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 .
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.
Withdrawn Objection
The objection to the specification is withdrawn in response to the amendments.
Priority
Acknowledgment is made of the present application as a proper National Stage (371) entry of PCT Application No. PCT/US2021/018015, filed 02/12/2021, which claims benefit under 35 U.S.C. 119(e) to provisional application No. 63/014,088, filed 04/22/2020 and to provisional application No. 62/977,133, filed 02/14/2020.
Information Disclosure Statement
The information disclosure statement filed 4/22/2026 is being considered by the examiner.
Status of the Claims
Claims 1-5, 7-9 and 13-39 are pending; claims 1 and 4-5 are amended, claims 6 and 10-12 are canceled; claims 15-36 are withdrawn. Claims 1-5, 7-9, 13-14 and 37-39 are examined below
Maintained Rejection
Claim Rejections - 35 USC § 112
The following is a quotation of 35 U.S.C. 112(b):
(b) CONCLUSION.—The specification shall conclude with one or more claims particularly pointing out and distinctly claiming the subject matter which the inventor or a joint inventor regards as the invention.
The following is a quotation of 35 U.S.C. 112 (pre-AIA ), second paragraph:
The specification shall conclude with one or more claims particularly pointing out and distinctly claiming the subject matter which the applicant regards as his invention.
Claim 5 is rejected under 35 U.S.C. 112(b) or 35 U.S.C. 112 (pre-AIA ), second paragraph, as being indefinite for failing to particularly point out and distinctly claim the subject matter which the inventor or a joint inventor (or for applications subject to pre-AIA 35 U.S.C. 112, the applicant), regards as the invention.
Claim 5 recites “wherein the capture antibody and the detection antibody bind to different moieties of GST-Pi”. Note that Applicant remarks (5/4/2026) that “claim 5's recitation of the two antibodies binding to different moieties simply means that they bind to different portions of the antigen (GST-Pi)” (page 10 para. 1). Therefore, the term “different moieties of GST-Pi” is hereby interpreted to mean “different portions of GST-Pi”. However, there is evidence in the art that the A303-628A capture antibody and the H00002950-M01 detection antibody bind to overlapping portions of GST-Pi. See for example, as evidenced by Rabbit anti-GSTP1 Antibody Affinity Purified (retrieved online https://www.fortislife.com/products/primary-antibodies/rabbit-anti-gstp1-antibody/BETHYL-A303-628?selected=A303-628A on 10/24/2025)-Cited on PTO 892 11/3/2025 (“Bethyl”), the antibody A303-628A binds to amino acids 160 to 210 of GST-Pi (“The epitope recognized by A303-628A maps to a region between residue 160 and 210 of human Glutathione S-Transferase Pi 1 using the numbering given in entry NP_000843.1 (GenelD 2950)” page 3 para. 2). Also, as evidenced by Abnova “GSTP1 monoclonal antibody (M01), clone 2G6-F6” (retrieved online https://www.abnova.com/en-global/product/detail/H00002950-M01 on 5/12/2026) (“Abnova”) the H00002950-M01 antibody binds to amino acids 1 to 210 of GST-Pi (“Mouse monoclonal antibody raised against a full length recombinant GSTP1. GSTP1 (MH10915. 1 a.a. - 210 a.a) full-length recombinant protein with GST tag” page 2 paras. 1-2). Notably the antibodies claimed fail to bind different portions of GST-Pi at amino acids 160-210 since both antibodies are expected to bind to these regions. Because of this, a person having ordinary skill in the art would not be capable of recognizing the metes and bounds of the claim.
Maintained Rejection
Claim Rejections - 35 USC § 102
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)(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.
Claim 37 is rejected under 35 U.S.C. 102(a)(2) as being anticipated by Doyle et al. (US 6080551 A) ("Doyle") (Cite No. 1 of IDS 5/2/2024).
