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
This application is a US national phase of PCT/US2020/021596, filed March 6, 2020. Applicant’s amendment filed January 20, 2026 is acknowledged.
Claims 1-36, 38-42, and 45-56 are canceled. Claim 37 is amended.
Claims 37, 43 and 44 are pending and under examination.
Claim Objections
The claim set filed 1/20/2026 recites/indicates “38.-42. (Canceled)”, however still recites claims 39-42 as ‘Previously Presented’, which appear to be pending. Applicant’s Remarks filed 1/20/2026 indicate claims 38-42 are canceled, thus needs to properly reflect this on the claim set. Appropriate correction is required.
Claim Rejections - 35 USC § 112
The following is a quotation of the first paragraph of 35 U.S.C. 112(a):
(a) IN GENERAL.—The specification shall contain a written description of the invention, and of the manner and process of making and using it, in such full, clear, concise, and exact terms as to enable any person skilled in the art to which it pertains, or with which it is most nearly connected, to make and use the same, and shall set forth the best mode contemplated by the inventor or joint inventor of carrying out the invention.
The following is a quotation of the first paragraph of pre-AIA 35 U.S.C. 112:
The specification shall contain a written description of the invention, and of the manner and process of making and using it, in such full, clear, concise, and exact terms as to enable any person skilled in the art to which it pertains, or with which it is most nearly connected, to make and use the same, and shall set forth the best mode contemplated by the inventor of carrying out his invention.
Claims 37 and 43-44 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. The claim(s) contains subject matter which was not described in the specification in such a way as to reasonably convey to one skilled in the relevant art that the inventor or a joint inventor, or for applications subject to pre-AIA 35 U.S.C. 112, the inventor(s), at the time the application was filed, had possession of the claimed invention.
Claims 37, 43 and 44 recite a stimulus response element (SRE) comprising human carbonic anhydrase 2 (CA2), wherein the CA2 comprises (i) a L156H mutation as set forth in SEQ ID NO: 210600, (ii) a CA2 and L156H mutation as set forth in SEQ ID NO: 210602, or (iii) a L156H, S172C, F178Y, and E186D mutation as set forth in SEQ ID NO:210756. As currently amended, claims 37 and 43-44 no longer require a CA2 as set forth in SEQ ID NO:11717 or a region thereof comprising amino acids 2-260 relative to SEQ ID NO:11717 with further substitutional mutations. Thus, the claimed genus only requires some mutations, but do not set forth the conserved residues, together with the mutations, to confer the claimed functions. The specification defines SRE comprising CA2 as a destabilizing domain (DD) in whole or in part, and the DD can be derived from different regions of the parent protein (para 64). The specification discloses CA2 DD may include but are not limited to those described in Table 5 and DDs derived from CA2 regions in Table 6 (para 74-75). The specification discloses DD’s may include one or more mutations described in the Tables, and may be conserved or non-conserved substitutions (para 76). The specification discloses the variant sequence may have the same or a similar activity as the reference sequence, alternatively, the variant may have an altered activity (e.g., increased or decreased) relative to a reference sequence, and be 40%-99% identical to the reference polypeptide (para 239).
To satisfy the written description requirement, a patent specification must describe the claimed invention in sufficient detail that one skilled in the art can reasonably conclude that the inventor had possession of the claimed invention. See, e.g., Moba, B.V. v. Diamond Automation, Inc., 325 F.3d 1306, 1319, 66 USPQ2d 1429, 1438 (Fed. Cir. 2003); Vas-Cath, Inc. v. Mahurkar, 935 F.2d at 1563, 19 USPQ2d at 1116. In analyzing whether the written description requirement is met for genus claims, it is first determined whether a representative number of species have been described by their complete structure. In the instant case, the specification merely gives working examples of a mutant library wherein every amino acid within positions 2-260 of SEQ ID NO: 11717 was mutated, fused to a reporter protein, and sorted based on GFP expression levels, as disclosed in Table 16 (para 692). The select constructs were transduced into NIH3T3 cells and responses of the mutants to increasing doses of acetazolamide and celecoxib were assessed (para 693). Clones showing at least a 5-fold increase in GFP expression had their genomic DNA isolated and DRD amplified by PCR, then inserted into a lentiviral vector (para 694). Mutations in cysteine at position 205 were demonstrated as destabilizing the protein, specifically mutations to serine (para 695). CA2 DD were operably linked to CARs to generate tunable CAR constructs (OT-001988 & OT-001989) (para 697). Ligand dependent responses of CA2 mutants to valdecoxib and celecoxib were also measured in Table 25 (para 703).
