the PDF copy and the CRF copy (the ASCII text file copy) are identical.
If the "Sequence Listing" required by 37 CFR 1.821(c) is filed on paper or read-only optical disc, then 37 CFR 1.821(e)(1)(ii) or 1.821(e)(2)(ii) requires submission of a statement that the "Sequence Listing" content of the paper or read-only optical disc copy and the CRF are identical.
Specific deficiencies and the required response to this Office Action are as follows:
Specific deficiency – Nucleotide and /or amino acid sequences appearing in the claim or specification are not identified by sequence identifiers in accordance with 37 CFR 1.821(d).
Required response – Applicant must provide:
A substitute specification in compliance with 37 CFR 1.52, 1.121(b)(3) and 1.125 inserting the required sequence identifiers, consisting of:
A copy of the previously-submitted specification, with deletions shown with strikethrough or brackets and insertions shown with underlining (marked-up version);
A copy of the amended specification without markings (clean version); and
A statement that the substitute specification contains no new matter.
Specific deficiency - Sequences appearing in the claim or specification are not identified by sequence identifiers (i.e., “SEQ ID NO:X” or the like) in accordance with 37 CFR 1.831(c).
Required response – Applicant must provide:
A substitute specification in compliance with 37 CFR 1.52, 1.121(b)(3), and 1.125 inserting the required sequence identifiers, consisting of:
• A copy of the previously-submitted specification, with deletions shown with strikethrough or brackets and insertions shown with underlining (marked-up version);
• A copy of the amended specification without markings (clean version); and
• A statement that the substitute specification contains no new matter.
Claim Rejections - 35 USC § 102
In the event the determination of the status of the application as subject to AIA 35 U.S.C. 102 and 103 (or as subject to pre-AIA 35 U.S.C. 102 and 103) is incorrect, any correction of the statutory basis (i.e., changing from AIA to pre-AIA ) for the rejection will not be considered a new ground of rejection if the prior art relied upon, and the rationale supporting the rejection, would be the same under either status.
The following is a quotation of the appropriate paragraphs of 35 U.S.C. 102 that form the basis for the rejections under this section made in this Office action:
A person shall be entitled to a patent unless –
(a)(1) the claimed invention was patented, described in a printed publication, or in public use, on sale, or otherwise available to the public before the effective filing date of the claimed invention.
(a)(2) the claimed invention was described in a patent issued under section 151, or in an application for patent published or deemed published under section 122(b), in which the patent or application, as the case may be, names another inventor and was effectively filed before the effective filing date of the claimed invention.
Claims 1, 2, and 12 are rejected under 35 U.S.C. 102(a)(1) as being anticipated by Geisbert et. al. (“Treatment of Ebola virus infection with a recombinant inhibitor of factor VIIa/tissue factor: a study in rhesus monkeys”, Thomas W Geisbert, Lisa E Hensley, Peter B Jahrling, Tom Larsen, Joan B Geisbert, Jason Paragas, Howard A Young, Terry M Fredeking, William E Rote, George P Vlasuk, THE LANCET, Vol 362, page 1953-1957, published December 13, 2003).
For claim 1, Geisbert et. al. teaches activation of coagulation and inflammation during severe infection is linked….cytokines are involved in the procoagulant state that follows endotoxaemia or severe infection; results of studies have shown that activated coagulation factors in turn are capable of eliciting a proinflammatory response (see page 1957, left col, 2nd paragraph). Geisbert et. al. investigated the cytokine and chemokine responses of rNAPc2-treated monkeys versus untreated controls, since many of these inflammatory mediators can play an important part in the interaction between coagulation and systemic inflammation during infections (see page 1957, left col, 2nd paragraph). Geisbert et. al. disclosed that survival of rNAPc2-treated macaques was associated with reduced activation of coagulation and fibrinolysis, and with attenuation of the systemic proinflammatory response (see Discussion 1st paragraph, page 1957). Geisbert et. al. further teaches rNAPc2 has a suitable pharmacokinetic and safety profile in human beings (see Discussion 2nd paragraph, page 1957).