Regarding claim 37, Doyle teaches a kit comprising for detecting and/or measuring the concentration of glutathione S-transferase Pi (GST-Pi) in a sample of a biological fluid (“a kit for carrying out a method for the detection of GST as hereinbefore defined” col. 5 lines 18-19, “Most preferably the GST is… πGST” col. 3 line 43), comprising a lateral flow immunoassay device (“Rapid assay” Title, see Figures 1-2 showing a lateral flow immunoassay device), for detecting and/or measuring the concentration of glutathione S-transferase Pi (GST-Pi) in a sample of a biological fluid (“based on the detection of one or more isoenzymes of glutathione S-transferase ( GST) in diverse biological fluids” Abstract, col. 3 line 43), said device comprising a test strip for detecting GST-Pi in the sample (“The technique is also illustrated with reference to FIG. 1. In FIG. 1 a nitrocellulose membrane strip is indicated generally at 10” col. 9 lines 3-5, “nitrocellulose membrane, pre-coated with anti-πGST IgG” col. 11 lines 9-10), wherein the test strip comprises: i) a sample pad, wherein the sample pad comprises an absorbent material and is configured to receive the sample (“in the case of a nitrocellulose membrane, the provision of a wick at the sample application end and another at the top of the membrane will facilitate chromatographic movement of gold-labelled IgG previously sprayed onto the membrane” col. 5 lines 5-9, “FIG. 1…Direction of flow of the sample on the nitrocellulose membrane 10 is indicated by the arrow… sample application end 13” col. 9 lines 3, 8-10 and 21). Note that although Doyle fails to use the language “sample pad”, the teaching of a sample application end on a nitrocellulose membrane which may include a wick for providing flow of the sample, inherently provides a sample pad comprising absorbent material configured to receive the sample. Doyle further teaches ii) a conjugate pad configured to store a detection antibody specific for GST-Pi and to release at least a portion of the stored detection antibody in the presence of a liquid, wherein the detection antibody is conjugated to a colored label (“The biological fluid is contacted with particle-labelled anti-GST antibody so that the GST isoenzyme to be detected is bound to said particle-labelled anti-GST antibody prior to being contacted with solid phase immobilised antibody. Particles which can be used as labels include colloidal particles, latex particles and metallic sol particles. Metallic sol particles are suitably gold particles… The particle-labelled anti-GST antibody can also be disposed adjacent the sample application end” col. 4 lines 40-51, “in the case of a nitrocellulose membrane…liquid present in a biological sample resuspends the gold-labelled anti-GST IgG and any GST isoenzyme present is bound by the gold-labelled IgG” col. 5 lines 5 and 13-15, “produces a pink-red line” col. 13 lines 40-41). Note that although Doyle fails to use the language “conjugate pad” the teaching of a particle-labelled anti-GST antibody adjacent to the sample application end on the nitrocellulose membrane inherently provides a conjugate pad to store and release the labeled antibody. Also note that although Doyle fails to use the language “colored label” the teaching that the gold nanoparticle produces a color inherently provides a colored label. Doyle further teaches iii) a colorimetric indicator site positioned downstream from the absorbent pad, wherein said colorimetric indicator site comprises a capture antibody specific for GST-Pi fixed to the test strip (“If sufficient GST isoenzyme is present, then the GST/gold-labelled anti-GST IgG complex is immobilized onto the membrane where bound anti-GST IgG is present. This results in a positive signal indicating that GST is present in the sample” col. 5 lines 17-21, col. 13 lines 40-41, see Figure 1B). Doyle further teaches one or more buffers (col. 5 lines 18-19, “Non-specific binding sites on the nitrocellulose membrane are optionally blocked depending on the format of the assay adopted as hereinafter described” col. 4 lines 3-5, “The strips were blocked by incubation for 30 minutes at room temperature in a solution of 2% (w/v) non-fat milk and 2% (w/v) polyvinylpyrrolidone in Tris buffered saline, pH 7.4” col. 12 lines 16-19).
New Rejections
Claim Rejections - 35 USC § 103
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.
Claim(s) 1, 3-5, 7 and 9 are rejected under 35 U.S.C. 103 as being unpatentable over Doyle et al. (US 6080551 A) ("Doyle") (Cite No. 1 of IDS 5/2/2024) in view of Andrukhova et al. Journal of Cardiac Failure Volume 20, Issue 2, February 2014, Pages 135-145 https://doi.org/10.1016/j.cardfail.2013.11.012-Cited on PTO 892 11/3/2025 (“Andrukhova”) and Maney et al. (WO 2014/193999 A2)-Cited on PTO 892 11/3/2025 (“Maney”) as evidenced by Rabbit anti-GSTP1 Antibody Affinity Purified (retrieved online https://www.fortislife.com/products/primary-antibodies/rabbit-anti-gstp1-antibody/BETHYL-A303-628?selected=A303-628A on 10/24/2025)-Cited on PTO 892 11/3/2025 (“Bethyl”) and Abnova “GSTP1 monoclonal antibody (M01), clone 2G6-F6” (retrieved online https://www.abnova.com/en-global/product/detail/H00002950-M01 on 5/12/2026) (“Abnova”).
