DETAILED ACTION
Response to Amendment
Applicant’s response to the office action filed on October 29, 2025 has been entered. The claims pending in this application are claims 1-19 wherein claims 13-15 have been withdrawn due to the restriction requirement mailed on June 5, 2025. The objections and rejections not reiterated from the previous office action are hereby withdrawn in view of applicant’s amendments filed on October 29, 2025. Claims 1-12 and 16-19 will be examined.
Specification
The amended specification filed on October 29, 2025 has not been entered by the office because applicant has not provided a marked up version of the amended specification. The objection below has been maintained. Note that there is no example 6 in the specification.
The disclosure is objected to because of the following informalities: there are Figures 3A, 3B, 4A to 4D, 5A to 5E, 6A to 6E, 7A to 7E, 8A to 8E, 9A to 9E, 10A to 10E, 11A to 11E, 12A to 12H, and 13A to 13H. However, Brief Description Of Drawings only describes Figures 3 to 13.
Appropriate correction is required.
Claim Objections
Claim 1 or 3 or 4 or 5 or 7 or 8 or 9 or 10 or 15 or 16 is objected to because of the following informality: “the cleaving a first flap and the cleaving a second flap” should be “said cleaving a first flap of a first cleave structure and said cleaving a second flap of a second cleave structure”.
Claim 3 is objected to because of the following informality: “a pH of” should be “a pH from”.
Claim 4 or 16 is objected to because of the following informality: “a temperature of” should be “a temperature from”.
Claim 6 is objected to because of the following informality: “2.5 mM to 20 mM” should be “from 2.5 mM to 20 mM”.
Claim 7 is objected to because of the following informality: “wherein a concentration of K⁺ in the aqueous solvent is greater than 0 mM and 100 mM or less” should be “wherein a concentration of K⁺ in the aqueous solvent is greater than 0 mM or 100 mM or less than 100 mM”.
Claim 8 is objected to because of the following informality: “wherein a concentration of trishydroxymethylaminomethane in the aqueous solvent is greater than 0 mM and 300 mM or less” should be “wherein a concentration of trishydroxymethylaminomethane in the aqueous solvent is greater than 0 mM or 300 mM or less than 300 mM”.
Claim 9 is objected to because of the following informality: “0.5 µM or greater to 8 µM or less” should be “from 0.5 µM to 8 µM”.
Claim 10 is objected to because of the following informality: “a volume of the
aqueous solvent is 10 aL or more and 10 µL or less” should be “a volume of the aqueous solvent is more than 10 µL or 10 µL or less than 10 µL”.
Claim 17 is objected to because of the following informality: “the amino acid sequence of a flap endonuclease of a microbe of Thermococcus kodakarensis strain KOD1” should be “the amino acid sequence of the flap endonuclease of the microbe of Thermococcus kodakarensis strain KOD1”.
Claim 18 is objected to because of the following informality: “the amino acid sequence of a flap endonuclease of a microbe of Pyrococcus abyssi strain GE5” should be “the amino acid sequence of the flap endonuclease of the microbe of Pyrococcus abyssi strain GE5”.
Claim 19 is objected to because of the following informality: “the amino acid sequence of a flap endonuclease of a microbe of Methanothermobacter thermautotrophicus strain Delta H” should be “the amino acid sequence of the flap endonuclease of the microbe of Methanothermobacter thermautotrophicus strain Delta H”.
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.
This application currently names joint inventors. In considering patentability of the claims the examiner presumes that the subject matter of the various claims was commonly owned as of the effective filing date of the claimed invention(s) absent any evidence to the contrary. Applicant is advised of the obligation under 37 CFR 1.56 to point out the inventor and effective filing dates of each claim that was not commonly owned as of the effective filing date of the later invention in order for the examiner to consider the applicability of 35 U.S.C. 102(b)(2)(C) for any potential 35 U.S.C. 102(a)(2) prior art against the later invention.
Claims 1-8, 10-12, 16, and 18 are rejected under 35 U.S.C. 103 as being unpatentable over Ogino et al., (WO 2019/026884 A1, published on February 7, 2019) in view of the amino acid sequence of the flap endonuclease-1 (FEN-1) from Pyrococcus abyssi strain GE5 (available in GenBank since March 7, 2015, see IDS filed on September 22, 2022).
