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and the fee set forth in 37 CFR 1.17(e) has been timely paid, the finality of the previous Office action has been withdrawn pursuant to 37 CFR 1.114.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 05/29/2026 has been entered.
Status of the Claims
Claims 26, 30-41, 44, 48-58 are pending in the application. The amendment filed on 05/29/2026 in which claim 26 and 41 were amended is acknowledged. Claims 49-58 were previously withdrawn.
Claims 26, 30-41, 44 and 48 are currently under examination on the merits.
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 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.
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 26, 30-34, 39-41 are rejected under 35 U.S.C. 103 as being unpatentable over Wang, in view of Ugen, and further in view Wang & Walfield (prior art of record).
See claims 26, 30-34, 39-41 as submitted on 05/29/2026.
Regarding claim 26, it is noted that amended claim 26 reads “or a combination of any of said spacers” on line 5. However, as previously explained, this limitations is already taught by the cited prior art of record. Specifically, Wang teaches a construct design or platform in which an Aβ peptide immunogen comprising the N-terminus of the Aβ peptide acts as the B cell epitope and it is covalently linked through spacer residues to a heterologous T helper cell (Th) epitope derived from pathogen proteins that act together to stimulate the generation of highly specific antibodies directed against the N-terminus of the Aβ peptide offering protective immune responses to patients at risk for, or with, Alzheimer's Disease (Abstract).
The construct design or platform taught by Wang incorporates three components into one construct for the benefit of generating a synthetic peptide-based immunotherapeutic and/or vaccine. The three components as taught by Wang are:
a target epitope which acts as a B cell epitope comprising the amino acid sequence of a targeted molecule defined by epitope mapping for functional antigenicity (Abstract; col 5, ¶ 4).
a T helper cell epitope comprising of the amino acid sequence derived from pathogen proteins that act together to stimulate the generation of highly specific antibodies (Abstract; col 12, ¶ 1). Th cell epitopes include Measles Virus Fusion (MVF) protein and HBsAg3 (col 4, ¶ 1). Note that Wang & Walfield refer to the T helper cell epitope as UBITh®. One example of a Th cell epitope taught by Wang is set forth in SEQ ID NO:46 which shared 100% sequence identity to instant SEQ ID NO: 83 (col 62, Table 2) (see alignment of record).
a heterologous spacer comprising a linker chosen from the group: Lys-, Gly-, Lys-Lys-Lys-, (α, ε-N)Lys, or ε-N-Lys-Lys-Lys-Lys (Abstract; 17, ¶ 2), wherein the heterologous spacer covalently links the B cell epitope to the T helper cell epitope (Abstract; col 12, ¶ 1). It is noted that instant SEQ ID NO: 148 (KKKK) shares 100% sequence identify with SEQ ID NO: 32 (KKKK) in Wang’s teachings (col 59, Table 1).
Wang does not explicitly teach the alpha-synuclein protein as the B cell epitope comprising the amino acid sequence of SEQ ID NO: 15.
However, as previously explained, Ugen teaches human α-synuclein (α-Syn) 3 peptides synthesized based upon predicted B cell epitopes within the full length α-Syn protein sequence for the purpose of developing a vaccine against Parkinson’s disease (PD) (Abstract). Ugen further teaches peptide fragments comprising amino acids 111-139 of the α-Syn 3 protein as the target sequences or epitopes (page 923). One such peptide termed “Peptide Fragment C” (MPVDPDNEAYEMPSEEGYQDY) comprises a sequence that shares 100% sequence identity with instant SEQ ID NO: 15 (see alignment of record - Peptide Fragment C with instant SEQ ID NO: 15). Further Ugen teaches an effective humoral immune response upon stimulation with Peptide Fragment B and Peptide Fragment C (page 923-924).
It would have been prima facie obvious to a person of ordinary skill in the art, at the time of filing, to have included the teachings of Ugen on the α-Syn 3 peptides to act as the B cell epitopes in the construct design or platform taught by Wang for the benefit of generating a synthetic peptide-based immunotherapeutic and/or vaccine against PD given that Ugen demonstrated effective antibody response against such α-Syn 3 peptides and Wang & Walfield teach that the construct design or platform taught by Wang, which is also described by Wang & Walfield, can be applied to the development of therapeutic and protective vaccines for multiple conditions including chronic and infectious diseases (Wang & Walfield, Abstract, page 1, 7).