Regarding claim 1, Doyle teaches a lateral flow immunoassay device (“Rapid assay” Title, see Figures 1-2 showing a lateral flow immunoassay device), for detecting and/or measuring the concentration of glutathione S-transferase Pi (GST-Pi) in a sample of a biological fluid (“based on the detection of one or more isoenzymes of glutathione S-transferase ( GST) in diverse biological fluids” Abstract, col. 3 line 43), said device comprising a test strip for detecting GST-Pi in the sample (“The technique is also illustrated with reference to FIG. 1. In FIG. 1 a nitrocellulose membrane strip is indicated generally at 10” col. 9 lines 3-5, “nitrocellulose membrane, pre-coated with anti-πGST IgG” col. 11 lines 9-10), wherein the test strip comprises: a) a sample pad, wherein the sample pad comprises an absorbent material and is configured to receive the sample (“in the case of a nitrocellulose membrane, the provision of a wick at the sample application end and another at the top of the membrane will facilitate chromatographic movement of gold-labelled IgG previously sprayed onto the membrane” col. 5 lines 5-9, “FIG. 1…Direction of flow of the sample on the nitrocellulose membrane 10 is indicated by the arrow… sample application end 13” col. 9 lines 3, 8-10 and 21). Note that although Doyle fails to use the language “sample pad”, the teaching of a sample application end on a nitrocellulose membrane which may include a wick for providing flow of the sample, inherently provides a sample pad comprising absorbent material configured to receive the sample. Doyle further teaches b) a conjugate pad configured to store a detection antibody specific for GST-Pi and to release at least a portion of the stored detection antibody in the presence of a liquid, wherein the detection antibody is conjugated to a colored label (“The biological fluid is contacted with particle-labelled anti-GST antibody so that the GST isoenzyme to be detected is bound to said particle-labelled anti-GST antibody prior to being contacted with solid phase immobilised antibody. Particles which can be used as labels include colloidal particles, latex particles and metallic sol particles. Metallic sol particles are suitably gold particles… The particle-labelled anti-GST antibody can also be disposed adjacent the sample application end” col. 4 lines 40-51, “in the case of a nitrocellulose membrane…liquid present in a biological sample resuspends the gold-labelled anti-GST IgG and any GST isoenzyme present is bound by the gold-labelled IgG” col. 5 lines 5 and 13-15, “produces a pink-red line” col. 13 lines 40-41). Note that although Doyle fails to use the language “conjugate pad” the teaching of a particle-labelled anti-GST antibody adjacent to the sample application end on the nitrocellulose membrane inherently provides a conjugate pad to store and release the labeled antibody. Also note that although Doyle fails to use the language “colored label” the teaching that the gold nanoparticle produces a color inherently provides a colored label. Doyle further teaches c) a colorimetric indicator site positioned downstream from the absorbent pad, wherein said colorimetric indicator site comprises a capture antibody specific for GST-Pi fixed to the test strip (“If sufficient GST isoenzyme is present, then the GST/gold-labelled anti-GST IgG complex is immobilized onto the membrane where bound anti-GST IgG is present. This results in a positive signal indicating that GST is present in the sample” col. 5 lines 17-21, col. 13 lines 40-41, see Figure 1B). Doyle further teaches one or more buffers (col. 5 lines 18-19, “Non-specific binding sites on the nitrocellulose membrane are optionally blocked depending on the format of the assay adopted as hereinafter described” col. 4 lines 3-5, “The strips were blocked by incubation for 30 minutes at room temperature in a solution of 2% (w/v) non-fat milk and 2% (w/v) polyvinylpyrrolidone in Tris buffered saline, pH 7.4” col. 12 lines 16-19).
Doyle fails to teach wherein the capture antibody is A303-628A and the detection antibody is H00002950-M01.
Andrukhova teaches “single-dose GSTP1 prevents infarction-induced heart failure” (Title). Andrukhova further teaches detecting and/or measuring GST-Pi using A303-628A antibody (“For GSTP1-TRAF2, GSTP1-JNK1, and GSTP1-p38 complex detection… use of GSTP1 antibody (Bethyl, Montgomery, Texas)” page 136 col. 2 para. 3). Note that as evidenced by Bethyl, the “GSTP1 antibody (Bethyl, Montgomery, Texas)” taught by Andrukhova is A303-628A (“Product Citations: 1 Single-dose GSTP1 prevents infarction-induced heart failure. In Journal of Cardiac Failure on 1 February 2014 by Andrukhova, O., Salama, M., et al.” page 4).
