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 .
Continued Examination Under 37 CFR 1.114
A request for continued examination under 37 CFR 1.114, including the fee set forth in 37 CFR 1.17(e), was filed in this application after final rejection. Since this application is eligible for continued examination under 37 CFR 1.114, and the fee set forth in 37 CFR 1.17(e) has been timely paid, the finality of the previous Office action has been withdrawn pursuant to 37 CFR 1.114. Applicant's submission filed on June 8, 2026 has been entered.
DETAILED ACTION
This application is a US national phase of PCT/US2020/021596, filed March 6, 2020. Applicant’s amendment filed June 8, 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 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. This is a new matter rejection.
Claim 37 as amended recites “wherein the CA2 comprises (i) SEQ ID NO: 210600 comprising a L156H mutation and an M1 deletion , (ii) SEQ ID NO: 210602 comprising L156H mutation, or (iii) SEQ ID NO: 210756 comprising a L156H, S172C, F178Y, and E186D mutation,” which is departure from the claims as originally filed and the specification does not describe a CA2 comprising “(i) SEQ ID NO: 210600 comprising a L156H mutation and an M1 deletion , (ii) SEQ ID NO: 210602 comprising L156H mutation, or (iii) SEQ ID NO: 210756 comprising a L156H, S172C, F178Y, and E186D mutation”. Therefore, this claim limitation is considered new matter. The claimed CA2 as described in the specification for SEQ ID NO: 210600 is described as having amino acid 2-260 of WT, L156H; for SEQ ID NO: 210602 is described as having L156H; and for SEQ ID NO: 210756 is described as having aa 2-260 of WT, L156H, S172C, F178Y, E186D, in Tables 1 & 2. The position of the mutated amino acids listed in Tables 1-2 is relative to the full length CA2 of SEQ ID NO. 11717. As used herein the term "CA2 WT', refers to the human wildtype CA2 protein sequence, which is defined as SEQ ID NO. 11717, with the GenBank Access NO. P00918. Thus, the specification [0013]-[0019] and [0023]-[0027] disclose those mutations relative to SEQ ID NO:11717, not comprised within SEQ ID NO: 210600, 210602 or 210756; thus, the recited SEQ ID NO’s comprising the recited mutations are not supported by the specification, thus constitutes new matter. Nowhere in the specification is it described as the recited SEQ ID NO’s comprising the recited mutations. If Applicant believes that such support is present in the specification and claimed priority documents, Applicant should point, with particularity, to where such support is to be found.
The inventions of claims 43-44 require the use of the inventions of claim 37, and therefore are likewise rejected under 35 U.S.C. 112, first paragraph, as failing to comply with the written description requirement.
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) SEQ ID NO: 210600 comprising a L156H mutation and an M1 deletion, (ii) SEQ ID NO: 210602 comprising a L156H mutation, or (iii) SEQ ID NO: 210756 comprising a L156H, S172C, F178Y, and E186D mutation. It is unclear whether the required mutation is in relation to another unrecited SEQ ID NO, or the SEQ ID NO:210600 has a substitutional mutation from Leu to His at position 156, i.e. L156H, and a M1 deletion at unknown positions as compared to a wild type sequence of unrecited SEQ ID NP. According to the Sequence Listing Version 2.1, SEQ ID NO: 210600 has His at amino acid position 155 and Gln (not Leu) at position 156; SEQ ID NO: 210602 has His at amino acid position 156; and SEQ ID NO: 210756 has His at amino acid position 155, Ala at position 172, Tyr at position 177, Asp at position 178, and Ser at position 186. One of ordinary skill could not interpret the recited substitution as already comprised within the required SEQ ID NO: because the substituted-to amino acid does not match that at the recited position. The specification does specify that the SEQ ID NO: 210600 has the L156H substitution relative to aa 2-260 of wild type CA2 sequence according to SEQ ID NO: 11717. Thus, the limitation of (i), (ii) or (iii) creates ambiguity as to the metes and bounds of the claimed invention.
Claims 43-44 are 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, hereinafter “Suri”) in view of Krebs et al. (The Journal of Biological Chemistry, 1993, vol. 268, no. 2, pgs. 948-954, hereinafter “Krebs”) and Hassan et al. (Bioorganic & Medicinal Chemistry 21 (2013) 1570–1582, hereinafter “Hassan”).