Next, then, it is determined whether a representative number of species have been sufficiently described by other relevant identifying characteristics, specific features, and functional attributes that would distinguish different members of the claimed genus. In the instant case, the only other identifying characteristics of a CA2 comprising the recited mutations are constructs listed in Tables 5, 6, and 9; and the payload may be a full CAR construct composed of the extracellular domain, the hinge and transmembrane domain and the intracellular signaling region, or be a component of the full CAR construct including an extracellular targeting moiety, a hinge region, a transmembrane domain, an intracellular signaling domain, one or more co-stimulatory domain, and other additional elements that improve CAR architecture and functionality including but not limited to a leader sequence, a homing element and a safety switch, or the combination of such components (para 204). Such broad limitations cannot be an identifying characteristic for the claimed diverse genus of CA2 variants comprising the recited mutations set forth in the claim, since by Applicant’s definition of variant or functional equivalent thereof all members of the claimed genus will have that characteristic.
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.
Claims 37 and 43-44 are 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 37 recites a stimulus response element (SRE) comprising human carbonic anhydrase 2 (CA2), wherein the CA2 comprises (i) a L156H mutation as set forth in SEQ ID NO: 210600, (ii) a CA2 and L156H mutation as set forth in SEQ ID NO: 210602, or (iii) a L156H, S172C, F178Y, and E186D mutation as set forth in SEQ ID NO:210756. However, SEQ ID NO: 210600 has His155 and Q156; and SEQ ID NO: 210756 has Q156, A172, D178 and S186, so it is contradictory to the limitation of a L156H mutation as set forth in SEQ ID NO: 210600, or (iii) a L156H, S172C, F178Y, and E186D mutation as set forth in SEQ ID NO:210756, rendering claim 37 indefinite if the required mutation is in relation to another unrecited SEQ ID NO. Furthermore, (ii) is unclear what “a CA2 and L156H mutation” is referring to, as SEQ ID NO’s: 210600 & 210602 are approximately the same length (256 & 260, respectively), however the claim could be interpreted to have another undisclosed or unrecited CA2 sequence.
Claims 43-44 are likewise rejected as being dependent on an indefinite claim.
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.
The factual inquiries for establishing a background for determining obviousness under 35 U.S.C. 103 are summarized as follows:
1. Determining the scope and contents of the prior art.
2. Ascertaining the differences between the prior art and the claims at issue.
3. Resolving the level of ordinary skill in the pertinent art.
4. Considering objective evidence present in the application indicating obviousness or nonobviousness.
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 37, 43 and 44 are rejected under 35 U.S.C. 103 as being unpatentable over Suri et al. (CA 3055202 A1, cited in PTO-892 mailed 9/6/2024, hereinafter “Suri”) in view of Krebs et al. (The Journal of Biological Chemistry, 1993, vol. 268, no. 2, pgs. 948-954, cited in PTO-892 mailed 10/21/2025, hereinafter “Krebs”) and Hassan et al. (Bioorganic & Medicinal Chemistry 21 (2013) 1570–1582, cited in PTO-892 mailed 9/6/2024, hereinafter “Hassan”).
For purposes of applying prior art, the Examiner interprets the CA2 comprises the sequences: SEQ ID NO’s: 210600, 210602, or 210756.
Suri teaches biocircuit systems, effector modules and compositions for cancer immunotherapy (abstract). Suri teaches a stimulus response element (SRE) is a destabilizing domain (DD) which is destabilized in the absence of its specific ligand and can be stabilized by binding to its specific ligand (para 8). The SRE can comprise CA2 (SEQ ID NO: 6) which has 99.6% sequence identity to instant SEQ ID NO: 210602 (only difference is the L156H mutation) (para 13, pg. 24, Table 1). Suri teaches the DD may be derived from a parent protein or from a mutant protein having one, two, three, or more amino acid mutations compared to the parent protein (para 13). Suri teaches variants of a particular polynucleotide or polypeptide will have at least 40% sequence identity to that particular reference polynucleotide or polypeptide as determined by sequence alignment programs and parameters (para 316).