For claim 2, Geisbert et. al. administered recombinant nematode anticoagulant protein c2 (rNAPc2), a potent inhibitor of tissue factor-initiated blood coagulation (see Methods, page 1953). Geisbert et. al. further specifies regarding treatment by subcutaneous injections of rNAPc2 (30 _µg/kg bodyweight, once daily) (see Treatment and Investigations 1st paragraph, page 1954).
For claim 12, Geisbert et. al. discloses the elimination half-life of rNAPc2 in nonhuman primates is about 18–20 h shorter than in people; therefore, administered the drug daily instead of every other day as was done in the clinical studies (see Treatment and Investigations 2nd paragraph, page 1954).
Claims 6, 3, 4, 7, 13-18, 20, and 23 are rejected under 35 U.S.C. 102 (a)(1) and 102(a)(2) as being anticipated by WO9612021 (published April 25, 1996; cited in IDS filed 04/28/2025).
For claim 6, WO’021 discloses the antithrombotic (prevention of thrombus formation) properties of NAP were evaluated using the established experimental rat model of acute vascular thrombosis (see page 135, line 10-12).
This is in direct correlation with the instant specification which states “In some embodiments, the subject was diagnosed with an autoimmune or inflammatory condition. The subject may be or have been diagnosed with the autoimmune or inflammatory condition by any means known in the art. In some embodiments, the subject was determined to have one or more symptoms of an autoimmune or inflammatory condition. A symptom of an autoimmune or inflammatory condition may be, for example, fatigue, skin lesions, rash, fever, thrombosis (e.g., venous thrombosis, pulmonary embolism)” (see [0009]).
For claim 3, WO’021 encode a NAP protein that incorporates a proline residue at the C-terminus (see Example 17).
For claim 4, WO’021 teaches NAP proteins that inhibit the serine protease trypsin or elastase are useful for treatment of acute inflammatory response mediated by leukocytes (see page 71, line 23-26).
For claim 7, WO’021 discloses that according to an alternate aspect of our invention, the proteins of the present invention are also useful as pharmaceutical agents for preventing or inhibiting thrombosis or blood coagulation in a mammal (see page 70, line 9-12).
For claims 13-17, WO’021 teaches the proteins of the present invention, alone or as part of a pharmaceutical composition, such doses are between about 0.01 mg/kg and 100 mg/kg body weight, preferably between about 0.01 and 10 mg/kg, body weight (page 68, line 5-9). The efficacy of AcaNAPS as an antithrombotic agent in preventing thrombus formation in the in vivo model was demonstrated by the dose-dependent reduction in the incidence of thrombotic occlusion, ranging from 0.001 mg/kg, 0.003 mg/kg, 0.01 mg/kg, 0.03 mg/kg, 0.1 mg/kg, 0.3 mg.kg, and 1.0 mg/kg (see Table 7, page 137) (Dose equivalent to 1 µg/kg, 3 µg/kg, 10 µg/kg, 30 µg/kg, etc.) WO’021 further specifies that administration is preferably parenteral, such as intravenous on a daily basis. Alternatively, administration is preferably oral, such as by tablets, capsules or elixers taken on a daily basis (see page 67, line 17-20).
As instantly claimed, NAPc2 or NAPc2/proline is administered at a dose of between 5 µg/kg and 10 µg/kg; at a dose of about 7.5 µg/kg. Prior art range fully overlaps and is broader than claimed range.
For claim 18, WO’021 lists the inhibition of the amidolytic activity of FXa and 10 additional serine proteases by either recombinant NAPc2. These NAPs demonstrate a high degree of specificity for the inhibition of FXa compared to the other, related serine proteases (page 128-129, line 33-40, Table 4). WO’021 teaches in practicing these methods, the proteins or pharmaceutical compositions of the present invention are administered alone or in combination with one another, or in combination with other therapeutic or in vivo diagnostic agents (page 67, line 21-25).