Claim 37 is interpreted as to require the CA2 comprises the sequences: SEQ ID NO’s: 210600, 210602, or 210756.
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 [0008]. The SRE can comprise CA2 (SEQ ID NO: 6, Uniprot ID: P00918) ([0013], pg. 24, Table 1), which is 99.6% identitical to instant SEQ ID NO: 210602 (only difference is L156H) and is 100% identical to instant SEQ ID NO: 11717 (disclosed in instant specification as the CA2 WT, Uniprot P00918).
Sequence comparison of SEQ ID NO: 210602 and Suri’s SEQ ID NO: 6 (Uniprot ID: P00918)
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Sequence comparison of SEQ ID NO: 11717 and Suri’s SEQ ID NO: 6 (Uniprot ID: P00918)
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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 [0013]. 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 [0316].
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, 99.6% identical 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, and any mutation in a B-sheet structural component of CA2 as taught by Hassan. One of ordinary skill in the art would have been motivated to design and perform a mutagenesis study with a reasonable expectation of success 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 [0131].
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 37, 43, and 44 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1, 5-6, and 9-13 of U.S. Patent No. 12,630,599B2 (hereinafter ‘599). Although the claims at issue are not identical, they are not patentably distinct from each other because the instant claims are anticipated by the patent claims.
Claims 1, 5-6, and 9-13 of ‘599 recite a polypeptide comprising a SRE, wherein the SRE comprises a drug responsive domain comprising human carbonic anhydrase 2 corresponding to amino acids 2-260 of SEQ ID NO. 5810, and comprises a L156H mutation in SEQ ID NO: 5810, which is 100% identical to instant SEQ ID NO’s: 210600 & 210602 (See sequence comparison below); or comprises four mutations relative to SEQ ID NO. 5810 corresponding to: (a) L156H, S172C, F178Y, and E186D, which would be 100% identical to instant SEQ ID NO: 210756 (See sequence comparison below), which anticipates the instant claims.
Sequence comparison of SEQ ID NO: 5810 & instant SEQ ID NO’s: 210600 & 210602
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Sequence comparison of SEQ ID NO: 5810 & instant SEQ ID NO’s: 210600 & 210602
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Regarding instant claims 43 and 44, claims 11-13 of ‘599 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 claims 37 and 43-44 are anticipated by claims 1, 5-6, and 9-13 of ‘599.
Response to Arguments
Applicant’s arguments, see pages 2-3, filed June 8, 2026, with respect to claims 37 and 43-44 have been fully considered and are persuasive. The 35 USC § 112(a) rejection of claims 37 and 43-44 has been withdrawn. However, upon further consideration, a new ground(s) of rejection under 35 USC § 112(a) is made in view of the newly amended limitations recited in claim 37 that constitutes new matter.
Applicant's arguments filed June 8, 2026 have been fully considered but they are not persuasive.
Regarding Remarks directed to the 35 USC § 103 rejection of claims 37 and 43-44, Applicant argues when examining the Suri and Krebs in combination, they fail to provide one of skill with sufficient guidance to arrive at the claimed SRE with a reasonable expectation of success. Applicant argues Krebs and Hasssan do not remedy the deficiencies of Suri for at least three reasons. First, a person having ordinary skill in the art would not combine the disclosures of Krebs and Hassan. None of the mutations in claim 37 are within the range of amino acids 190-210 described in Krebs. Based on the guidance provided by the combined references, one of skill could not have known the CA2 mutations recited in claim 37 would serve useful as a destabilizing domain. Instead, based on the cited references, in combination, one of ordinary skill in the art would have selected either wild type CA2 or CA2 comprising one of the mutations in Krebs, which are not claimed.
