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 .
DETAILED ACTION
1. Applicant’s amendment and response filed 6/17/26 is acknowledged and has been entered.
2. Applicant is reminded of Applicant's election without traverse of Group I and species of SEQ ID NO: 15, a fusion protein comprising in N- to -C-terminal order: peptide P12 (SEQ ID NO: 32)-GS linker that is SEQ ID NO: 1, (G4S)3-b2m peptide (SEQ ID NO: 81). It is noted by the Examiner that there is additionally an N-terminal sequence in SEQ ID NO: 15 that is a signal peptide, i.e., MSRSVALAVLALLSLSGLEA or SEQ ID NO: 3, a 20 amino acid signal peptide (see [00379] of the instant specification).
Claims 101, 107, 109-113, 115 and newly added claims 136 and 137 read on the elected species.
Claims 101, 107, 109-113, 115, 136 and 137 are presently being examined as they read upon the elected species and upon the species enunciated below in the art rejection.
Claim 101 is an independent claim.
3. Claim interpretation: The specification discloses at [0087] that the term “presenting peptide” as used herein refers to short peptides that can stably bind to the antigen binding groove of an MHC to form a stable MHC complex that can be recognized by receptors on immune cells. The specification further discloses at [0088] that each MHC has its own matched presenting peptides, and that a presenting peptide that is “restricted” to a particular MHC molecule means that the presenting peptide can form a stable complex with this particular MHC molecule. The specification further discloses at [0082] that MHC complexes include class I MHC molecules that comprise a polymorphic heavy chain (or class I MHC alpha chain), and a light chain which is b2m, and that in humans classic class I MHC include HLA-A, -B and -C and nonclassical class I MHC include HLA-E, -F and -G. The specification discloses at [0084] that the term “b2m peptide” refers to the full length protein of b2m or a functional fragment or variant thereof. The specification further discloses that the mature form of human b2m does not include the signal peptide and consists of 99 amino acid residues and corresponds to the sequence consisting of that depicted in SEQ ID NO: 81. The specification discloses at [0086] that the term “variant” in relation to a protein or a polypeptide refers to a different protein or polypeptide (than the reference protein or polypeptide) comprising one or more amino acid substitutions, deletions, and/or additions as compared to the reference protein or polypeptide, and a functional fragment or variant of a protein or polypeptide maintains the basic structural and functional properties of the reference protein or polypeptide. The specification discloses at [0089] that the term “inhibitory receptor” refers to the receptor molecule expressed on the surface of the immune cell that can inhibit the activity of the immune cells upon binding to its ligand. Note that the claimed fusion protein is not isolated. Also note that there is no limiting definition in the specification for the limitation “about”.
The Examiner notes that although the specification at [00129] discloses that “For example, the amino acid sequence of one allelic form of human HLA-E heavy chain corresponds to the sequence having GenBank No. ARB08449.1…”, it also discloses at [00109] that “Exemplary genes and polypeptides are described herein with reference to GenBank numbers, GI numbers and/or SEQ ID NOS.” Applicant has presently stated on the record (in the amendment and response filed 6/17/26) in response to the indefiniteness rejection made in the prior office action of record that the limitation “HLA-E heavy chain” refers to the HLA-E-gene-encoded alpha polypeptide chain, but not to the extracellular domain thereof (see Applicant’s response at the paragraph spanning pages 11-12). Therefore, the limitation “lacks and HLA-E heavy chain” recited in instant base claim 101 is being interpreted as the fusion protein may comprise an HLA-E extracellular domain (ECD) that does not further comprise the TM and cytoplasmic domains in the HLA-E gene-encoded alpha polypeptide chain (and/or is being interpreted as comprising a different HLA than HLA-E heavy chain or ECD thereof). That is, a soluble construct comprising the recited presenting peptide covalently linked to a b2m peptide with a linker may further comprise the ECD of HLA-E heavy chain or a different HLA heavy chain or ECD thereof other than HLA-E.
4. Applicant’s amendment filed 6/17/26 has overcome the prior rejection of record of claims 101-106, 109-113, 115 and 135 are rejected under 35 U.S.C. 112(a) or 35 U.S.C. 112 (pre-AIA ), first paragraph, as failing to comply with the written description requirement.
Applicant has amended the claims to recite a genus of fully defined presenting peptides comprised in the claimed fusion protein, and has canceled claims 102-106 and 135.
5. Applicant’s amendment filed 6/17/26 has overcome the prior rejection of record of claims 101-107, 109-113, 115 and 135 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.
6. 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.