Regarding claims 1-8, 10, 12, and 16, Ogino et al., teach a method for detecting a target nucleic acid, the method comprising: cleaving a first flap of a first cleavage structure formed by a target nucleic acid, a first nucleic acid, and a second nucleic acid; cleaving a second flap of a second cleavage structure formed by a third nucleic acid (ie., the fourth nucleic acid in paragraph [0010]), the first flap that has been cleaved (ie., the third nucleic acid in paragraph [0010]), and a fourth nucleic acid (ie., the fifth nucleic acid in paragraph [0010]); and detecting the presence of the target nucleic acid by detecting the second flap that has been cleaved, wherein said cleaving a first flap of a first cleave structure and said cleaving a second flap of a second cleave structure are carried out by cleaving the first flap and the second flap with a flap endonuclease (eg., FEN-1) as recited in claim 1 wherein the target nucleic acid is a DNA as recited in claim 2, said cleaving a first flap of a first cleave structure and said cleaving a second flap of a second cleave structure are carried out under the conditions of a pH from 7.5 to 9.0 as recited in claim 3, said cleaving a first flap of a first cleave structure and said cleaving a second flap of a second cleave structure are carried out under the conditions of a temperature from 55°C to 70°C as recited in claim 4, said cleaving a first flap of a first cleave structure and said cleaving a second flap of a second cleave structure are carried out in an aqueous solvent that includes Mg2+ as recited in claim 5, a concentration of Mg2+ in the aqueous solvent is from 2.5 mM to 20 mM as recited in claim 6, said cleaving a first flap of a first cleave structure and said cleaving a second flap of a second cleave structure are carried out in an aqueous solvent, and wherein a concentration of K+ in the aqueous solvent is greater than 0 mM or 100 mM or less than 100 mM as recited in claim 7, said cleaving a first flap of a first cleave structure and said cleaving a second flap of a second cleave structure are carried out in an aqueous solvent, and wherein a concentration of trishydroxymethylaminomethane in the aqueous solvent is greater than 0 mM or 300 mM or less than 300 mM as recited in claim 8, said cleaving a first flap of a first cleave structure and said cleaving a second flap of a second cleave structure are carried out in an aqueous solvent, and a volume of the aqueous solvent is more than 10 µL or 10 µL or less than 10 µL (ie., 10 µl) as recited in claim 10, the cleaved second flap is detected by detecting fluorescence as recited in claim 12, and said cleaving a first flap of a first cleave structure and said cleaving a second flap of a second cleave structure are carried out under the conditions of a temperature from 60°C to 65°C as recited in claim 16 (see paragraph [0001], [0003], [0004], [0010], [0011], [0042] to [0044], [0063], [0064], [0069], [0123], and [0127]).
Regarding claim 11, since Ogino et al., teach that “[I]n the second stage, the third nucleic acid generated in the first stage corresponds to the IP in the invasion structure of the second stage, and the fourth nucleic acid having the second flap site and a base sequence with which the third nucleic acid can hybridize corresponds to the FP, and the second invasion structure is formed by forming a complex. The second flap site associated with the second invasion structure is cleaved by the second nucleic acid cleavage enzyme to generate a cleaved product. At this time, the fourth nucleic acid has a base sequence with which the third nucleic acid can hybridize, and has the function of the target nucleic acid and the FP in the first stage combined, but the function may be divided by using the target nucleic acid in the second stage as the fifth nucleic acid” (see paragraph [0022]), the fourth nucleic acid having a base sequence with which the third nucleic acid can hybridize, and has the function of the target nucleic acid taught by Ogino et al., can be considered as the third nucleic acid and the fourth nucleic acid bonded by a linker molecule (ie., one or more nucleotides) as recited in claim 11.
Ogino et al., do not disclose that the flap endonuclease has an amino acid sequence having a sequence identity of 96% or higher with the amino acid sequence of the flap endonuclease from Pyrococcus abyssi strain GE5 as recited in claims 1 and 18.
The amino acid sequence of the flap endonuclease-1 (FEN-1) from Pyrococcus abyssi strain GE5 is available in GenBank since March 7, 2015.