One of ordinary skill in the art would have had a reasonable expectation of success for introducing the α-Syn peptides into the construct comprising a Th cell epitope and a heterologous spacer sequence as taught by Wang given that the methods of vector cloning and peptide expression are known, successfully demonstrated, and commonly used as evidenced by the applied prior art.
Regarding claims 30 and 31, it is noted that no amendments were introduced to claims 30 and 31 in the amendment filed on 05/29/2026. As previously explained, Wang already teaches a ε-N-Lys spacer sequence as well as an ε-N-Lys-Lys-Lys-Lys spacer sequence (Abstract; 17, ¶ 2), SEQ ID NO: 32 (KKKK) in Wang’s teachings (col 59, Table 1) has 100% sequence identity to instant SEQ ID NO: 148 (KKKK).
Regarding claim 32, it is noted that no amendments were introduced to claim 32 in the amendment filed on 05/29/2026. As previously explained, Wang teaches wherein the heterologous spacer covalently links the B cell epitope to the T helper cell epitope (Abstract; col 12, ¶ 1).
Regarding claim 33, it is noted that no amendments were introduced to claim 33 in the amendment filed on 05/29/2026. As previously noted, all of the limitations of claim 33 are already taught by the cited prior art. As previously explained, Wang and Ugen teach all three components of the construct as recited in claim 26: a) the α-Syn as the B cell epitope, b) the Th cell epitope, and c) a spacer which covalently links the B cell epitope to the Th cell epitope. Therefore, the construct of Wang in view of Ugen comprises one or both formulas as recited in claim 33. Further, Wang recites the same formula on col. 17, ¶ 1 ((peptide)-(A)0 -(Th)-X) for a different target peptide. Further, the T helper epitope of SEQ ID NO: 83 is already taught by Wang (see alignment of record). Further, it is noted that Wang also teaches the heterologous spacer of SEQ ID NO: 148 (see above) and Ugen teaches the α-Syn epitope of SEQ ID NO: 15 (see alignment of record). Further, Wang already teaches wherein the heterologous spacer covalently links the B cell epitope to the T helper cell epitope (Abstract; col 12, ¶ 1). Accordingly, the teachings of Wang, Ugen, and Wang & Walfield combined meet the limitations of claim 33.
It would have been prima facie obvious to a person of ordinary skill in the art, at the time of filing, to have included the teachings of Ugen on the α-Syn 3 peptides to act as the B cell epitopes in the construct design or platform taught by Wang for the benefit of generating a synthetic peptide-based immunotherapeutic and/or vaccine against PD given that Ugen demonstrated effective antibody response against such α-Syn 3 peptides and Wang & Walfield teach that the construct design or platform taught by Wang, which is also described by Wang & Walfield, can be applied to the development of therapeutic and protective vaccines for multiple conditions including chronic and infectious diseases (Wang & Walfield, Abstract, page 1, 7).
One of ordinary skill in the art would have had a reasonable expectation of success for introducing the α-Syn peptides into the construct comprising a Th cell epitope and a heterologous spacer sequence as taught by Wang given that the methods of vector cloning and peptide expression are known, successfully demonstrated, and commonly used as evidenced by the applied prior art.
Regarding claim 34, it is noted that no amendments were introduced to claim 34 in the amendment filed on 05/29/2026. As previously explained, as indicated above the α-Syn epitope of SEQ ID NO: 15 was taught by Ugen and all other components of the construct which are formulated as indicated by the formulas of claim 33 are taught by Wang. It is noted that Wang also teaches the heterologous spacer of SEQ ID NO: 148 (see above). Therefore, the limitations of claim 34 are met by the teachings of Wang, Ugen, and Wang & Walfield.
Regarding claim 39, it is noted that no amendments were introduced to claim 39 in the amendment filed on 05/29/2026. As previously explained, Wang further teaches a pharmaceutical composition comprising the construct as recited in claim 26 and further comprising a pharmaceutically acceptable delivery vehicle and/or adjuvant (Abstract; claims 3, 4; col 18, ¶ 5).