Maney teaches “biomarker methods and compositions” (Title). Maney further teaches that “[b]iomarkers can be assessed for diagnostic, therapy-related or prognostic methods to identify phenotypes, such as a condition or disease, or the stage or progression of a disease, select candidate treatment regimens for diseases, conditions, disease stages, and stages of a condition, and to determine treatment efficacy. Circulating biomarkers from a bodily fluid can be used in profiling of physiological states or determining phenotypes. These include…protein” (Abstract). Maney further suggests that antibodies conjugated to a particle can be used for assessing biomarkers in body fluids (“[v]arious types of binding agents can be used in the methods of the invention…antibody… The at least one binding agent can be labeled” para. 22, “A binding agent can also be bound to particles such as beads or microspheres” para. 190, “the
detection agent is labeled and the label is detected, thereby detecting the biomarker or vesicle. The detection agent can be a binding agent, e.g., an antibody” para. 497). Maney further suggests detecting and/or measuring GST-Pi using the detection antibody H00002950-M01 (“the invention provides use of the at least one reagent to carry out the methods of invention… reagent capable of binding to a target protein in Table 46” para. 29, “The detection agent, which may also be an…antibody, carries a detectable label” para. 39, “Table 46: Capture Antibodies… GSTPl NOVUS BIOLOGICALS H00002950-M01 12174-S2 GSTPl NOVUS BIOLOGICALS H00002950-M01 D5092-S2” pages 321 and 323, “One of skill will appreciate that targets of capture agents and detection agents can be used interchangeably” para. 501). Note that although Maney teaches the H00002950-M01 antibody in the Table labeled “Capture Antibodies”, the teachings that “[o]ne of skill will appreciate that targets of capture agents and detection agents can be used interchangeably” suggests that the H00002950-M01 antibody is a detection antibody.
It would have been prima facie obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to have modified the teachings of Doyle to rely on the capture antibody being A303-628A taught by Andrukhova because it would have been a simple matter of applying a known technique to a known method. In this case, both Doyle and Andrukhova teach measuring and/or detecting GSTP1 using an antibody specific for GSTP1. Andrukhova simply applies the art-recognized technique of using the commercially available antibody A303-628A from Bethyl. Therefore, a person having ordinary skill in the art would have found it obvious to apply the technique of Andrukhova to the base method taught by both Doyle and Andrukhova. A person having ordinary skill in the art would have had a reasonable expectation of success because antibody A303-628A is commercially available from the company Bethyl. Furthermore both Doyle and Andrukhova use the capture antibody in a solid phase assay, i.e. both techniques require a step of immobilizing the antibody and a step of detecting the GSTP1.
It would have been further prima facie obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to have modified the teachings of Doyle in view of Andrukhova to rely on the detection antibody being H00002950-M01 taught by Maney because it would have been a simple matter of applying a known technique to a known method. In this case, both Doyle and Maney teach measuring and/or detecting GSTP1 using an antibody specific for GSTP1 conjugated to a particle label for diagnostics. Maney simply applies the art-recognized technique of using the commercially available antibody H00002950-M01. Therefore, a person having ordinary skill in the art would have found it obvious to apply the technique of Maney to the base method taught by both Doyle and Maney. A person having ordinary skill in the art would have been motivated to try picking antibody H00002950-M01 from the finite list of antibodies taught by Maney because Maney suggests that GSTP1 is a diagnostic and prognostic biomarker of disease as well as a biomarker for treatment efficacy. Therefore, it would have been obvious to try picking H00002950-M01 from said finite list. A person having ordinary skill in the art would have had a reasonable expectation of success given that Maney teaches the vendor and two lot numbers of the H00002950-M01 antibody.
Regarding claim 3, Doyle in view of Andrukhova and Maney teach the device of claim 1 as discussed above.
Doyle in view of Andrukhova and Maney further teach wherein at least a portion of the test strip comprises a nitrocellulose membrane (col. 9 lines 3-5, col. 11 lines 9-10 of Doyle).
Regarding claim 4, Doyle in view of Andrukhova and Maney teach the device of claim 1 as discussed above.
Doyle in view of Andrukhova and Maney further teach wherein at least a portion of the test strip comprises a nitrocellulose membrane with an average pore size of at least, at most, or about 5, 10, 15, 20, 25, or 30 µm (“Suitably, the nitrocellulose membrane has a pore size in the range 5-10 µm” col. 4 lines 1-2 of Doyle).
Regarding claims 5, Doyle in view of Andrukhova and Maney teach the device of claim 1 as discussed above.