Suri teaches one or more mutations may be introduced into the biocircuits of the invention directing the expression of the protein, to maintain its functionality while simultaneously rendering the identified epitope less or non-immunogenic [00127]. Suri teaches destabilizing domains identified using random mutagenesis may be used to identify structural properties of the candidate DDs that may be required for destabilization, which may then be used to further generate libraries of mutations using site directed mutagenesis [00141].
Suri does not teach the structure of CA2, and substitutional mutations of the CA2 domain as recited in claim 37.
However, Krebs teaches a random mutagenesis study that reveals the functional importance of a conserved hydrophobic face in CA2, which includes the amino acid residues 190-210 (abstract). Krebs teaches side chains of amino acids in B-sheet structure are required for the formation of folded, stable protein while those in the turn region determine catalytic efficiency and inhibitor specificity (abstract). Krebs teaches mutations in the B-sheet structure (Asp190-Ser197 and Val207-Ile210) decrease the protein expression of CAII in E. coli, causing the formation of insoluble protein aggregates in many cases, which may suggest an important role for these residues in the folding process (abstract). Krebs teaches the data indicated that many amino acid replacements in nonaromatic residues (such as serine and leucine) also decrease the steady-state expression of soluble CAII in E. coli by 10-fold or more, wherein these substitutions are clustered primarily in the B-sheet structures (pg. 954, col. 1, para 2). Krebs teaches the mutational study revealed W209S (corresponding to W208S of SEQ ID NO: 11717) caused the formation of insoluble inclusion bodies, which indicates a crucial residue for correct folding (pg. 952, Fig. 3a, pg. 954, col. 1, para 2). Krebs teaches mutations at Leu198 (corresponding to L197 of SEQ ID NO: 11717) enhance binding 4-8-fold to dansylamide, confirming the suggestion from modeling studies that the branched side chain of Leu198 forms unfavorable steric interactions with ortho-substituted benzene sulfonamides (pg. 953, col. 2, para 5). Krebs also teaches the mutation L198P (corresponding to L197P of SEQ ID NO: 11717) significantly decreased both esterase and hydrase activity, which would result in a less immunogenic peptide (pg. 950, col. 2, para 3). Krebs teaches conserved elements in the B-sheet structure of the hydrophobic region are maintained throughout evolution primarily to ensure efficient expression of native CAII (pg. 954, col. 1, para 2).
Hassan teaches structure, function, and applications of CA isozymes (title). Hassan teaches 16 different isoforms of CA, but all CA isozymes possess conserved tertiary structure fold with β-strands in their catalytic domains (abstract). Hassan teaches three dimensional structural analysis revealed a high degree of structural similarity, corresponding with an active of CA with three conserved His-residues in a tetrahedral manner (pg. 1570, col. 2, para 3). Hassan teaches CA ranges from 260 to 459 amino acid residues with conserved active sites at His64 and Tyr127 (Proton acceptor), wherein the His64 is conserved in CAI, CAII, CAIV, CAVI, CAVII, and CAXII (pg. 1572, sec. 2.1, para 1). Hassan teaches CAII represents most of the CAs, a well-studied isoform, showing greater sequence and structural similarity with all CAs (pg. 1573, sec. 2.2, para 1). On the basis of hydrophobic and hydrophilic nature, the active site cavity is characteristically divided into two halves, the hydrophobic part contains Ala121 and 135, Val 207, Phe91, Leu131, 138, 146, 109, and Pro201, 202 while the hydrophilic part of the cavity consists of His64, 67, 200, Asn69, Gln92, Thr199, Tyr7 and Val62 (pg. 1573, sec. 2.2, para 1). As disclosed by Hassan, L156 is located in a Beta sheet (the hydrophobic part) (Fig. 1).