Regarding claim 40, it is noted that no amendments were introduced to claim 40 in the amendment filed on 05/29/2026. As previously explained, Wang further teaches a pharmaceutical composition comprising an CpG oligodeoxynucleotide (ODN) to form a stabilized immunostimulatory complex (col 21, ¶ 4).
Regarding claims 41, it is noted that the amendment of claim 41 submitted on 05/29/2026 did not introduced any new limitations to claim 41. As previously explained, Wang teaches a pharmaceutical composition wherein the adjuvant is ADJUPHOS® or Aluminum phosphate (AlPO4) (col 22, ¶ 2).
Claims 35-38, 44, 48 are rejected under 35 U.S.C. 103 as being unpatentable over Wang, in view of Ugen, and Wang & Walfield, as applied to claims 26, 30-34, 39-41 above, and further in view of Ingelsson (prior art of record).
See claims 35-38, 44 and 48 as submitted on 05/29/2026.
Regarding claims 35 and 36, it is noted that no amendments were introduced to claims 35 and 36 in the amendment filed on 05/29/2026. As previously explained, and indicated above, SEQ ID NO: 112 comprises the following sequences: SEQ ID NO: 83 - SEQ ID NO: 148 - SEQ ID NO: 15. Wang, Ugen, and Wang & Walfield teach a construct with the following features:
a Th cell epitope of the sequence set forth in SEQ ID NO: 83 (ISITEIKGVIVHRIETILF); Wang, SEQ ID NO:46 (col 62, Table 2). See alignment of record.
the spacer sequence of SEQ ID NO: 148 (KKKK). See SEQ ID NO: 32 (KKKK) in Wang’s teachings (col 59, Table 1) has 100% sequence identity to instant SEQ ID NO: 148 (KKKK).
an α-Syn epitope comprising the sequence of SEQ ID NO: 15 EMPSEEGYQD; Ugen, Peptide Fragment C, (page 923). See alignment of record.
While, Ugen’s Peptide Fragment C comprises the sequence of SEQ ID NO: 15, neither Wang, nor Ugen, nor Wang & Walfield explicitly teach an α-Syn epitope including amino acids 126-135 (EMPSEEGYQD) of the α-Syn protein as set forth in SEQ ID NO: 15.
However, Igelsson teaches a fragment of the α-Syn protein consisting of amino acids 126-135 (EMPSEEGYQD) as identified by immunohistochemistry studies of Lewy bodies present in brain stem and neocortex sections of patients with Parkinson’s disease (PD) (page 1, Figure 1).
It would have been prima facie obvious to a person of ordinary skill in the art, before the effective filing date, to have included the teachings of Ingelsson on the α-Syn peptide (amino acids 126-135) to act as the B cell epitope in the construct design or platform taught by Wang for the benefit of generating a synthetic peptide-based immunotherapeutic and/or vaccine against PD given that Ingelsson demonstrated the presence of this fragment in PD pathology and Wang & Walfield teach that the construct design or platform taught by Wang can be applied to the development of therapeutic and protective vaccines for multiple conditions including chronic and infectious diseases.
One of ordinary skill in the art would have had a reasonable expectation of success for introducing the α-Syn fragment (amino acids 126-135) into the construct comprising a Th cell epitope and a heterologous spacer sequence as taught by Wang given that the methods of vector cloning and peptide expression are known, successfully demonstrated, and commonly used as evidenced by the applied prior art.
Accordingly, the sequence taught by Wang, Ugen, Wang & Walfield, and Ingelsson combined shares 100% sequence identity with instant SEQ ID NO: 112 which is 33 amino acid long, as outlined below:
a Th cell epitope of the sequence set forth in SEQ ID NO: 83 (amino acids 1-19 of SEQ ID NO: 112) (ISITEIKGVIVHRIETILF); taught by Wang, SEQ ID NO:46 (col 62, Table 2). See alignment above.
a spacer sequence of SEQ ID NO: 148 (KKKK) (amino acids 20-23 of SEQ ID NO: 112). Taught by Wang’s SEQ ID NO: 32 (KKKK) (col 59, Table 1) which has 100% sequence identity to instant SEQ ID NO: 148 (KKKK).
an α-Syn epitope comprising amino acids 126-135 (EMPSEEGYQD) of the α-Syn protein of SEQ ID NO: 15 (amino acids 24-33 of SEQ ID NO: 112), taught by Ingelsson (page 1, Figure 1).