Claim Rejections - 35 USC § 103
In the event the determination of the status of the application as subject to AIA 35 U.S.C. 102 and 103 (or as subject to pre-AIA 35 U.S.C. 102 and 103) is incorrect, any correction of the statutory basis (i.e., changing from AIA to pre-AIA ) for the rejection will not be considered a new ground of rejection if the prior art relied upon, and the rationale supporting the rejection, would be the same under either status.
The following is a quotation of 35 U.S.C. 103 which forms the basis for all obviousness rejections set forth in this Office action:
A patent for a claimed invention may not be obtained, notwithstanding that the claimed invention is not identically disclosed as set forth in section 102, if the differences between the claimed invention and the prior art are such that the claimed invention as a whole would have been obvious before the effective filing date of the claimed invention to a person having ordinary skill in the art to which the claimed invention pertains. Patentability shall not be negated by the manner in which the invention was made.
The factual inquiries for establishing a background for determining obviousness under 35 U.S.C. 103 are summarized as follows:
1. Determining the scope and contents of the prior art.
2. Ascertaining the differences between the prior art and the claims at issue.
3. Resolving the level of ordinary skill in the pertinent art.
4. Considering objective evidence present in the application indicating obviousness or nonobviousness.
Claims 20, 23, 25, and 27 are rejected under 35 U.S.C. 103 as being unpatentable over Cohen et. al. (“Rivaroxaban in antiphospholipid syndrome (RAPS) protocol: a prospective, randomized controlled phase II/III clinical trial of rivaroxaban versus warfarin in patients with thrombotic antiphospholipid syndrome, with or without SLE”; H Cohen, C J Doré, S Clawson, B J Hunt, D Isenberg, M Khamashta, N Muirhead; RAPS Trial Protocol Collaborators, Lupus 2015 Sep;24(10):1087-94; published May 4, 2015; cited in IDS filed 04/28/2025) in view of Bergum et. al. (“Role of zymogen and activated factor X as scaffolds for the inhibition of the blood coagulation factor VIIa-tissue factor complex by recombinant nematode anticoagulant protein c2”; P W Bergum, A Cruikshank, S L Maki, C R Kelly, W Ruf, G P Vlasuk; J Biol Chem. 2001 Mar 30;276(13):10063-71; published January 3, 2001; cited in IDS filed 04/28/2025).
Cohen et. al. teaches a method for treating a subject for autoimmune condition (antiphospholipid syndrome or APS), which is an acquired autoimmune disorder characterized by venous and/or arterial thromboembolism associated with persistent antiphospholipid antibodies (see Introduction, page 1087, 1st paragraph). APS may occur alone, or with another autoimmune disease (see page 1088, left col, 1st paragraph). Patients with systemic lupus erythematosus (SLE) develop thrombotic APS, which is considered to be a major prognostic factor in patients with SLE (see page 1088, left col, 1st paragraph).
Cohen et. al. demonstrates in patients with APS, with or without systemic lupus erythematosus (SLE), the intensity of anticoagulation achieved with rivaroxaban (see Introduction); and anti-factor Xa assays in the patients on rivaroxaban (see page 1091, left col, 3rd paragraph). Rivaroxaban have very specific targets (factor Xa); and it is possible that autoimmune antiphospholipid antibodies (aPL) could directly interfere with the anticoagulant action of rivaroxaban, although this is unlikely as rivaroxaban is a small molecule with high affinity for its specific target (see page 1091-1092, Discussion, 3rd paragraph). Cohen et. al. demonstrated the method comprising administering to the subject a therapeutically effective amount of composition comprising anti-Factor Xa anticoagulant, however, does not explicitly teach about Factor Xa inhibitor comprising nematode anticoagulant protein c2 (NAPc2).