Therefore, it would have been prima facie obvious to one having ordinary skill in the art at the time the invention was made to have performed the methods recited in claims 1 and 18 using an flap endonuclease which has an amino acid sequence having a sequence identity of 96% or higher with the amino acid sequence of the flap endonuclease from Pyrococcus abyssi strain GE5 in view of the prior arts of Ogino et al., and the amino acid sequence of the flap endonuclease-1 (FEN-1) from Pyrococcus abyssi strain GE5. One having ordinary skill in the art would have been motivated to do so because the amino acid sequence of the flap endonuclease-1 (FEN-1) from Pyrococcus abyssi strain GE5 is available in GenBank since March 7, 2015 and the simple substitution of one kind of flap endonuclease (ie., the FEN-1 taught by Ogino et al.,) from another kind of flap endonuclease (ie., the flap endonuclease-1 (FEN-1) from Pyrococcus abyssi strain GE5 which is available in GenBank since March 7, 2015), in the absence of convincing evidence to the contrary, would have been prima facie obvious to one having ordinary skill in the art at the time the invention was made since the FEN-1 taught by Ogino et al., and the flap endonuclease-1 (FEN-1) from Pyrococcus abyssi strain GE5 which is available in GenBank since March 7, 2015 are used for the same purpose (ie., used for an invasive cleavage assay). One having ordinary skill in the art at the time the invention was made would have a reasonable expectation of success to perform the methods recited in claims 1 and 18 by making the flap endonuclease-1 (FEN-1) from Pyrococcus abyssi strain GE5 based on its amino acid sequence in GenBank and substituting the FEN-1 taught by Ogino et al., from the flap endonuclease-1 (FEN-1) from Pyrococcus abyssi strain GE5 in the invasive cleavage assay taught by Ogino et al., in view of the prior arts of Ogino et al., and the amino acid sequence of Flap endonuclease-1 (FEN-1) from Pyrococcus abyssi strain GE5.
Furthermore, the motivation to make the substitution cited above arises from the expectation that the prior art elements will perform their expected functions to achieve their expected results when combined for their common known purpose. Support for making the obviousness rejection comes from the M.P.E.P. at 2144.06, 2144.07 and 2144.09.
Also note that there is no invention involved in combining old elements is such a manner that these elements perform in combination the same function as set forth in the prior art without giving unobvious or unexpected results. In re Rose 220 F.2d. 459, 105 USPQ 237 (CCPA 1955).
Claims 1-8, 10-12, 16, and 17 are rejected under 35 U.S.C. 103 as being unpatentable over Ogino et al., (WO 2019/026884 A1, published on February 7, 2019) in view of the amino acid sequence of the flap structure-specific endonuclease from Thermococcus kodakarensis strain KOD1 (available in GenBank since September 29, 2018, see IDS filed on September 22, 2022).
The teachings of Ogino et al., have been summarized previously, supra. Ogino et al., teach all limitations recited in claims 1-8, 10-12, and 16 (see above rejection under 35 U.S.C. 103 related to the Rejection Item No. 15).
Ogino et al., do not disclose that the flap endonuclease has an amino acid sequence having a sequence identity of 96% or higher with the amino acid sequence of the flap endonuclease from Thermococcus kodakarensis strain KOD1 as recited in claims 1 and 17.
An amino acid sequence of the flap structure-specific endonuclease from Thermococcus kodakarensis strain KOD1 is available in GenBank since September 29, 2018.
Therefore, it would have been prima facie obvious to one having ordinary skill in the art at the time the invention was made to have performed the methods recited in claims 1 and 17 using an flap endonuclease which has an amino acid sequence having a sequence identity of 96% or higher with the amino acid sequence of the flap endonuclease from Thermococcus kodakarensis strain KOD1 in view of the prior arts of Ogino et al., and the amino acid sequence of the flap structure-specific endonuclease from Thermococcus kodakarensis strain KOD1. One having ordinary skill in the art would have been motivated to do so because the amino acid sequence of flap structure-specific endonuclease from Thermococcus kodakarensis strain KOD1 is available in GenBank since September 29, 2018 and the simple substitution of one kind of flap endonuclease (ie., the FEN-1 taught by Ogino et al.,) from another kind of flap endonuclease (ie., the flap structure-specific endonuclease from Thermococcus kodakarensis strain KOD1 which is available in GenBank since September 29, 2018), in the absence of convincing evidence to the contrary, would have been prima facie obvious to one having ordinary skill in the art at the time the invention was made since the FEN-1 taught by Ogino et al., and the flap structure-specific endonuclease from Thermococcus kodakarensis strain KOD1 which is available in GenBank since September 29, 2018 are used for the same purpose (ie., used for an invasive cleavage assay). One having ordinary skill in the art at the time the invention was made would have a reasonable expectation of success to perform the methods recited in claims 1 and 17 by making the flap structure-specific endonuclease from Thermococcus kodakarensis strain KOD1 which is available in GenBank since September 29, 2018 based on its amino acid sequence in GenBank and substituting the FEN-1 taught by Ogino et al., from Thermococcus kodakarensis strain KOD1 in the invasive cleavage assay taught by Ogino et al., in view of the prior arts of Ogino et al., and the amino acid sequence of the flap structure-specific endonuclease from Thermococcus kodakarensis strain KOD1.