7. For the purpose of prior art rejections, the filing date of the instant claims is deemed to be the filing date of PCT/CN2019/124321, i.e., 12/10/19. Applicant has presently provided a certified translation of China 201910746355. However, this latter said document does not provide support for the structural formula as recited in instant base claim 101, i.e., it is missing “I” at position 1 (P1), Q at P5, A at P6, and T at P8. The said document also does not provide support for SEQ ID NO: 29, SEQ ID NO: 30, SEQ ID NO: 31, SEQ ID NO: 35, and SEQ ID NO: 37. Although the said document has support for a chimeric single chain molecule that is one of SEQ ID NO: 5 or SEQ ID NO: 13, and also has support for the components of SEQ ID NO: 14-17 (and the b2m portion thereof is identical to instantly recited SEQ ID NO: 81), it does not have support for an amino acid sequence at least 95% identical thereto, nor one at least 95% to amino acid residues 21-143 thereof of SEQ ID NO: 5 or 13-17. The said document also does not provide support for the limitation in claim 113 “wherein the amino acid sequence of the b2M peptide is at least 85%...identical to SEQ ID NO: 81.” The only support in the said document is the species that is 100% identical to SEQ ID NO: 81.
8. Applicant’s amendment filed 6/17/26 has overcome the prior rejection of record of claims 101-107, 109-113, 115 and 135 under 35 U.S.C. 102(a)(2) as being anticipated by US2021/0268028 A1 (pgPub of 17/256,434, priority to at least 6/14/19, of record) or WO 2020/007593 A1 (PCT/EP2019/065761, priority to at least 6/14/19, of record), as evidenced by Kremer et. al. (Stem Cells International, 2015, article ID 346714, pages 1-12, of record).
Applicant has amended instant base claim 101 to recite that the fusion protein lacks an HLA-E heavy chain and has stated on the record that the limitation “HLA-E heavy chain” refers to the HLA-E-gene-encoded alpha polypeptide chain, but not to the extracellular domain thereof (see Applicant’s response at the paragraph spanning pages 11-12).
In contrast, the art reference teaches a fusion protein that comprises the entire HLA-E alpha polypeptide chain (and that the sequence of one allelic form of human HLA-E heavy chain corresponds to the sequence having GenBank No. ARB08449.1 (which is 358 amino acid residues in length); thus the art reference does not meet the present claim limitation “lacks and HLA-E heavy chain.
9. 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.
10. Claims 101, 107 and 110-113 are rejected under 35 U.S.C. 102(a)(2) as being anticipated by WO2020097188 A1 (priority to at least 11/6/19, of record), as is evidenced by A_Geneseq_202544 BHU30189 (2020, 2 pages, of record) shown below.
This is a new ground of rejection necessitated by Applicant’s amendment filed 6/17/26. Applicant has amended instant base claim 101 to recite a specific presenting peptide and has deleted recitation that the fusion protein comprises less than 500 amino acids and has stated on the record that the limitation “lacks an HLA-E heavy chain” refers to lack of a full length heavy chain that is an HLA-Encoded heavy chain, but does not refer to the extracellular domain of the HLA-E heavy chain.
Independent claim 101 recites: “A fusion protein comprising a presenting peptide covalently linked to a beta-2- microglobulin (b2M) peptide via a linker” wherein the presenting peptide comprises the recited structural formula with fully defined residues, “and wherein the fusion protein lacks an HLA-E heavy chain.”
Note that the art reference sequence is 477 amino acid residues in length and lacks an HLA-E heavy chain as is evidenced by evidentiary reference A_Geneseq_202544 BHU30189 (2020) shown below.
WO2020097188 A1 teaches a sequence that comprises a sequence that is identical to instantly recited SEQ ID NO: 15 that inhibits NK mediated cell killing (see entire reference, especially Table A at SEQ ID NO: 8 (second entry in the table)). Instantly recited SEQ ID NO: 15 is depicted below as “Qy”, while the portion of the art reference sequence that is identical to instantly recited SEQ ID NO: 15 is depicted below as “Db”. WO2020097188 A1 teaches at Table A that SEQ ID NO: 8 of the art reference comprises the VMAPRTLFL sequence (which is identical to instantly recited SEQ ID NO: 32, Applicant’s elected species) and the linker between the peptide and the b2m sequence portion of the fusion protein is (GGGGS)3 which is identical to instantly recited SEQ ID NO: 112 and also to SEQ ID NO: 1 that are recited in instant dependent claims 111 and 112, respectively.