Applicant argues that combining Krebs and Hassan to reach the claimed SRE would require excessive experimentation. Nothing in Krebs nor Hassan provides any guidance in reaching the specific mutations claimed. The Examiner argues that a person having ordinary skill in the art would make mutations at amino acid residues identified as part of a hydrophobic beta sheet in Hassan, such as L156H. Final Office Action at 10. However, a person having ordinary skill in the art would first need to select position 156 out of the myriad CA2 amino acid residues identified as part of a hydrophobic beta sheet, and second, choose to replace the native amino acid leucine with histidine over the other numerous amino acids that could be substituted. Neither Krebs nor Hassan provide any guidance for which residue to select for mutation, nor for which amino acid to replace the native residue with. The path to the claimed SRE in view of Suri, Krebs, and Hassan is not routine optimization, rather reaching the claimed SRE requires so much experimentation that it amounts to a research project. The references cannot render the claims obvious for this reason. And third, Krebs and Hassan are cited as disclosing that hydrophobic beta sheet regions are implicated in CA2 expression. Nothing in Krebs nor Hassan provides any guidance related to utilizing CA2 as a destabilizing domain. As described throughout the specification including the Examples 4 and 6-10, SREs comprising CA2 with one or more of the mutations recited in claim produce a more effective destabilizing domain for regulating payload expression than wild type CA2. Particularly, SREs comprising CA2 with one or more of the claimed mutations reduce basal payload abundance in the absence of ligand and confer ligand-dependent stabilization of the payload in the presence of the ligand. See Examples 4 and 6-10 of the present application. Nothing in Suri, Krebs, nor Hassan provide any guidance related to utilizing CA2 as a destabilizing domain or making the claimed mutations which produce a more effective CA2 destabilizing domain. Applicant argues structural similarity does not allow a person having ordinary skill in the art to have a reasonable expectation of success regarding ligand binding and ligand-dependent regulation because CA isozymes respond differently to ligands. Applicant argues that importing the CA2 mutations into a CA7 construct did not provide meaningful ligand-dependent regulation, and discloses data showing that CA7 constructs with mutations equivalent to L183S, Y193I, L156H, and D72F, V241F, and P49L mutations did not display a significant max fold increase in payload expression upon ligand administration as compared to the wildtype CA7 construct. Applicant argues the cited references fail to disclose or suggest each and every element of the claims, and thus the claims are not obvious over the prior art.
In response to applicant’s argument that there is no teaching, suggestion, or motivation to combine the references, the examiner recognizes that obviousness may be established by combining or modifying the teachings of the prior art to produce the claimed invention where there is some teaching, suggestion, or motivation to do so found either in the references themselves or in the knowledge generally available to one of ordinary skill in the art. See In re Fine, 837 F.2d 1071, 5 USPQ2d 1596 (Fed. Cir. 1988), In re Jones, 958 F.2d 347, 21 USPQ2d 1941 (Fed. Cir. 1992), and KSR International Co. v. Teleflex, Inc., 550 U.S. 398, 82 USPQ2d 1385 (2007). In this case, Suri teaches the SRE comprising a destabilizing domain that is destabilized absence of its specific ligand, and discloses the SRE can comprise CA2 (albeit wild-type). Suri also teaches the DD can be derived from the parent protein comprising one or more mutations. Suri also teaches the one or more mutations may be introduced to maintain its functionality while simultaneously rendering it less or non-immunogenic. Suri points to the well-understood and routine practice in the art to conduct random mutagenesis studies to identify structural properties of candidate DDs. Suri does not disclose the structural and functional components of CA2. However, Krebs reveals the functional importance of conserved regions in the CA2, and disclose the B-sheet structure that infer stability to the protein, and indicate mutations in non-aromatic residues (i.e. leucine) in the B-sheet also decrease expression of CA2. Hassan also teaches structure and function of CA isozymes, and discloses L156 is located in the B-sheet. Therefore, with the primary Suri reference teaching the overall claimed invention, except for the specific mutations identified in the claims, and the structural components of CA2 related to functionality in decreasing protein activity and stabilizing amino acid conserved residues, one of ordinary skill in the art would have been motivated to try a point mutation mutagenesis study to determine destabilizing substitutions in relation to ligand specificity. 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)).
Applicant’s arguments with respect to claim(s) 37 and 43-44 rejected under provisional non-statutory double patenting over copending application 17/596281, have been considered but are moot because the copending application has been abandoned.
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 (now U.S. Patent No. 12,630,599B2) 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
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/LOUISE W HUMPHREY/Supervisory Patent Examiner, Art Unit 1657
/JESSICA EDWARDS/
Examiner, Art Unit 1657