Therefore, it would have been prima facie obvious to one of ordinary skill in the art before the effective filing date to modify the SRE composition comprising a mutated destabilizing domain derived from CA2 (SEQ ID NO: 6, with 99.6% sequence identity to instant SEQ ID NO: 210602) that may comprise one, two, three, or more mutations of the parent CA2 as taught by Suri, and substitute particular amino acids to determine destabilizing effects as taught by Krebs, such as any mutation in a B-sheet structural component of CA2 as taught by Hassan with a reasonable expectation of success. One of ordinary skill in the art would have been motivated to design and perform a mutagenesis study to determine specific amino acid mutations (such as replacing nonaromatic residues, i.e. L156H, that may decrease the steady state expression of CA2) and their destabilizing effects, as well as specific small molecule ligands (such as acetazolamide) binding that would stabilize the mutated CA2 domain, based on the studies disclosed by the prior art.
Regarding claims 43 and 44, Suri teaches the CA2’s (DD) corresponding ligands are celecoxib and acetazolamide (pg. 24, Table 1). Suri teaches the presence, absence or an amount of a small molecule ligand that binds to or interacts with the DD, can, upon such binding or interaction modulate the stability of the payload(s) and consequently the function of the payload (para 131).
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.
(maintained/modified rejection) Claims 37, 43 and 44 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1, 3, 7-9, 15, 17, 19-23 of copending Application No. 17/596277 (hereinafter ‘277) in view of Suri.
Regarding instant claim 37, claims 1, 3, 7-9, 11, 15, 17 of ‘277 recite a polypeptide comprising a SRE, wherein the SRE comprises a drug responsive domain comprising human carbonic anhydrase 2 (CA2, SEQ ID NO. 5810, which has 99.6% identity to instant SEQ ID NO: 210602) and further comprises one or more mutations in said CA2, such as L156H. Claims 19 and 20 of ‘277 recite the DRD region of the human CA2 is the full-length CA2 with aa 1-260 or the region of CA2 with aa 2-260. Claim 37 does not recite the instant invention is operably linked to a payload comprising a membrane associated interleukin 12 (IL12) as recited in claim 1 of ‘277.
However, Suri teaches a payload, IL12 attached to a destabilizing domains (DD) that can comprise CA2 (para 245, 13).
Therefore, it would have been prima facie obvious to utilize the SRE-payload composition taught by Suri, and further modify the DD/DRD comprising CA2 with the specific mutations recited in ‘277 with a reasonable expectation of success. One of ordinary skill in the art would have been motivated to attach IL12 to the CA2, as this fusion polypeptide may be directly used as an immunotherapeutic agent as taught by Suri (para 248).
Regarding instant claims 43 and 44, claims 21-23 of ‘277 recite the SRE is responsive to one or more stimuli, wherein the stimuli is a small molecule such as acetazolamide, inter alia, which anticipates the instant claims.
Thus, instant claim 37 and 43-44 are obvious over claims 1, 3, 7-9, 11, 15, 17, 19-23 of ‘277 in view of Suri.
This is a provisional nonstatutory double patenting rejection.
(maintained/modified rejection) Claims 37, 43 and 44 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1, 3, 9, 11, 20-21 of copending Application No. 17/596281 (hereinafter ‘281) in view of Suri.
Regarding instant claims 37-42, claims 1, 3, 9, 11, of ‘281 recite a polypeptide comprising a SRE, wherein the SRE comprises a drug responsive domain comprising human carbonic anhydrase 2 (CA2, SEQ ID NO. 5810, which has 99.6% identity to instant SEQ ID NO: 210602) and further comprises one or more mutations in said CA2, such as L156H recited in claim 1 of ‘281. Claims 20 and 21 of ‘281 recite the DRD region of the human CA2 is the full-length CA2 with aa 1-260 or the region of CA2 with aa 2-260. Claim 37 does not recite the instant invention is operably linked to a payload comprising CD40L as recited in claim 1 of ‘281.
However, Suri teaches a payload, CD40L attached to a destabilizing domains (DD) that can comprise CA2 (para 260, 13).
Therefore, it would have been prima facie obvious to utilize the SRE-payload composition taught by Suri, and further modify the DD/DRD comprising CA2 with the specific mutations recited in ‘281 with a reasonable expectation of success. One of ordinary skill in the art would have been motivated to attach CD40L to the CA2, as CD40L is a part of the TNFα superfamily that can cause cytolysis of tumor cells (para 260).
