DETAILED ACTION
Notice of Pre-AIA or AIA Status
The present application, filed on or after March 16, 2013, is being examined under the first inventor to file provisions of the AIA .
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and the fee set forth in 37 CFR 1.17(e) has been timely paid, the finality of the previous Office action has been withdrawn pursuant to 37 CFR 1.114.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 04/23/2026 has been entered.
Receipt is acknowledged of an amendment, 04/23/2026, in which claims 1 and 21 were amended, claims 2, 3, 7, 11, 22, 26, 30, 40, 41, 45, 49, 53 and 55 were previously presented and claim 59 was newly added. Claims 40, 41, 45, 49, 53 and 55 were previously withdrawn due to a restriction requirement set forth in the office action mailed on 07/01/2025.
Claims 1-3, 7, 11, 21, 22, 26, 30 and 59 are currently under examination.
Claim Rejections - 35 USC § 103
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.
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 text of those sections of Title 35, U.S. Code not included in this action can be found in a prior Office action.
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.
Claims 1-3, 7, 11, 21, 22, 26, 30 and 59 are rejected under 35 U.S.C. 103 as being
unpatentable by Park et al (J Med Genet. 1998; 35: 813-820; cited in a prior action) in view of Buerki et al (WO 2014/028884 A2), Cali et al (European Journal of Medical Genetics 60, 93-99; 2017) and Buck et al (BioTechniques, 27:3, 528-536; 1999; cited in a prior action) as evidenced by GenBank Accession No. NM_000267.3 (Published September 10th, 2019; cited in a prior action). This is a rejection made in the previous office action mailed on 01/23/2026 and amended to address the amendments Applicant filed on 04/23/2026.
Park teaches a protein truncation assay to screen for mutations in 15 NFl patients and
obtained positive results in 11 of them (Page 813, Abstract). Park teaches mutations identified in
cDNA was confirmed by direct sequencing of PCR products generated using genomic DNA and
exon specific primers (Page 815, Column 1). Park teaches investigating the genomic basis of
exon skipping, specific exons were amplified from genomic DNA and used for direct sequencing
(Page 816, Column 2). Park teaches the sequences listed as "F" in table 2 are all 100% identical
to exons within NM_ 000267.3 (See Appendix A). Park teaches primers listed as "R" or reverse in table 2 are all 100% identical to exons within NM_000267.3 (See Appendix B). Park teaches
primers capable of hybridizing to a continuous stretch of at least 20 nucleotides within exons 12
and 20 of the NFl sequence (Page 815, Table 2).
Park does not teach wherein the antisense oligonucleotide is selected from the group consisting of: an oligonucleotide comprising a non-natural backbone; a phosphorodiamidate morpholino oligonucleotide; an oligonucleotide containing at least one residue that is modified to increase nuclease resistance, to increase the affinity of the oligonucleotide for the target nucleotide sequence, or both; or a combination of two or more of the foregoing.
Buerki teaches the use of modified probes and/or primers for the detection and targeting a plurality of target sequences including pre-mRNA [0168, 0193-0194 and 0215]. Buerki teaches modified or substituted backbone of the probes or primers provide desirable properties such as enhanced affinity for a target gene and increased stability [0209].
It would have been obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to modify the teachings of Park to include the modified backbone of primers as taught by Buerki because Park teaches it is within the ordinary skill in the art to use primers capable of hybridizing to a continuous stretch of at least 20 nucleotides within exons of the NFl sequence and Buerki teaches the use of modified probes and/or primers for the detection and targeting a plurality of target sequences.
One would have been motivated to make such a modification in order to receive the expected benefit of desirable properties such as enhanced affinity for a target gene and increased stability by modified probes/primers as taught by Buerki.
Park does not teach the specific sequences listed in claims 3, 7, 11, 15, 22, 26, 30 and 34
such as SEQ ID NOs: 1-24, 49, 57, 63, 64 and/or 65.