Bergum et. al. discloses recombinant nematode anticoagulant protein c2 (rNAPc2) is a potent, factor Xa (fXa)-dependent small protein inhibitor of factor VIIa-tissue factor (fVIIa-TF), which binds to a site on fXa that is distinct from the catalytic center (exo-site) (see Abstract). Bergum et. al, teaches the exposure of tissue factor to circulating blood is the triggering event that results in the formation of a catalytic complex (fVIIa-TF) that initiates the amplified cascade of proteolytic events leading to the formation of the serine protease thrombin (see page 10063, right col, 1st paragraph). The serine protease factor VIIa (fVIIa)1 present in the blood specifically binds to tissue factor, a transmembrane receptor glycoprotein bound to subendothelial structures or present on the surface of monocytic or other inflammatory cells (see page 10063, left col, 1st paragraph). Bergum et. al. characterizes the interaction of rNAPc2 with fX derivatives that support inhibition of fVIIa-TF (see page 10064, left col, 2nd paragraph). Overall, Bergum et. al data support a mechanism of fVIIa-TF inhibition by rNAPc2, which utilizes an exo-site of either the product of this catalytic complex, fXa (see page 10064, left col, 2nd paragraph).
The underlying mechanism of treatment comprising NAPc2 is in direct correlation with the instant application which specifies, “as used herein, NAPc2, (SEQ ID NO: 1), "rNAPc2" describes a recombinant NAPc2 protein rNAPc2 is understood to inhibit the activity of the TF:Factor (F) VIIa complex that initiates the TF pathway in coagulation, and other key pathways, through the formation of a quaternary complex following binding to zymogen FX” (see [0053]).
It would have been obvious to one of ordinary skill in the art before the effective filling date of the claimed invention to modify the method of treatment proposed by Cohen et. al. to further comprise administering the composition comprising nematode anticoagulant protein c2 (NAPc2) from the teachings of Bergum et. al. One of ordinary skill in the art would have been motivated to utilize the said method of treatment administering NAPc2 anticoagulant protein with a reasonable expectation of success because the overall anticoagulant potency of rNAPc2, results from a coordinated recognition of an exo-site on fX/fXa (see Abstract); the unique properties of rNAPc2 …offer future opportunities in gaining a better understanding of the mechanistic details of fVIIa-TF-mediated initiation of blood coagulation; …a possible new approach to clinical anticoagulant therapy (see page 10071, left col, last paragraph).
Regarding claim 25, Cohen et. al. teaches antiphospholipid syndrome (APS) is an acquired autoimmune disorder (see Introduction, page 1087, 1st paragraph). Patients with thrombotic APS with or without systemic lupus erythematosus, who have had either a single episode of venous thromboembolism (see Study Design, Inclusion criteria, page 1089) were included in the study by Cohen et. al.
Regarding claim 27, Cohen et. al. teaches antiphospholipid syndrome (APS) is an acquired autoimmune disorder characterized by venous and/or arterial thromboembolism associated with persistent antiphospholipid antibodies (see Introduction, page 1087, 1st paragraph).
Regarding claims 20 and 23, Cohen et. al teaches patients with thrombotic APS, with or without SLE, who have had either a single episode of venous thromboembolism whilst not on anticoagulation or recurrent episode(s) which occurred whilst off anticoagulation or on sub-therapeutic anticoagulant therapy (see Methods, Inclusion Criteria, point 1, page 1089).
A person skilled in the art could have easily conceived of optimizing the administration conditions of NAPc2 and with or without an additional drug with the expectation of remarkable effect. Therefore, before the effective filing date of the claimed invention, the claimed invention was prima facie obvious to the artisan of ordinary skill.
Therefore, the presently claimed invention was prima facie obvious to one of ordinary skill in the art at the time of the effective filing date.