Regarding instant claims 43 and 44, claim 1 of ‘281 recite the SRE is responsive to acetazolamide or celecoxib, which anticipates the instant claims.
Thus, instant claim 37 and 43-44 are obvious over claims 1, 3, 9, 11, 20-21 of ‘281 in view of Suri.
This is a provisional nonstatutory double patenting rejection.
Response to Arguments
Applicant's arguments filed January 20, 2026 have been fully considered but they are not persuasive.
Regarding Remarks directed to the 103 rejection, Applicant argues the cited references fail to disclose or suggest each and every element of the claim and therefore the claimed invention is not obvious over the prior art. Applicant argues the cited references fail to provide one of ordinary skill in the art with a reasonable expectation of success, since Suri and Krebs fail to disclose the recited mutations, and one of skill could not have known the CA2 mutation in claim 37 would serve useful as a destabilizing domain. Applicant points to Examples 4 & 6-10 demonstrating CA2’s comprising one or more of the claimed mutations reduce basal payload abundance in the absence of ligan and confer ligan-dependent stabilization of the payload.
In response to applicant's arguments against the references individually, one cannot show nonobviousness by attacking references individually where the rejections are based on combinations of references. See In re Keller, 642 F.2d 413, 208 USPQ 871 (CCPA 1981); In re Merck & Co., 800 F.2d 1091, 231 USPQ 375 (Fed. Cir. 1986). Suri teaches destabilizing domains and techniques used to determine particular mutations for destabilizing, such as random mutagenesis studies, and discloses the CA2 parent sequence that can have one or more mutations to confer destabilization. Krebs teaches random mutagenesis studies that reveals the functional importance of a conserved hydrophobic face in CA2, as well as side chains of amino acids in B-sheet structure are required for the formation of folded, stable protein while those in the turn region determine catalytic efficiency and inhibitor specificity. Krebs also teaches mutations in the B-sheet structure (Asp190-Ser197 and Val207-Ile210) decrease the protein expression of CAII in E. coli, causing the formation of insoluble protein aggregates in many cases, as well as many amino acid replacements in nonaromatic residues (such as serine and leucine) decrease the steady-state expression of soluble CAII in E. coli by 10-fold or more, wherein these substitutions are clustered primarily in the B-sheet structures (where L156H is located). Furthermore Hassan teaches three dimensional structural analysis revealing a high degree of structural similarity, corresponding with an active CA, and on the basis of hydrophobic and hydrophilic nature, the active site cavity is characteristically divided into two halves, the hydrophobic part contains Ala121 and 135, Val 207, Phe91, Leu131, 138, 146, 109, and Pro201, 202 while the hydrophilic part of the cavity consists of His64, 67, 200, Asn69, Gln92, Thr199, Tyr7 and Val62, which Hassan discloses L156 is located in a Beta sheet (the hydrophobic part) (Fig. 1). Thus, one of ordinary skill in the art would have motivation to mutate one or more substitutions in a mutagenesis study based on the well-known structural components of CA2 to determine destabilizing mutations that would confer desirable properties (payload, less immunogenic), the person skilled in the art knows that changes in the amino acid sequence result in changes in the structure of the protein and thus affect its function. Furthermore the specification does not describe any objective Examples, etc. proving that even any sequences containing a lot of mutations including L156H, relative to the amino acid sequence of SEQ ID NO. 11717, and having low sequence identities (such as those having identities lower than 90's) to the amino acid sequence of SEQ ID NO. 11717 still can function as the stimulus response element (SRE, destabilizing domain (DD)).
Regarding response directed to the provisional non-statutory double patenting rejections, Applicant argues the priority date of co-pending U.S. Application Nos. 17/596,277 and 17/596,281 is June 12, 2019, which is later than the patent term filing date of the present application, and should be withdrawn if it is the only remaining rejection to permit the application to issue as a patent.
The Examiner will follow the MPEP § 1490(VI)(D)(2)(a) guidelines when this becomes the case, thus the provisional non-statutory double patenting rejections are maintained.
Conclusion
Applicant's amendment necessitated the new grounds 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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/LOUISE W HUMPHREY/Supervisory Patent Examiner, Art Unit 1657
/JESSICA EDWARDS/
Examiner, Art Unit 1657