Furthermore, the motivation to make the substitution cited above arises from the expectation that the prior art elements will perform their expected functions to achieve their expected results when combined for their common known purpose. Support for making the obviousness rejection comes from the M.P.E.P. at 2144.06, 2144.07 and 2144.09.
Also note that there is no invention involved in combining old elements is such a manner that these elements perform in combination the same function as set forth in the prior art without giving unobvious or unexpected results. In re Rose 220 F.2d. 459, 105 USPQ 237 (CCPA 1955).
Claims 1-8, 10-12, 16, and 19 are rejected under 35 U.S.C. 103 as being unpatentable over Ogino et al., (WO 2019/026884 A1, published on February 7, 2019) in view of the amino acid sequence of the flap endonuclease-1 from Methanothermobacter thermautotrophicus strain Delta H (integrated into UniProtKB/Swiss-Prot on February 12, 2003).
The teachings of Ogino et al., have been summarized previously, supra. Ogino et al., teach all limitations recited in claims 1-8, 10-12, and 16 (see above rejection under 35 U.S.C. 103 related to the Rejection Item No. 15).
Ogino et al., do not disclose that the flap endonuclease has an amino acid sequence having a sequence identity of 96% or higher with the amino acid sequence of the flap endonuclease from Methanothermobacter thermautotrophicus strain Delta H as recited in claims 1 and 19.
The amino acid sequence of the flap endonuclease from Methanothermobacter thermautotrophicus strain Delta H is integrated into UniProtKB/Swiss-Prot on February 12, 2003.
Therefore, it would have been prima facie obvious to one having ordinary skill in the art at the time the invention was made to have performed the methods recited in claims 1 and 19 using an flap endonuclease which has an amino acid sequence having a sequence identity of 96% or higher with the amino acid sequence of the flap endonuclease from Methanothermobacter thermautotrophicus strain Delta H in view of the prior arts of Ogino et al., and the amino acid sequence of the flap endonuclease from Methanothermobacter thermautotrophicus strain Delta H. One having ordinary skill in the art would have been motivated to do so because the amino acid sequence of the flap endonuclease from Methanothermobacter thermautotrophicus strain Delta H is integrated into UniProtKB/Swiss-Prot on February 12, 2003 and the simple substitution of one kind of flap endonuclease (ie., the FEN-1 taught by Ogino et al.,) from another kind of flap endonuclease (ie., the flap endonuclease from Methanothermobacter thermautotrophicus strain Delta H which is integrated into UniProtKB/Swiss-Prot on February 12, 2003), in the absence of convincing evidence to the contrary, would have been prima facie obvious to one having ordinary skill in the art at the time the invention was made since the FEN-1 taught by Ogino et al., and the flap endonuclease from Methanothermobacter thermautotrophicus strain Delta H which is integrated into UniProtKB/Swiss-Prot on February 12, 2003 are used for the same purpose (ie., used for an invasive cleavage assay). One having ordinary skill in the art at the time the invention was made would have a reasonable expectation of success to perform the methods recited in claims 1 and 19 by making the flap endonuclease from Methanothermobacter thermautotrophicus strain Delta H based on its amino acid sequence and substituting the FEN-1 taught by Ogino et al., from the flap endonuclease from Methanothermobacter thermautotrophicus strain Delta H in the invasive cleavage assay taught by Ogino et al., in view of the prior arts of Ogino et al., and the amino acid sequence of the flap endonuclease from Methanothermobacter thermautotrophicus strain Delta H.
Furthermore, the motivation to make the substitution cited above arises from the expectation that the prior art elements will perform their expected functions to achieve their expected results when combined for their common known purpose. Support for making the obviousness rejection comes from the M.P.E.P. at 2144.06, 2144.07 and 2144.09.