The amino acid sequence of the b2m peptide portion of the fusion protein is 100% identical to instantly recited SEQ ID NO: 81. The remainder of the fusion C-terminal to the b2m consists of a second linker and the sequence of an HLA-G heavy chain. Thus, the art sequence meets the instant claim limitation of “wherein the fusion protein lacks an HLA-E heavy chain.” The length of the entire amino acid sequence is 477.
A_Geneseq_202544 BHU30189
ID BHU30189 standard; protein; 477 AA.
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AC BHU30189;
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DT 09-JUL-2020 (first entry)
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DE HLA-G trimer protein, SEQ ID 8.
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KW HLA class I antigen alpha G; HLA-G protein; autoimmune disease; cancer;
KW cytostatic; immunosuppressive; protein identification; protein therapy;
KW screening; therapeutic.
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OS Homo sapiens.
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CC PN WO2020097188-A1.
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CC PD 14-MAY-2020.
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CC PF 06-NOV-2019; 2019WO-US060045.
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PR 06-NOV-2018; 2018US-0756411P.
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CC PA (SAGM ) SANGAMO THERAPEUTICS INC.
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CC PI Conway A, De Almeida P, Jain S, Spelman M;
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DR WPI; 2020-42031S/042.
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CC PT Identifying molecule that reduces or prevents natural killer (NK)-
CC PT mediated killing of donor cell involves e.g. incubating genetically
CC PT modified donor cells of molecule with effector NK cells and incubating
CC PT cell mixture with dye and antibody.
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CC PS Disclosure; SEQ ID NO 8; 118pp; English.
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CC The present invention relates to a method for identifying a molecule that
CC reduces or prevents natural killer (NK)-mediated killing of a donor cell.
CC The method involves (a) incubating genetically modified donor cells
CC comprising the molecule with effector NK cells; (b) incubating the cell
CC mixture of step (a) cells with at least one dye and an antibody that
CC binds to cleaved caspase-3, where the dyes preferentially accumulate in
CC live or dead cells; (c) analyzing the donor cells for viability based on
CC accumulation of the dyes; and (d) analyzing apoptosis in the donor cells
CC by evaluating cleaved caspase-3 levels, where an increase of live or non-
CC apeptotic genetically modified donor cells as compared to control cells
CC is indicative that the molecule reduces or prevents NK- mediated killing
CC of the donor cell. The invention also provides: a molecule identified by
CC the method, where the molecule is a protein expressed on the cell surface
CC of the donor cell; and a composition comprising a population of donor
CC cells and at least one molecule. The method of the invention is useful
CC for treating cancer, autoimmune disease, or a tissue or cell graft.
XX
SQ Sequence 477 AA;
Query Match 100.0%; Score 752; Length 477;
Best Local Similarity 100.0%;
Matches 143; Conservative 0; Mismatches 0; Indels 0; Gaps 0;
Qy 1 MSRSVALAVLALLSLSGLEAVMAPRTLFLGGGGSGGGGSGGGGSIQRTPKIQVYSRHPAE 60
Db 1 MSRSVALAVLALLSLSGLEAVMAPRTLFLGGGGSGGGGSGGGGSIQRTPKIQVYSRHPAE 60
Qy 61 NGKSNFLNCYVSGFHPSDIEVDLLKNGERIEKVEHSDLSFSKDWSFYLLYYTEFTPTEKD 120
Db 61 NGKSNFLNCYVSGFHPSDIEVDLLKNGERIEKVEHSDLSFSKDWSFYLLYYTEFTPTEKD 120
Qy 121 EYACRVNHVTLSQPKIVKWDRDM 143
Db 121 EYACRVNHVTLSQPKIVKWDRDM 143
The presenting peptide and the b2m portions are underlined, whereas the glycine-serine linker is italicized.
Applicant’s arguments have been fully considered but are not persuasive.
Applicant’s said arguments are of record in the amendment and response filed 6/17/26 at section “D”.
Applicant argues that with the filing of a certified English translation of China CN201910746355.8, the priority date that the instant application is entitled to is 8/13/19, the filing date of the said application.
However, the priority date for the purpose of prior art rejections is deemed to be the filing date of PCT/ CN2019/124321, i.e., 12/10/19, for the reasons enunciated above at item #7 of this office action. Therefore WO2020097188 A1 having priority to at least 11/6/19, is available as prior art.