Cali teaches that the mutations occur in each of the exons such as exons 17, 4 7, 5 2, and
13 (Page 96-97, Table 1). Cali teaches that comprehensive analysis of the entire NFl gene using
NGS was known, possible, and relevant owing to substantial genetic heterogeneity in NFl
patients (Page 95, Column 2). Cali teaches making primers to the entire NFl coding sequence
(Page 94, Column 1 to Column 2). Cali teaches that NFl is one of the largest human genes,
composed of 57 exons such as GenBank Accession number as NM_00267.3 (Page 93, Column
2).
While teaching primers covering the entire NFl transcript, Cali does not teach the primer
sequences.
Buck teaches the idealized primer characteristics for primer design such as the
sequencing primers should be 18-24 nt in length (Page 532, Column 2). Buck teaches This study
confirms earlier observations that there is a broad tolerance in these and other characteristics of
sequencing primers (Page 535, Column 2). Buck et al expressly provide evidence of the
equivalence of primers. Specifically, Buck et al invited primer submissions from a number of
labs (39) (e.g., page 532, column 3), with 69 different primers being submitted (e.g., page 530,
column 1). Buck et al also tested 95 primers spaced at 3 nucleotide intervals along the entire
sequence at issue, thereby testing more than 1/3 of all possible 18 mer primers on the 300 base-pair sequence (e.g., page 530, column 1). When Buck et al tested each of the primers selected by the methods of the different labs, Buck found that every single primer worked (e.g., page 533,
column 1). Only one primer ever failed, No. 8, and that primer functioned when repeated.
Further, every single control primer functioned as well (e.g., page 533, column 1). Buck et al expressly states "The results of the empirical sequencing analysis were surprising in that nearly all of the primers yielded data of extremely high quality (page 535, column 2)." Therefore, Buck et al provides direct evidence that all primers would be expected to function, and in particular, all primers selected according to the ordinary criteria, however different, used by 39 different laboratories. It is particularly striking that all 95 control primers functioned, which represent 1/3 of all possible primers in the target region. This clearly shows that every primer would have an expectation of success.
It would have been obvious before the effective filing date of the claimed invention to
have designed primers covering the complete coding sequence of the NFl gene taught by Cali
(i.e., GenBank NM_00267.3), using the primer design principles of Buck, for use in analysis of
NFl genotype and use of primers in NFl patients as taught by Park.
Before the effective filing date, it was known that NFl patients exhibit genetic heterogeneity (see Cali), and that as taught by Park, identification of patients with NFl mutations
and the use of primers for exon splicing for the correction of those mutations. Cali provides a
method for comprehensively analyzing genotype of NFl patients, but does not teach the primer
sequences used in the method. The sequence of NFl was known and is 12381 nucleotides in
length. Buck teaches that primers are 25 nts in length. Accordingly, there are a finite number of
potential primers 25-nts in length which are 100% complementary to the NFl gene taught by
Cali (i.e., GenBank NM_00267.3). Among these potential solutions are SEQ ID NOs: 1-18, 51,
53, 57 and 63-65, which are themselves 100% complementary to the NFl gene taught by Cali (i.e., GenBank NM_00267.3) (See appendices 1-XXIV). The skilled artisan could have pursued
the finite, predictable solutions with a reasonable expectation of success because primer design
principles were known as evidenced by at least Buck and Cali, and because Buck teaches that
every primer works.
The skilled artisan would have been motivated to design primers for use in
the method of Cali because Park teaches identification of NFl mutations in patients and the
successful use of primers for exon splicing for the correction of the mutations within the patients.
Accordingly, claims 1-3, 7, 11 and 59 are obvious.
Regarding claims 21, 22, 26 and 30, Cali teaches a composition comprising the
primers (see section 2.2 NGS sequencing).