Also note that there is no invention involved in combining old elements is such a manner that these elements perform in combination the same function as set forth in the prior art without giving unobvious or unexpected results. In re Rose 220 F.2d. 459, 105 USPQ 237 (CCPA 1955).
Claim 9 is rejected under 35 U.S.C. 103 as being unpatentable over Ogino et al., in view of the amino acid sequence of the flap endonuclease-1 (FEN-1) from Pyrococcus abyssi strain GE5 as applied to claims 1-8, 10-12, 16, and 18 above
The teachings of Ogino et al., the amino acid sequence of Flap endonuclease-1 (FEN-1) from Pyrococcus abyssi strain GE5 have been summarized previously, supra.
Ogino et al., do not disclose that the amino acid sequence of Flap endonuclease-1 (FEN-1) from Pyrococcus abyssi strain GE5 do not disclose that a concentration of the flap endonuclease in the aqueous solvent is 0.5 µM or greater to 8 µM or less as recited in claim 9. However, Ogino et al., teach that said cleaving a first flap of a first cleave structure and said cleaving a second flap of a second cleave structure are carried out in an aqueous solvent as recited in claim 9 wherein the concentration of Flap nuclease in the assay is 0.03 mg/ml (see paragraph [0127]). Since the molecular weight of Flap endonuclease-1 (FEN-1) from Pyrococcus abyssi strain GE5 is about 37730 Da (343×110 (number of amino acid× average molecular weight of an amino acid)), the concentration of Flap endonuclease-1 (FEN-1) from Pyrococcus abyssi strain GE5 in the assay in claim 1 should be 0.795 µM.
Therefore, it would have been prima facie obvious to one having ordinary skill in the art at the time the invention was made to have performed the method recited in claim 9 wherein a concentration of the flap endonuclease in the aqueous solvent is from 0.5 µM to 8 µM in view of the prior arts of Ogino et al., and the amino acid sequence of Flap endonuclease-1 (FEN-1) from Pyrococcus abyssi strain GE5. One having ordinary skill in the art would have been motivated to do so because Ogino et al., teach that the concentration of Flap nuclease in the assay is 0.03 mg/ml (see paragraph [0127] which is 0.795 µM. One having ordinary skill in the art at the time the invention was made would have a reasonable expectation of success to perform the method recited in claim 9 using 0.03 mg/ml of the flap endonuclease-1 (FEN-1) from Pyrococcus abyssi strain GE5 in view of the prior arts of Ogino et al., and the amino acid sequence of the flap endonuclease-1 (FEN-1) from Pyrococcus abyssi strain GE5 such that said cleaving a first flap of a first cleave structure and said cleaving a second flap of a second cleave structure would be carried out in an aqueous solvent, and a concentration of the flap endonuclease from Pyrococcus abyssi strain GE5 in the aqueous solvent is from 0.5 µM to 8 µM.
Response to Arguments
In page 14, sixth paragraph bridging to page 16, second paragraph of applicant’s remarks, applicant argues that “[A]pplicant’s claimed invention to be based, in part, upon the selection of flap endonuclease that has an amino acid sequence having a sequence identity of 96% or higher with the amino acid sequence of a flap endonuclease of one of the three microbes recited in claims 1 and 14, from among all the microbes identified in Table 1 of the specification. Accordingly, there is no basis for the Examiner's assumption that one skilled in the art would choose any of the three microbes recited in claims 1 and 14. More particularly, there is no
basis for one skilled in the art to expect the superior S/N values reported in the specification,
especially in Table 4 of the specification. The S/N ratio data in that table was obtained by calculating the ratio between the red fluorescence intensity (signal) in the case where the concentration of the target nucleic acid was1.5 pM at the time point after 30 minutes from the initiation of reaction and the red fluorescence intensity (noise) in the case where the concentration of the target nucleic acid was OM. The results are shown in Table 4. That data shows that unexpectedly superior S/N ratio values are obtained with Tko, which is representative of the three microbes recited in claims 1 and 14. That data also shows that Applicant's superior S/N values are strong across a range enzyme concentrations. The data Tables 5 to 9 show that these superior S/N values are especially strong under when pH, temperature, Mg²⁺ concentration, K⁺ concentration, and tris concentration conditions meet the requirements of claims 3-8”.