Applicant’s further argument regarding SEQ ID NO: 9 of the art reference is off-point, as the art reference is not relying on a teaching of SEQ ID NO: 9, but rather of SEQ ID NO: 8. Applicant’s argument stating that the art reference discloses sequences that incorporate the HLA-E heavy chain as part of the molecule and therefore do not embody the design principle of the instant application and do not anticipate the instant claims is also off-point, as the art reference teaches a sequence that meets the claim limitations, including not comprising a HLA-E heavy chain. Applicant’s argument alleging advantages of a peptide-linker-b2m construct as opposed to one further comprising an HLA-E heavy chain are also off-point, as the art reference teaches a sequence that meets the claim limitations and as the instant rejection is anticipation, not obviousness.
11. 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.
12. Court rulings have been quite clear that ONLY DIVISIONAL applications are entitled to the shield from double patenting under 35 USC 121. Indeed, in AMGEN INC v. HOFFMANN LA ROCHE LTD GMBH LA (Nos. 2009-1020, 2009-1096) the court discusses this issue at length and states:
Turning to the legislative history, the court observed that a House Report also referred specifically to “divisional application[s].” Id. Notably absent from the legislative history, in the court's view, was a suggestion “that the safe-harbor provision was, or needed to be, directed at anything but divisional applications.” Id. at 1361. From there, the court “conclude^] that the protection afforded by section 121 to applications (or patents issued therefrom) filed as a result of a restriction requirement is limited to divisional applications.” Id. at 1362. Accordingly, the court decided that the § 121 safe harbor did not apply to the patent before it, which issued from a continuation-in-part application. Id.
We are persuaded by the reasoning in Pfizer that the § 121 safe harbor provision does not protect continuation applications or patents descending from only continuation applications. The statute on its face applies only to divisional applications, and a continuation application, like a continuation-in-part application, is not a divisional application.
Given that Applicant chose to file the 18/294,928 case as a separate unrelated application, not as a DIV of the instant application, the instant rejection has been set forth.
Claims 101, 107, 109-113, 115, 136 and 137 are provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-3, 5, 12-14, 16, 17, 28, 30, 34-36, 39, 42, 43, 47, 50, 51, 62-64, 74, 116, 123, 141, 147, 155, 157, 158 and 160-163 of copending Application No. 18/294,928.
This is a new ground of rejection necessitated by Applicant’s amendment filed 6/17/2026. Applicant has amended the claims and has added new claims 136 and 137.
Claims 1-3, 5, 12-14, 16, 17, 28, 30, 34-36, 39, 42, 43, 47, 50, 51, 62, 63 and 155 of 18/294,928 are drawn to a modified cell comprising a fusion protein comprising VMAPRTLFL (SEQ ID NO: 29 of ‘928 that is identical to instantly recited SEQ ID NO: 32, Applicant’s elected species), a glycine serine linker that is (G4S)3 (SEQ ID NO: 99 of ‘928 that is identical to instantly recited SEQ ID NO: 1), and mature b2m, and wherein the fusion protein that forms a complex is capable of inhibiting an immune cell. The fusion protein may also comprise a signal sequence peptide.
Claims 63, 74, 116, 123, 141, 147 and 161 of 18/294,928 are drawn to a nucleic acid sequence encoding the said fusion protein/pharmaceutical composition thereof and a method for preparing the modified cell by inserting the said polynucleotide into a cell.
Claims 157 and 158 of 18/294,928 are drawn to a method for allogeneic transplantation comprising administering the said modified cell.
Claim 160 of 18/294,928 is drawn to a method for treating a tumor comprising administering the modified cell.
Claim 162 of 18/294,928 is drawn to a method for allogenic transplantation comprising administering the isolated nucleic acid molecule.
Claim 163 of 18/294,928 is drawn to a method for treating a tumor comprising administering the isolated nucleic acid molecule.
Please note that the fusion protein has the same peptide and linker as well as a mature b2m. An obvious variant of a mature b2m is mature human b2m (such as that recited in instant claim 113 that is 100% identical to instantly recited SEQ ID NO: 81). As is enunciated above in the claim interpretation section, the specification discloses that the mature form of human b2m does not include the signal peptide and consists of 99 amino acid residues and corresponds to the sequence consisting of that depicted in SEQ ID NO: 81.