Claims 1, 2 and 21 are rejected under 35 U.S.C. 103 as being unpatentable over Pros et al (Human Mutation, Vol 30 No 3, Pages 454-462; March 2009; cited in a prior action); in view of Xu et al (International Journal of Molecular Medicine, Vol 34 No 1, Pages 53-60; July 2014; cited in a prior action) as evidenced by GenBank Accession No. NM_000267.3 (Published September 10th, 2019; cited in a prior action). This is a rejection made in the previous office action mailed on 01/23/2026 and amended to address the amendments Applicant filed on 04/23/2026.
Regarding claim 1, Pros teaches the use of antisense morpholino oligomers to restore
normal splicing in primary fibroblast and lymphocyte cell lines derived from six NFl patients
bearing three deep intronic mutations in the NFl gene (Abstract). Pros teaches a method
comprising administering to a subject a therapeutically effective amount of a composition
comprising an antisense oligonucleotide that specifically hybridizes to a continuous stretch of at
least 20 nucleotides within NFl pre-mRNA from at least one exon (Abstract and Page 456,
column 1). Pros teaches along with antisense oligonucleotides, antisense phosphorodiamidate morpholino oligomers (AMOs) are analogs of oligonucleotides with a six-membered morpholino ring replacing ribose or deoxyribose (Page 455, Column 1). Pros AMO is a phosphorodiamidate morpholino oligonucleotide, which comprises a non-natural backbone, and is modified to increase nuclease resistance and affinity for its target ("Among AONs, antisense phosphorodiamidate morpholino oligomers (AMOs) are analogs of oligonucleotides with a six-membered morpholino ring replacing ribose or deoxyribose. AMOs have high binding specificity, stability, and resistance to nucleases, and their activity is highly durable," pg. 455, left col.). Pros teaches AMOs have high binding specificity, stability, and resistance to nucleases, and their activity is highly durable (Page 455, Column 1). Pros teaches treatment of the six NFl patients harboring three different deep intronic NFl mutation cell lines with specifically designed AMOs showed that this antisense approach corrected aberrant splicing and significantly increased the levels of wild-type NFl transcripts (Page 461, Column 1). Pros teaches specific AMOs to block the effect of three independent NFl deep intronic mutations that causes the inclusion of cryptic exons in NFl patients (Page 455, Column 1). Pros teaches that the designed AMOs target the newly created 5' splice site to prevent the incorporation of cryptic exons (Page 457, Column 2). Pros teaches AMO treatment decreased the active Ras-GTP levels in the same cells, which is consistent with the hypothetical restoration of neurofibromin GTPase activity to wild-type levels (Page 461, Column 1). Pros teaches the same or similar therapeutic strategies could possibly be applied to other types of NFl mutations as well as to other genetic disorders (Page 462, Column 1).
Pros does not teach antisense oligonucleotides that specifically hybridize to the specific exons such as exons 17, 52, 47, 9, 12, 13, 20, 21, 25, 36 or 41 of NFl.
Xu teaches exon skipping in NFl exons 21 and 25 identified from clinically diagnosed individuals having NFl (Page 56, Table 2, Splicing mutations at the consensus splice sites).
While Pros provides motivation to provide AMOs that specifically hybridize to a target exon in NFl pre-mRNA to remedy aberrant splicing caused by mutation, and Xu teaches a mutation in exons 21 and 25 that causes aberrant splicing of NFl pre-mRNA, neither Pros or Xu teach the NFl pre-mRNA sequence such that the skilled artisan could prepare AMOs to exons 21 and 25.
However, GenBank Accession No. NM_000267.3 teaches the sequence of NFl premRNA, including exons 21 and 25, which corresponds to nucleotides 2793-3233 and nucleotides 4358-4493, respectively.
It would have been obvious to one of ordinary skill in the art to modify the isolated antisense oligonucleotide that specifically hybridizes to NFl pre-mRNA, as taught by Pros, to include or instead target exons 21 or 25 as taught by Xu. Pros teaches that one of ordinary skill in the art to use therapeutic antisense oligonucleotides targeting NFl splice sites to restore normal intron-exon splicing while Xu teaches NFl mutations identified from clinically diagnosed individuals having NFl related disease, including those producing IVS in exons 21 and 25 which form inactive splice sites. This combination would allow the method and antisense oligonucleotide therapeutics of Pros to target other clinically relevant NFl mutations on exons 21 and 25 taught by Xu.