Doyle in view of Andrukhova and Maney further teach wherein the capture antibody and the detection antibody bind to different moieties of GST-Pi (page 136 col. 2 para. 3 of Andrukhova and paras. 29, 39 and 501 and pages 321 and 323 of Maney). Note that the A303-628A capture antibody and the H00002950-M01 detection antibody bind to different portions of GST-Pi at amino acid positions 1-159. See for example, as evidenced by Bethyl, the antibody A303-628A binds to amino acids 160 to 210 of GST-Pi (“The epitope recognized by A303-628A maps to a region between residue 160 and 210 of human Glutathione S-Transferase Pi 1 using the numbering given in entry NP_000843.1 (GenelD 2950)” page 3 para. 2). Also, as evidenced by Abnova the H00002950-M01 antibody binds to amino acids 1 to 210 of GST-Pi (“Mouse monoclonal antibody raised against a full length recombinant GSTP1. GSTP1 (MH10915. 1 a.a. - 210 a.a) full-length recombinant protein with GST tag” page 2 paras. 1-2). Given that the A303-628A capture antibody and the H00002950-M01 detection antibody bind to different portions of the GST-Pi antibody at amino acid positions 1-159, Doyle in view of Andrukhova and Maney address the claim.
Regarding claim 7, Doyle in view of Andrukhova and Maney teach the device of claim 1 as discussed above.
Doyle in view of Andrukhova and Maney further teach wherein the colored label comprises a gold or latex nanoparticle (“gold particles having an average diameter in the range 15-40 nm” col. 4 lines 45-47 of Doyle).
Regarding claim 9, Doyle in view of Andrukhova and Maney teach the device of claim 1 as discussed above.
Doyle in view of Andrukhova and Maney further teach wherein the capture antibody and/or the detection antibody are present at a concentration of 0.1, 0.2, 0.3, 0.4, 0.5, 0.6, 0.7, 0.8, 0.9, 1.0, 1.1, 1.2, 1.3, 1.4 or 1.5, 1.6, 1.7, 1.8, 1.9 or 2.0 mg/mL (“Anti-πGST IgG (murine monoclonal; 0.6 mg/ml” col. 10 line 58 of Doyle).
Claim 2 is rejected under 35 U.S.C. 103 as being unpatentable over Doyle in view of Andrukhova and Maney as applied to claim 1 above, and further in view of Nelson et al. (US 20180021026 A1)-Cited on PTO 892 11/3/2025 ("Nelson").
Regarding claim 2, Doyle in view of Andrukhova and Maney teach the lateral flow immunoassay device of claim 1 as discussed above.
Doyle in view of Andrukhova and Maney fail to teach wherein the device further comprises a lancet with a capillary channel.
Nelson teaches a “self-contained sampling device for processing whole blood” (Title). Nelson teaches that the sampling device is used for sampling whole blood and dispensing and analyzing the whole blood in lateral flow assays (“diagnostic sampling device for processing whole blood and dispensing the processed whole blood” para. 2, “or drawing fluids, such as whole blood from a finger stick, for further processing or analysis, such as direct use in…lateral flow assays” para. 5). Nelson further teaches wherein the device comprises a lancet with a capillary channel (“While some exemplary embodiments use a capillary to draw blood from a finger stick, it is also envisioned to integrate a lancet and/or needle directly into the device, so that the puncture for the blood draw can be integrated into the device” para. 43, see Figure 1 showing the capillary channel 14).
It would have been prima facie obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to have modified the teachings of Doyle in view of Andrukhova and Maney to include a lancet with a capillary channel taught by Nelson because Nelson teaches that this enables direct collection, processing and dispensing of the sample onto a lateral flow assay. A person having ordinary skill in the art would have had a reasonable expectation of success given that both Doyle in view of Andrukhova and Maney and Nelson are drawn to lateral flow assays.
Claim 8 is rejected under 35 U.S.C. 103 as being unpatentable over Doyle in view of Andrukhova and Maney as applied to claim 1 above, and further in view of Serebrennikova et al. Nano-Micro Lett. 10, 24 (2018). https://doi.org/10.1007/s40820-017-0180-2-Cited on PTO 892 11/3/2025.
Regarding claim 8, Doyle in view of Andrukhova and Maney teach the lateral flow immunoassay device of claim 1 as discussed above.
Doyle in view of Andrukhova and Maney fail to teach wherein the colored label is present at an optical density of 1, 2, 3, 4, 5, 6, 7, 8, 9, or 10 OD.
Serebrennikova teaches “hierarchical nanogold labels to improve the sensitivity of lateral flow assay immunoassay” (Title). Serebrennikova further teaches a lateral flow immunoassay device for detecting antigens in a fluid sample comprising a sample pad, a conjugate pad and a colorimetric indicator (Fig. 1 page 24). Serebrennikova further suggests that a colored label (gold nanoparticle) present at an optical density of 2 or 4 OD provides optimal color intensity with low background (“In order to choose the optimal dilution of gold nanoparticle–antibody conjugates for LFIA, the optical density of solutions at an appropriate wavelength was varied from 0.5 to 4. Sufficient color intensity of the test line with low background was achieved by the spreading of pAb-GNS with optical density of 2, pAb-GNPN, and pAb-GNST with optical density of 4” page 23 col. 2 para. 2).