Therefore with regard to instant claim 113 (and also to instant claim 115 that recites sequences that comprise instantly recited SEQ ID NO: 81), it would have been prima facie obvious to one of ordinary skill in the art before the filing date of the claimed invention to have used mature human b2m as the mature b2m in the fusion protein. One of ordinary skill in the art would have been motivated to do this, and with a reasonable expectation of success in doing so, in order to make a composition for human use. Please also note that the fusion protein is 123 amino acid residues (9-mer signal sequence peptide-15-mer amino acid residue linker-human mature b2m of 99 amino acid residues in length). The fusion protein recited in the claims of 18/294,928 is not isolated. None-the-less, it would have been prima facie obvious to one of ordinary skill in the art to have made an isolated version of the fusion protein as per the teaching of IDS reference Tafuro et. al. (Eur. J. Immunol. 2001, 31: 440-449, IDS reference) who teach that an epitope peptide linked to the N-terminus of human b2m refolded efficiently in vitro and could be used to bind specifically to cognate immune cells when multimerized with a class I MHC heavy chain (see entire reference). One of ordinary skill in the art would have been motivated to do this, and with a reasonable expectation of success in doing so, for that reason. Alternatively, it would have been prima facie obvious to one of ordinary skill in the art to have made an isolated version of the fusion protein as per the teaching of IDS reference Uger et. al. (J. Immunol. 1999, 162: 6024-6028, IDS reference) as Uger et. al. teach that tethering peptide epitopes to human b2m and expressed recombinantly result in enhanced MHC stabilization as compared with the uncoupled counterpart peptide/b2m. One of ordinary skill in the art would have been motivated to do this, and with a reasonable expectation of success in doing so, for that reason.
Instant claims 109, 136 and 137 are included in this rejection because the peptide-linker-mature b2m fusion protein is 123 amino acid residues in length (i.e., 9-mer peptide plus 15-mer linker plus 99 amino acid residue mature human b2m peptide).
This is a provisional nonstatutory double patenting rejection because the patentably indistinct claims have not in fact been patented.
Claims 101, 107, 109-113, 115, 136 and 137 are directed to an invention not patentably distinct from claims 1-3, 5, 12-14, 16, 17, 28, 30, 34-36, 39, 42, 43, 47, 50, 51, 62-64, 74, 116, 123, 141, 147, 155, 157, 158 and 160-163 of commonly assigned 18/294,928, as enunciated supra.
The U.S. Patent and Trademark Office may not institute a derivation proceeding in the absence of a timely filed petition. The USPTO normally will not institute a derivation proceeding between applications or a patent and an application having common ownership (see 37 CFR 42.411). Commonly assigned 18/294,928, discussed above, may form the basis for a rejection of the noted claims under 35 U.S.C. 102 or 103 if the commonly assigned case qualifies as prior art under 35 U.S.C. 102(a)(2) and the patentably indistinct inventions were not commonly owned or deemed to be commonly owned not later than the effective filing date under 35 U.S.C. 100(i) of the claimed invention.
In order for the Examiner to resolve this issue the applicant or patent owner can provide a statement under 35 U.S.C. 102(b)(2)(C) and 37 CFR 1.104(c)(4)(i) to the effect that the subject matter and the claimed invention, not later than the effective filing date of the claimed invention, were owned by the same person or subject to an obligation of assignment to the same person. Alternatively, the applicant or patent owner can provide a statement under 35 U.S.C. 102(c) and 37 CFR 1.104(c)(4)(ii) to the effect that the subject matter was developed and the claimed invention was made by or on behalf of one or more parties to a joint research agreement that was in effect on or before the effective filing date of the claimed invention, and the claimed invention was made as a result of activities undertaken within the scope of the joint research agreement; the application must also be amended to disclose the names of the parties to the joint research agreement.
A showing that the inventions were commonly owned or deemed to be commonly owned not later than the effective filing date under 35 U.S.C. 100(i) of the claimed invention will preclude a rejection under 35 U.S.C. 102 or 103 based upon the commonly assigned case. Alternatively, applicant may take action to amend or cancel claims such that the applications, or the patent and the application, no longer contain claims directed to patentably indistinct inventions.
Applicant’s arguments (of record in the amendment and response at section “E”) are not persuasive, as this double patenting rejection is not the only remaining rejection in this application.
13. Claim 115 is objected to because of the following informality: Applicant has amended the claim to recite “at least 95% or 100% identical”. The limitation “at least 95%” identical includes 100% identical. Appropriate correction is required.
14. No claim is allowed.
15. 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.
16. Any inquiry concerning this communication or earlier communications from the examiner should be directed to MARIANNE DIBRINO whose telephone number is (571)272-0842. The examiner can normally be reached on M, T, Th, F.
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/Marianne DiBrino/
Marianne DiBrino, Ph.D.
Patent Examiner
Group 1640
Technology Center 1600
/MISOOK YU/Supervisory Patent Examiner, Art Unit 1641
Prosecution Insights