One would have been motivated to make such a modification in order to receive the expected benefit of the method of using AMO therapeutics to target mutations of the NFl gene as taught by Pros to target other clinically relevant NFl mutations, such as on exons 21 and 25 as taught by Xu.
Regarding claim 2, Pros AMO is 25-nts in length (Page 456, Column 1, Morpholino
Oligomer Design and Treatment).
Regarding claim 21, Pros teaches a composition comprising the AMO (Page 456, Column 1 bridging to Column 2). Pros teaches the use of antisense morpholino oligomers to restore normal splicing in primary fibroblast and lymphocyte cell lines derived from six NFl patients bearing three deep intronic mutations in the NFl gene (Abstract). Pros teaches a method
comprising administering to a subject a therapeutically effective amount of a composition
comprising an antisense oligonucleotide that specifically hybridizes to a continuous stretch of at
least 20 nucleotides within NFl pre-mRNA from at least one exon (Abstract and Page 456,
column 1). Pros teaches along with antisense oligonucleotides, antisense phosphorodiamidate morpholino oligomers (AMOs) are analogs of oligonucleotides with a six-membered morpholino ring replacing ribose or deoxyribose (Page 455, Column 1). Pros AMO is a phosphorodiamidate morpholino oligonucleotide, which comprises a non-natural backbone, and is modified to increase nuclease resistance and affinity for its target ("Among AONs, antisense phosphorodiamidate morpholino oligomers (AMOs) are analogs of oligonucleotides with a six-membered morpholino ring replacing ribose or deoxyribose.AMOs have high binding specificity, stability, and resistanceto nucleases, and their activity is highly durable," pg. 455, left col.). Pros teaches AMOs have high binding specificity, stability, and resistance to nucleases, and their activity is highly durable (Page 455, Column 1). Pros teaches treatment of the six NFl patients harboring three different deep intronic NFl mutation cell lines with specifically designed AMOs showed that this antisense approach corrected aberrant splicing and significantly increased the levels of wild-type NFl transcripts (Page 461, Column 1). Pros teaches specific AMOs to block the effect of three independent NFl deep intronic mutations that causes the inclusion of cryptic exons in NFl patients (Page 455, Column 1). Pros teaches that the designed AMOs target the newly created 5' splice site to prevent the incorporation of cryptic exons (Page 457, Column 2). Pros teaches AMO treatment decreased the active Ras-GTP levels in the same cells, which is consistent with the hypothetical restoration of neurofibromin GTPase activity to wild-type levels (Page 461, Column 1). Pros teaches the same or similar therapeutic strategies could possibly be applied to other types of NFl mutations as well as to other genetic disorders (Page 462, Column 1).
Pros does not teach antisense oligonucleotides that specifically hybridize to the specific exons such as exons 17, 52, 47, 9, 12, 13, 20, 21, 25, 36 or 41 of NFl.
Xu teaches exon skipping in NFl exons 21 and 25 identified from clinically diagnosed individuals having NFl (Page 56, Table 2, Splicing mutations at the consensus splice sites).
While Pros provides motivation to provide AMOs that specifically hybridize to a target exon in NFl pre-mRNA to remedy aberrant splicing caused by mutation, and Xu teaches a mutation in exons 21 and 25 that causes aberrant splicing of NFl pre-mRNA, neither Pros or Xu teach the NFl pre-mRNA sequence such that the skilled artisan could prepare AMOs to exons 21 and 25.
However, GenBank Accession No. NM_000267.3 teaches the sequence of NFl premRNA, including exons 21 and 25, which corresponds to nucleotides 2793-3233 and nucleotides 4358-4493, respectively.