It would have been prima facie obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to have modified the teachings of Doyle in view of Andrukhova and Maney to rely on the colored label being present at an optical density of 2 or 4 OD taught by Serebrennikova because Serebrennikova suggests this provides an optimal color intensity with low background. A person having ordinary skill in the art would have had a reasonable expectation of success given that both Doyle in view of Andrukhova and Maney and Serebrennikova teach a lateral flow immunoassay device for detecting antigens in a fluid sample comprising a sample pad, a conjugate pad and a colorimetric indicator, and gold nanoparticles as colored labels.
Claims 13-14 are rejected under 35 U.S.C. 103 as being unpatentable over Doyle in view of Andrukhova and Maney as applied to claim 1 above, and further in view of Aharinejad (US 20120213761 A1) (Cite No. 3 of IDS file 9/15/2022).
Regarding claims 13-14, Doyle in view of Andrukhova and Maney teach the lateral flow immunoassay device of claim 1 as discussed above.
Doyle further teaches that an “area where a rapid assay format is required is in assessing organs prior to transplantation” (col. 2 lines 19-20).
Doyle fails to teach wherein the GST-Pi comprises a polypeptide sequence of SEQ ID NO: 1, wherein the GST-Pi comprises a polypeptide sequence sharing at least 90%, 95%, or 99% sequence identity with SEQ ID NO: 1.
Aharinejad teaches “use of GSTP1” (Title). Aharinejad further teaches detecting GSTP1 using an immunoassay (“Preferred techniques for determining the amount of GSTP1 include antibody-liked techniques” paragraph 33). Aharinejad further teaches that “[d]etection and quantification of GSTP1 by using anti GSTP1 antibodies is well established in the art” (para. 43). Aharinejad further suggests measuring GST-Pi prior to heart transplantation in order to diagnose cardiomyopathies or ischemic heart disease (“the present invention relates to GSTP1 as a diagnostic target for CMP or IHD” para. 30, “Importantly, patients who develop CMP based on IHD, in particular end-stage CMP, have currently only limited therapeutic options (e.g. cardiac transplantation” para. 6, “Serum GSTP1 is a Sensitive Marker of CMP…The study cohort comprised 141 end-stage CMP patients scheduled for cardiac transplantation” paras. 76-77, “ For protein array randomly selected serum samples were obtained from end-stage CMP patients shortly before transplant” para. 80, “In the targeted protein array screen of pooled serum samples in selected CMP patients GSTP1 was identified as a novel protein to be associated with CMP” para. 87). Aharinejad further teaches wherein the GST-Pi comprises a polypeptide sequence of SEQ ID NO: 1, wherein the GST-Pi comprises a polypeptide sequence sharing at least 90%, 95%, or 99% sequence identity with SEQ ID NO: 1 (“The human sequence (Seq. ID. No. 1) is listed as "GSTPl HUMAN, P09211" in the UniProtKB/SwissProt database (HGNC:4638, Entrez Gene: 2950)” para. 21). Note that SEQ ID NO: 1 of Aharinejad is 100% matched to SEQ ID NO: 1 of the instant claims.
It would have been prima facie obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to have modified the teachings of Doyle in view of Andrukhova and Maney to rely on wherein the GST-Pi comprises a polypeptide sharing at least 90%, 95%, or 99% sequence identity with SEQ ID NO: 1 taught by Aharinejad because Aharinejad suggests that this enables the diagnosis of cardiomyopathies of patients scheduled for organ transplantation and Doyle teaches that rapid assay formats are needed for patients under organ transplantation. Furthermore, Doyle teaches a sandwich-type immunoassay where the detection antibody and the capture antibody both have to bind to GST-Pi and thus would require antibodies, such as those taught by Aharinejad that can bind to different portions on GST-Pi. A person having ordinary skill in the art would have had a reasonable expectation of success because Aharinejad teaches that detection and quantification of GSTP1 by using anti GSTP1 antibodies is well established in the art and both Doyle in view of Andrukhova and Maney and Aharinejad are drawn to measuring GST-Pi levels of patients before organ transplantation.
Maintained Rejection
Claims 38-39 are rejected under 35 U.S.C. 103 as being unpatentable over Doyle as applied to claim 1 above, and further in view of Aharinejad (US 20120213761 A1) (Cite No. 3 of IDS file 9/15/2022).
Regarding claims 38-39, Doyle teaches the kit of claim 37 as discussed above.
Doyle further teaches that an “area where a rapid assay format is required is in assessing organs prior to transplantation” (col. 2 lines 19-20).