The above arguments have been fully considered but they are not persuasive toward the withdrawal of the rejection.
First, although applicant argues that “there is no basis for the Examiner's assumption that one skilled in the art would choose any of the three microbes recited in claims 1 and 14”, since the amino acid sequence of the flap endonuclease from each of Thermococcus kodakarensis strain KOD1, Methanothermobacter thermautotrophicus strain Delta H, and Pyrococcus abyssi strain GE5 are well known in the art (see above rejection under 35 U.S.C 103), one having ordinary skill in the art would have been motivated to perform the method recited in claim 1 or 17 or 18 or 19 by “obvious to try” substituting the FEN-1 taught by Ogino et al., from the flap endonuclease from Thermococcus kodakarensis strain KOD or the flap endonuclease from Pyrococcus abyssi strain GE5 or the flap endonuclease from Methanothermobacter thermautotrophicus strain Delta H (MPEP 2144.05) because the FEN-1 taught by Ogino et al., and the flap endonuclease from Thermococcus kodakarensis strain KOD or the flap endonuclease from Pyrococcus abyssi strain GE5 or Methanothermobacter thermautotrophicus strain Delta H are used for the same purpose (ie., used for an invasive cleavage assay). Furthermore, one having ordinary skill in the art at the time the invention was made would have a reasonable expectation of success to perform the method recited in claim 1 or 17 or 18 or 19 using the flap endonuclease from Thermococcus kodakarensis strain KOD or the flap endonuclease from Pyrococcus abyssi strain GE5 or the flap endonuclease from Methanothermobacter thermautotrophicus strain Delta H in the invasive cleavage assay taught by Ogino et al..
Second, although applicant argues that there is no basis for one skilled in the art to expect the superior S/N values reported in the specification, especially in Table 4 of the specification”, there is no S/N values in the claims. Although the claims are interpreted in light of the specification, limitations from the specification are not read into the claims. See In re Van Geuns, 988 F.2d 1181, 26 USPQ2d 1057 (Fed. Cir. 1993).
Double Patenting
The nonstatutory double patenting rejection is based on a judicially created doctrine grounded in public policy (a policy reflected in the statute) so as to prevent the unjustified or improper timewise extension of the “right to exclude” granted by a patent and to prevent possible harassment by multiple assignees. A nonstatutory double patenting rejection is appropriate where the conflicting claims are not identical, but at least one examined application claim is not patentably distinct from the reference claim(s) because the examined application claim is either anticipated by, or would have been obvious over, the reference claim(s). See, e.g., In re Berg, 140 F.3d 1428, 46 USPQ2d 1226 (Fed. Cir. 1998); In re Goodman, 11 F.3d 1046, 29 USPQ2d 2010 (Fed. Cir. 1993); In re Longi, 759 F.2d 887, 225 USPQ 645 (Fed. Cir. 1985); In re Van Ornum, 686 F.2d 937, 214 USPQ 761 (CCPA 1982); In re Vogel, 422 F.2d 438, 164 USPQ 619 (CCPA 1970); In re Thorington, 418 F.2d 528, 163 USPQ 644 (CCPA 1969).
A timely filed terminal disclaimer in compliance with 37 CFR 1.321(c) or 1.321(d) may be used to overcome an actual or provisional rejection based on nonstatutory double patenting provided the reference application or patent either is shown to be commonly owned with the examined application, or claims an invention made as a result of activities undertaken within the scope of a joint research agreement. See MPEP § 717.02 for applications subject to examination under the first inventor to file provisions of the AIA as explained in MPEP § 2159. See MPEP § 2146 et seq. for applications not subject to examination under the first inventor to file provisions of the AIA . A terminal disclaimer must be signed in compliance with 37 CFR 1.321(b).
The filing of a terminal disclaimer by itself is not a complete reply to a nonstatutory double patenting (NSDP) rejection. A complete reply requires that the terminal disclaimer be accompanied by a reply requesting reconsideration of the prior Office action. Even where the NSDP rejection is provisional the reply must be complete. See MPEP § 804, subsection I.B.1. For a reply to a non-final Office action, see 37 CFR 1.111(a). For a reply to final Office action, see 37 CFR 1.113(c). A request for reconsideration while not provided for in 37 CFR 1.113(c) may be filed after final for consideration. See MPEP §§ 706.07(e) and 714.13.