It would have been obvious to one of ordinary skill in the art to modify the isolated antisense oligonucleotide that specifically hybridizes to NFl pre-mRNA, as taught by Pros, to include or instead target exons 21 or 25 as taught by Xu. Pros teaches that one of ordinary skill in the art to use therapeutic antisense oligonucleotides targeting NFl splice sites to restore normal intron-exon splicing while Xu teaches NFl mutations identified from clinically diagnosed individuals having NFl related disease, including those producing IVS in exons 21 and 25 which form inactive splice sites. This combination would allow the method and antisense oligonucleotide therapeutics of Pros to target other clinically relevant NFl mutations on exons 21 and 25 taught by Xu.
One would have been motivated to make such a modification in order to receive the expected benefit of the method of using AMO therapeutics to target mutations of the NFl gene as taught by Pros to target other clinically relevant NFl mutations, such as on exons 21 and 25 as taught by Xu.
Response to Arguments - Claim Rejections - 35 USC § 103
The previous rejection of claims 1-3, 7, 11, 21, 22, 26, 30 and 59 under 35 U.S.C. 103 as being unpatentable by Park et al (J Med Genet. 1998; 35: 813-820; cited in a prior action) in view of Buerki et al (WO 2014/028884 A2), Cali et al (European Journal of Medical Genetics 60, 93-99; 2017) and Buck et al (BioTechniques, 27:3, 528-536; 1999; cited in a prior action) as evidenced by GenBank Accession No. NM_000267.3 (Published September 10th, 2019; cited in a prior action) has been maintained in view of Applicant arguments filed 04/23/2026.
Applicant’s arguments have been fully considered but have not been found to be persuasive. Applicant argues Park teaches PCR primers that bind within certain exons to allow the amplification of genomic and cDNA sequences to detect potentially deleterious mutations. Applicant continues to argue that Park does not teach oligonucleotides that bind to pre-mRNA of any kind, much less the pre-mRNA of the listed exons. Applicant further argues that because Park’s purpose is the detection of mutations that reside within the genome by using PCR, Park had no reason to design primers that complement pre-mRNA. Applicant continues to argue that Buerki teaches numerous kinds of probes to detect any of hundreds of targets that are purportedly biomarkers of cancer. Applicant argues that modified nucleic acids can be used and lists over a dozen of classes of modified nucleic acids, including PMOs. Applicant argues that Buerki teaches that the probes can target coding and non-coding DNA, but does not teach that the probes complement pre-mRNA. Applicant further argues that many kinds of modified nucleic acids cannot function as PCR primers because they are not recognized by the enzyme suite that is required for PCR. Applicant argues that Cali is cited to teach that mutations can occur in several exons on NF1 and to indirectly teach that the genomic sequence of NF1 was known at the time and to teach PCR primers that are complementary to nonspecific parts of the NF1 genomic sequence. Applicant continues to argue that Cali does not teach an oligonucleotide that is complementary to any pre-mRNA, much less to a pre-mRNA of the exons listed in the claims. Applicant further argues Buck is cited to teach how to design PCR primers, however, this does not compensate for the deficiencies of Park, Buerki, and Cali; and Buck says nothing about oligonucleotides that complement pre-mRNA. Applicant continues to argue that although Park and Cali recognized that mutations in NF1 can have clinical significance, this would not lead the reader to specifically design oligonucleotides that complement the pre-mRNA that is produced from the claimed exon regions of NF1. In addition, Applicant argues that Park and Cali’s oligonucleotides have diagnostic properties whereas the claimed oligonucleotides have therapeutic properties. Finally, Applicant argues that claim 1 and 21 require that the oligonucleotide causes at least partial exon skipping of said exon when hybridized to the target sequence and further, there is no teaching, either explicit or inherent, in any of the cited references that the oligonucleotides taught therein cause at least partial exon skipping of said exon when hybridized to the target.