Doyle fails to teach wherein the GST-Pi comprises a polypeptide sequence of SEQ ID NO: 1, wherein the GST-Pi comprises a polypeptide sequence sharing at least 90%, 95%, or 99% sequence identity with SEQ ID NO: 1.
Aharinejad teaches “use of GSTP1” (Title). Aharinejad further teaches detecting GSTP1 using an immunoassay (paragraph 33). Aharinejad further suggests wherein the capture antibody and the detection antibody are configured to bind to different moieties of GST-Pi (para. 38). Aharinejad further teaches that “[d]etection and quantification of GSTP1 by using anti GSTP1 antibodies is well established in the art” (para. 43). Aharinejad further suggests measuring GST-Pi prior to heart transplantation in order to diagnose cardiomyopathies or ischemic heart disease (paras. 6, 30, 76-77, 80 and 87). Aharinejad further teaches wherein the GST-Pi comprises a polypeptide sequence of SEQ ID NO: 1, wherein the GST-Pi comprises a polypeptide sequence sharing at least 90%, 95%, or 99% sequence identity with SEQ ID NO: 1 (para. 21). Note that SEQ ID NO: 1 of Aharinejad is 100% matched to SEQ ID NO: 1 of the instant claims.
It would have been prima facie obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to have modified the teachings of Doyle to rely on wherein the GST-Pi comprises a polypeptide sharing at least 90%, 95%, or 99% sequence identity with SEQ ID NO: 1 taught by Aharinejad because Aharinejad suggests that this enables the diagnosis of cardiomyopathies of patients scheduled for organ transplantation and Doyle teaches that rapid assay formats are needed for patients under organ transplantation. Furthermore, Doyle teaches a sandwich-type immunoassay where the detection antibody and the capture antibody both have to bind to GST-Pi and thus would require antibodies, such as those taught by Aharinejad that can bind to different epitopes on GST-Pi. A person having ordinary skill in the art would have had a reasonable expectation of success because Aharinejad teaches that detection and quantification of GSTP1 by using anti GSTP1 antibodies is well established in the art and both Doyle and Aharinejad are drawn to measuring GST-Pi levels of patients before organ transplantation.
Pertinent Art
The prior art made of record and not relied upon is considered pertinent to applicant's disclosure.
bioNova PRIMARY ANTIBODIES (retrieved online https://www.bionova.es/documents/bethyl/primary_ab_2014.pdf on 5/12/2026) (Year: 2019) (“BioNova”).
BioNova teaches the catalog of primary antibodies of Bethyl (page 1). BioNova further teaches the capture antibody A303-628A for GSTP1(page 41). BioNova further teaches that the antibody is a reliable quality product (“This attention to quality at every step and the integration across each stage of the process means scientists can rely on Bethyl antibodies” page 2 para. 2). Bionova further teaches that they “also offer expert technical support to help ensure your success” page 2 para. 3).
Note that as evidenced by the Wayback Machine (retrieved online https://web.archive.org/web/20260000000000*/https://www.bionova.es/documents/bethyl/primary_ab_2014.pdf on 5/12/2026) the Bethyl antibody catalog (BioNova) was publicly available since at least “April 10, 2019” (page 1).
Response to Arguments
Applicant's arguments filed 5/4/2026 have been fully considered but they are not persuasive.
Regarding the 112b rejections,
Applicant argues “As such, claim 5's recitation of the two antibodies binding to different moieties simply means that they bind to different portions of the antigen (GST-Pi). One of ordinary skill would immediately understand the scope of this claim” (page 10 para. 1).
However, a person having ordinary skill in the art would fail to immediately understand the scope of the claim because the recited capture antibody A303-628A and the detection antibody H00002950-M01 bind to overlapping portions of GST-Pi (see 112b rejection above). Because of this, there is a question regarding the metes and bounds of the claim.
Regarding the 102 and 103 rejections,
Applicant argues that “One of ordinary skill in the art would conclude from Doyle that whilst measuring αGST in blood plasma was possible, measuring πGST was much more challenging and unlikely to succeed with levels below 50 ng/ml” (page 11 para. 3).
However, this argument is not persuasive given that the claim is not limited by detecting GST-Pi levels below 50 ng/ml.
Applicant further argues that “Example 5 of Doyle used a device with printed capture antibody on the nitrocellulose and pre-mixing of plasma with gold-labelled anti-GSTPl before placing the nitrocellulose strip into a chamber containing the sample/gold-anti-GSTP conjugate mixture. This differs fundamentally from the device of the present invention” (page 11 para. 4).