The USPTO Internet website contains terminal disclaimer forms which may be used. Please visit www.uspto.gov/patent/patents-forms. The actual filing date of the application in which the form is filed determines what form (e.g., PTO/SB/25, PTO/SB/26, PTO/AIA /25, or PTO/AIA /26) should be used. A web-based eTerminal Disclaimer may be filled out completely online using web-screens. An eTerminal Disclaimer that meets all requirements is auto-processed and approved immediately upon submission. For more information about eTerminal Disclaimers, refer to www.uspto.gov/patents/apply/applying-online/eterminal-disclaimer.
Claims 1-12 and 16-19 are provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-13 and 17-23 of copending Application No. 17/912, 220 (reference application). Although the conflicting claims are not identical, they are not patentably distinct from each other because the examined claims in this instant application are either anticipated by, or would have been obvious over, the reference claims. See In re Goodman, 11 F.3d 1046, 29 USPQ2d 2010 (Fed. Cir. 1993); In re Longi, 759 F.2d 887, 225 USPQ 645 (Fed. Cir. 1985); In re Van Ornum, 686 F.2d 937, 214 USPQ 761 (CCPA 1982); In re Vogel, 422 F.2d 438, 164 USPQ 619 (CCPA 1970); and, In re Thorington, 418 F.2d 528, 163 USPQ 644 (CCPA 1969). Although claims 1-12 and 16-19 in this instant application are not identical to claims 1-13 and 17-23 of copending Application No. 17/912, 220 (reference application), since the phrase “the flap endonuclease has an amino acid sequence having a sequence identity of 65% or higher with an amino acid sequence of a flap endonuclease of a microbe selected from the group consisting of microbes belonging to Thermococcus kodakarensis strain KOD1 and Pyrococcus abyssi strain GE5 and Methanothermobacter Thermautotrophicus strain Delta H” in claim 2 of copending Application No. 17/912, 220 can be reasonably read as “the flap endonuclease has an amino acid sequence having a sequence identity of 96% or higher with an amino acid sequence of a flap endonuclease of a microbe selected from the group consisting of microbes belonging to Thermococcus kodakarensis strain KOD1, Pyrococcus abyssi strain GE5, and Methanothermobacter Thermautotrophicus strain Delta H”, claims 1-13 and 17-23 of copending Application No. 17/912, 220 are directed to the same subject matter and fall entirely within the scope of claims 1-12 and 16-19 in this instant application. In other words, claims 1-12 and 16-19 in this instant application are anticipated by claims 1-13 and 17-23 of copending Application No. 17/912, 220.
This is a provisional nonstatutory double patenting rejection because the patentably indistinct claims have not in fact been patented.
Conclusion
Applicant’s submission of an information disclosure statement under 37 CFR 1.97(c) with the timing fee set forth in 37 CFR 1.17(p) on October 20, 2025 prompted the new ground(s) of rejection presented in this Office action. Accordingly, THIS ACTION IS MADE FINAL. See MPEP § 609.04(b). Applicant is reminded of the extension of time policy as set forth in 37 CFR 1.136(a).
Applicant's submission of an information disclosure statement under 37 CFR 1.97(c) with the timing fee set forth in 37 CFR 1.17(p) on October 29, 2025 prompted the new ground(s) of rejection presented in this Office action. Accordingly, THIS ACTION IS MADE FINAL. See MPEP § 609.04(b). 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.
23. No claim is allowed.
24. Papers related to this application may be submitted to Group 1600 by facsimile transmission. Papers should be faxed to Group 1600 via the PTO Fax Center. The faxing of such papers must conform with the notices published in the Official Gazette, 1096 OG 30 (November 15, 1988), 1156 OG 61 (November 16, 1993), and 1157 OG 94 (December 28, 1993)(See 37 CAR § 1.6(d)). The CM Fax Center number is (571)273-8300.
Any inquiry concerning this communication or earlier communications from the examiner should be directed to Frank Lu, Ph.D., whose telephone number is (571)272-0746. The examiner can normally be reached on Monday-Friday from 9 A.M. to 5 P.M.
If attempts to reach the examiner by telephone are unsuccessful, the examiner's supervisor, Dr. Anne Gussow, Ph.D., can be reached on (571)272-6047.
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/FRANK W LU/Primary Examiner, Art Unit 1683
January 21, 2026