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, Applicant’s arguments are specific to only Park and do not include the limitations that are found obvious in view of the other cited references. Specifically, Park teaches
primers capable of hybridizing to a continuous stretch of at least 20 nucleotides within exons 12 and 20 of the NFl sequence (Page 815, Table 2). Park is used in combination with Buerki, Cali and Buck to reach the full limitations of the claims. Buerki teaches the use of modified probes and/or primers for the detection and targeting a plurality of target sequences including pre-mRNA, Cali teaches the specific sequences for exons within the NF1 gene and Buck teaches the design methods for primers to target exons within a gene. Therefore, in combination, the cited references teach the claimed invention as currently outlined in the claims.
Finally, in response to applicant's argument that the claimed composition must be used for the specific purpose of exon skipping, a recitation of the function of the claimed invention must result in a structural difference between the claimed invention and the prior art in order to patentably distinguish the claimed invention from the prior art. If the prior art structure is capable of performing the function, then it meets the claim.
The previous rejection of claims 1, 2 and 21 under 35 U.S.C. 103 as being unpatentable over Pros et al (Human Mutation, Vol 30 No 3, Pages 454-462; March 2009; cited in a prior action); in view of Xu et al (International Journal of Molecular Medicine, Vol 34 No 1, Pages 53-60; July 2014; cited in a prior action) as evidenced by GenBank Accession No. NM_000267.3 (Published September 10th, 2019; cited in a prior action) has been maintained in view of Applicant arguments filed 04/23/2026.
Applicant’s arguments have been fully considered but have not been found to be persuasive. Applicant argues that Pros teaches PMO-ASO to restore normal splicing by hybridizing to NF1 pre-mRNA of at least one exon, however, Pros used PMO-ASO that hybridized to intronic pre-mRNA. Applicant specifically points to Fig. 1 and argues that the PMO-ASO bound to introns between exons 3 and 4, exons 36 and 37 and exons 45 and 46.
Applicant continues to argue that although assuming the Examiner’s argument is correct that one would be motivated to use the method of Pros to use an oligonucleotide complementary to pre-mRNA from the exons to restore normal splicing, that is not the claimed invention. Applicant specifies that the claimed ASO causes exon skipping and it does not restore normal splicing like Xu. Applicant further argues that the goal of Pros is to restore normal splicing and there is no teaching, either explicit or inherent, in any of the cited references that the oligonucleotides taught therein are capable of causing at least partial exon skipping of said exon when hybridized to pre-mRNA.
However, Applicant’s arguments are not persuasive because Park teaches primers capable of hybridizing to a continuous stretch of at least 20 nucleotides within exons 12 and 20 of the NFl sequence for the purpose of exon skipping (Page 815, Table 2 and Page 816, Column 2). Therefore, the composition is known in the art and not found to function in a way that would produce unexpected results
Finally, in response to applicant's argument that the claimed composition must be used for the specific purpose of exon skipping, a recitation of the function of the claimed invention must result in a structural difference between the claimed invention and the prior art in order to patentably distinguish the claimed invention from the prior art. If the prior art structure is capable of performing the function, then it meets the claim.
Applicant continues to argue that the specification teaches unexpected results. Applicant argues that the references cited do not teach every limitation of the claims and in addition, the claimed oligonucleotides produce more than predictable results. Applicant argues that the cited references teach that the oligonucleotides can be used for PCR amplification, probing and the restoration of normal splicing; however, Examples 4-7 of the instant specification claims oligonucleotides that have the property of inducing exon skipping to produce abnormal splice variants. Applicant specifically points to In re Sullivan, 498 F.3d 1345 (Fed. Cir. 2007) which concluded with the federal circuit ruling that unexpected use of a novel composition is evidence of non-obviousness.
However, Applicant’s arguments are not persuasive because Park teaches primers capable of hybridizing to a continuous stretch of at least 20 nucleotides within exons 12
and 20 of the NFl sequence for the purpose of exon skipping (Page 815, Table 2 and Page 816, Column 2). Therefore, the composition is known in the art and not found to function in a way that would produce unexpected results.
Conclusion
No claims are allowed.
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/ALEXANDRA ROSE LIPPOLIS/Examiner, Art Unit 1637
/CELINE X QIAN/Primary Examiner, Art Unit 1637
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