However, Doyle in view of in view of Andrukhova and Maney teach the device of claim 1 (see rejection above). Furthermore, the claim is not limited by method steps. Therefore, Applicant’s arguments are not persuasive.
Applicant further argues that “No evidence was provided that this device would function with plasma or whole blood…Doyle further fails to provide any detail regarding the anti-GSTPl antibodies…the POSA is merely being invited to perform undue experimentation to identify a pair of capture and detection antibodies with little expectation of success for measuring GSTPl in plasma or whole blood” (page 12 para. 1).
However, the claims as currently recited are no longer limited by the sample being whole blood. Nevertheless, given that Doyle in view of Andrukhova and Maney teach the claimed device including the antibodies (see rejection above), the device taught by Doyle in view of Andrukhova and Maney would also be expected to function with whole blood.
Applicant further argues that “According to the Office Action, the Bethyl webpage was accessed on October 24, 2025 -several years after the priority date of the present application…There is no evidence that a POSA would have had access to Bethyl before the priority date of the present application… For at least this reason, the current combination of asserted prior art fails to render obvious a lateral flow assay - or any other assay - using A303-628A” (page 12 para. 5 and page 13 para. 1).
However, contrary to Applicant’s remark, the Bethyl webpage is used as evidence of intrinsic physical or chemical property of materials taught in the prior art, namely, that the antibody taught by Andrukhova is A303-628A. Furthermore, the reference bioNova cited above teaches that the Bethyl A303-628A antibody was published since at least April 10, 2019 according to the Wayback Machine (see pertinent art above). For these reasons, Applicant’s arguments are not persuasive.
Applicant further argues that “Andrukhova merely teaches that the "GSTPl antibody (Bethyl, Montgomery, Texas)" was used for Western blotting…. It is well known that antibodies that are suitable for one application should not be expected to work with all applications and that testing is required to confirm the suitability of a given antibody with a given application… Numerous other websites, laboratory manuals, and textbooks are available to demonstrate this same well recognized issue” (page 13 para. 2). Applicant further argues that “A POSA would have been aware of this issue, and would therefore have had no reasonable expectation of success, with respect to substituting the antibodies used in Doyle with those described in the secondary references relied upon in the Office Action” (page 15 para. 1).
However, although Andrukhova teaches the A303-628A antibody using Western Blot, and that numerous websites, laboratory manuals, and textbooks teach that antibodies that are suitable for one application should not be expected to work with all applications, in this case, a person having ordinary skill in the art would have had a reasonable expectation of success in using the A303-628A antibody in the lateral flow device because both Doyle and Andrukhova use an GSTPl antibody in a solid phase assay (see rejection above). Applicant has not provided enough evidence that the A303-628A antibody specifically is not expected to work in a lateral flow assay device.
Applicant further argues that “Perhaps the most critical deficit in the teaching of Andrukhova is that this study was measuring GSTPl heterocomplexes from cardiac tissue after enrichment using antibodies against putative GSTPl binding proteins (TRAF2, JNKl, p38)… but there is no support for detecting circulating free GSTPl from blood” (page 13 last paragraph).
However, the claims as currently recited are no longer limited by the sample being blood.
Applicant further argues that “Applicant also rebuts the Examiner's interpretation of MAB 10823 to be "any antibody specific for GST-Pi" as set forth in the Office Action on pp. 14-17. Applicant's own experimental data demonstrates that not all antibodies are suitable for a given application, and also shows that the same antibody will often perform differently in lateral flow assays when paired with alternative capture/detection antibodies” (page 14 para. 3).
However, the claims as currently recited are no longer limited by the MAB 10823 antibody.
Applicant further argues that “Reconsideration and allowance of the application are earnestly solicited” (page 16 para. 1).
However, no claim is allowed.
Conclusion
Applicant's amendment necessitated the new ground(s) of rejection presented in this Office action. Accordingly, THIS ACTION IS MADE FINAL. See MPEP § 706.07(a). Applicant is reminded of the extension of time policy as set forth in 37 CFR 1.136(a).
A shortened statutory period for reply to this final action is set to expire THREE MONTHS from the mailing date of this action. In the event a first reply is filed within TWO MONTHS of the mailing date of this final action and the advisory action is not mailed until after the end of the THREE-MONTH shortened statutory period, then the shortened statutory period will expire on the date the advisory action is mailed, and any nonprovisional extension fee (37 CFR 1.17(a)) pursuant to 37 CFR 1.136(a) will be calculated from the mailing date of the advisory action. In no event, however, will the statutory period for reply expire later than SIX MONTHS from the mailing date of this final action.
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/Fernando Ivich/Examiner, Art Unit 1678
/GREGORY S EMCH/Supervisory Patent Examiner, Art Unit 1678
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