Claims 8 and 30 are rejected under 35 U.S.C. 103 as being unpatentable over Cohen et. al. (“Rivaroxaban in antiphospholipid syndrome (RAPS) protocol: a prospective, randomized controlled phase II/III clinical trial of rivaroxaban versus warfarin in patients with thrombotic antiphospholipid syndrome, with or without SLE”; H Cohen, C J Doré, S Clawson, B J Hunt, D Isenberg, M Khamashta, N Muirhead; RAPS Trial Protocol Collaborators, Lupus 2015 Sep;24(10):1087-94; published May 4, 2015; cited in IDS filed 04/28/2025) in view of Bergum et. al. (“Role of zymogen and activated factor X as scaffolds for the inhibition of the blood coagulation factor VIIa-tissue factor complex by recombinant nematode anticoagulant protein c2”; P W Bergum, A Cruikshank, S L Maki, C R Kelly, W Ruf, G P Vlasuk; J Biol Chem. 2001 Mar 30;276(13):10063-71; published January 3, 2001; cited in IDS filed 04/28/2025) and WO9612021 (published April 25, 1996; cited in IDS filed 04/28/2025).
Regarding claim 8, the teachings of Cohen et. al, Bergum et. al, and WO’021 are stated above. A person skilled in the art could have easily conceived of optimizing the administration conditions of NAPc2 and using an additional drug with the expectation of remarkable effect. Therefore, before the effective filing date of the claimed invention, the claimed invention was prima facie obvious to the artisan of ordinary skill.
Regarding claim 30, the teachings of Cohen et. al, Bergum et. al, and WO’021 are stated above. Additionally, WO’021 teaches the presence of secreted AcaNAPc2/proline in the growth media was detected by the prolongation of the coagulation time of human plasma (see Example 17B).
A person skilled in the art could have easily conceived of optimizing the administration conditions of NAPc2 and additional administer NAPc2/proline with the expectation to enhance the overall anticoagulant potency. Therefore, before the effective filing date of the claimed invention, the claimed invention was prima facie obvious to the artisan of ordinary skill.
Therefore, the presently claimed invention was prima facie obvious to one of ordinary skill in the art at the time of the effective filing date.
Claim 60 is rejected under 35 U.S.C. 103 as being unpatentable over Bergum et. al. (“Role of zymogen and activated factor X as scaffolds for the inhibition of the blood coagulation factor VIIa-tissue factor complex by recombinant nematode anticoagulant protein c2”; P W Bergum, A Cruikshank, S L Maki, C R Kelly, W Ruf, G P Vlasuk; J Biol Chem. 2001 Mar 30;276(13):10063-71; published January 3, 2001; cited in IDS filed 04/28/2025) in view of Artim-Esen et. al. (“Factor Xa Mediates Calcium Flux in Endothelial Cells and is Potentiated by Igg From Patients With Lupus and/or Antiphospholipid Syndrome”; Bahar Artim-Esen, Natalia Smoktunowicz, Thomas McDonnell, Vera M Ripoll, Charis Pericleous, Ian Mackie, Eifion Robinson, David Isenberg, Anisur Rahman, Yiannis Ioannou, Rachel C Chambers, Ian Giles; Sci Rep. 2017 Sep 7;7(1):10788; published September 7, 2017; cited in IDS filed 04/28/2025).
Bergum et. al. teaches the exposure of tissue factor to circulating blood is the triggering event that results in the formation of a catalytic complex (fVIIa-TF) that initiates the amplified cascade of proteolytic events leading to the formation of the serine protease thrombin (see page 10063, right col, 1st paragraph). The serine protease factor VIIa (fVIIa)1 present in the blood specifically binds to tissue factor, a transmembrane receptor glycoprotein bound to subendothelial structures or present on the surface of monocytic or other inflammatory cells (see page 10063, left col, 1st paragraph). Bergum et. al. teaches the pathway leading from the formation of the fVIIa-TF complex to thrombin proceeds through the serine protease factor Xa (fXa). Factor Xa is formed by the proteolytic activation of the zymogen factor X (fX) either by the fVIIa-TF complex or by the catalytic complex composed of the serine protease factor IXa and its nonenzymatic cofactor factor VIIIa assembled on an appropriate phospholipid surface. Factor Xa catalyzes the formation of thrombin following assembly into a macromolecular catalytic complex (prothrombinase) with the nonenzymatic cofactor factor Va (fVa) that binds to a procoagulant phospholipid surface, such as activated platelets or inflammatory cells (see page 10063, right col, 2nd paragraph).
Bergum et. al. characterizes the interaction of rNAPc2 with fX derivatives that support inhibition of fVIIa-TF (see page 10064, left col, 2nd paragraph). Overall, Bergum et. al. data support a mechanism of fVIIa-TF inhibition by rNAPc2, which utilizes an exo-site of either the product of this catalytic complex, fXa (see page 10064, left col, 2nd paragraph). Bergum et al teaches rNAPc2 quantitatively binds to circulating fX, when administered to humans (see Discussion, page 10069, right col, 1s paragraph).
However, Bergum et. al. fails to explicitly disclose administering to the cell an effective amount of NAPc2.
Artim-Esen et. al. teaches thrombin reactive IgG were significantly elevated in patients with antiphospholipid syndrome (APS) and in patients with systemic lupus erythematosus (SLE) who were antiphospholipid antibodies (aPL) positive but lacked APS (SLE/aPL+) compared to healthy controls. Furthermore, IgG purified from patients with APS displayed higher avidity for thrombin, and significantly inhibited antithrombin-III inactivation of thrombin compared with IgG from SLE/aPL+ (without APS) and healthy control subjects (page 2, 2nd paragraph). Artim-Esen et. al, specifies about use of thrombotic APS compared with non-thrombotic APS, thrombosis without APS and healthy controls (see page 10, 7th paragraph); the effects of aFXa IgG upon FXa mediated EC signalling pathways were tested by incubating aFXa IgG with or without FXa before stimulating HUVEC (cells) (see Measurement of intracellular signalling, page 12, 2nd paragraph).
It would have been obvious to one of ordinary skill in the art before the effective filling date of the claimed invention to modify the inhibiting method of by Bergum et. al. to further comprise administering to the said cell the NAPc2 of Artim-Esen et. al. The motivation would have been to conduct said method for the clinical administration of a NAPc2 anticoagulant protein.
One of ordinary skill in the art would have been motivated to utilize the method of treatment administering NAPc2 anticoagulant protein as taught by Bergum et. al. the overall anticoagulant potency of rNAPc2, results from a coordinated recognition of an exo-site on fX/fXa (see Abstract); the unique properties of rNAPc2 …offer future opportunities in gaining a better understanding of the mechanistic details of fVIIa-TF-mediated initiation of blood coagulation; …a possible new approach to clinical anticoagulant therapy (see page 10071, left col, last paragraph).
Therefore, the presently claimed invention was prima facie obvious to one of ordinary skill in the art at the time of the effective filing date.
Conclusion
No claim is allowed.
Any inquiry concerning this communication or earlier communications from the examiner should be directed to KOYELI BANERJEE whose telephone number is (571)272-5751. The examiner can normally be reached Monday-Friday 8-4PM.
Examiner interviews are available via telephone, in-person, and video conferencing using a USPTO supplied web-based collaboration tool. To schedule an interview, applicant is encouraged to use the USPTO Automated Interview Request (AIR) at http://www.uspto.gov/interviewpractice.
If attempts to reach the examiner by telephone are unsuccessful, the examiner’s supervisor, Melissa Fisher can be reached at (571) 270-7430. The fax phone number for the organization where this application or proceeding is assigned is 571-273-8300.
Information regarding the status of published or unpublished applications may be obtained from Patent Center. Unpublished application information in Patent Center is available to registered users. To file and manage patent submissions in Patent Center, visit: https://patentcenter.uspto.gov. Visit https://www.uspto.gov/patents/apply/patent-center for more information about Patent Center and https://www.uspto.gov/patents/docx for information about filing in DOCX format. For additional questions, contact the Electronic Business Center (EBC) at 866-217-9197 (toll-free). If you would like assistance from a USPTO Customer Service Representative, call 800-786-9199 (IN USA OR CANADA) or 571-272-1000.
/KOYELI BANERJEE/Examiner, Art Unit 1658
/Melissa L Fisher/Supervisory Patent Examiner, Art Unit 1658
Prosecution Insights