Therefore, the teachings of Wang, Ugen, Wang & Walfield, and Ingelsson combined meet the limitations of claims 35 and 36.
Regarding claim 37, it is noted that no amendments were introduced to claim 37 in the amendment filed on 05/29/2026. As previously explained, instant Specification does not provide a clear indication of what the basic and novel characteristics actually are as to SEQ ID NO:112, therefore, “consisting essentially of” will be construed as equivalent to “comprising.” See MPEP 2111.03. For the purposes of searching for and applying prior art under 35 U.S.C. 102 and 103, absent a clear indication in the specification or claims of what the basic and novel characteristics actually are, “consisting essentially of” will be construed as equivalent to “comprising.” See, e.g., PPG, 156 F.3d at 1355, 48 USPQ2d at 1355 (“PPG could have defined the scope of the phrase ‘consisting essentially of’ for purposes of its patent by making clear in its specification what it regarded as constituting a material change in the basic and novel characteristics of the invention.”)
Accordingly, as indicated above, the construct taught by Wang in view of Ugen, Wang and Walfield, and Ingelsson comprises the sequences outlined above and therefore shares 100% sequence identity with SEQ ID NO: 112.
Regarding claim 38, it is noted that no amendments were introduced to claim 38 in the amendment filed on 05/29/2026. As previously explained, the sequence taught by Wang, Ugen, Wang & Walfield, and Ingelsson combined shares 100% sequence identity with instant SEQ ID NO: 112 which is 33 amino acid long, as outlined above. It is noted that the combination of the sequences taught by Wang and Ingelsson as outlined above consist of the sequence of SEQ ID NO: 112. It is further noted that the sequences taught by Wang and Ingelsson consists of the exact regions as outlined above. Accordingly, the construct taught by Wang in view of Ugen, Wang and Walfield, and Ingelsson consists of the sequences outlined above which shares 100% sequence identity with SEQ ID NO: 112.
Regarding claim 44, it is noted that no amendments were introduced to claim 44 in the amendment filed on 05/29/2026. As previously explained, Wang further teaches a pharmaceutical composition of claim 41 comprising the construct of claim 26 and set forth in SEQ ID NO: 112 which, as explained above, was rendered obvious by the teachings of Wang, Ugen, Wang & Walfield, and Ingelsson.
Regarding claims 48, it is noted that no amendments were introduced to claim 48 in the amendment filed on 05/29/2026. As previously explained, Wang further teaches a pharmaceutical composition of claim 40 as indicated above which comprises the construct of claim 26 and set forth in SEQ ID NO: 112 which, as explained above, was rendered obvious by the teachings of Wang, Ugen, Wang & Walfield, and Ingelsson. Wang teaches a pharmaceutical composition wherein the adjuvant is ADJUPHOS® or Aluminum phosphate (AlPO4) (col 22, ¶ 2).
Response to Arguments
Applicant's arguments filed 05/29/2026 have been fully considered but they are not persuasive.
Applicant contends on page 9 of the Remarks submitted on 05/29/2026:
“nothing in the cited references motivates or provides a reason for picking and choosing the specific B cell epitope of Applicant's claims for combining with the T helper cell epitope/spacer as claimed. Further, the cited references, considered together, do not render the peptide immunogen constructs of the claims predictable with a reasonable expectation of success. It was not reasonably predictable based on Wang, Wang & Walfield, Ugen, and Ingelsson that a peptide immunogen combining the B cell epitope of SEQ ID NO: 15 and the T helper cell epitope of SEQ ID NO: 83 would be specifically effective against pathological forms of alpha-synuclein.”
In response:
The instant rejection is in view of instant claim language. Although the claims are interpreted in light of the Specification, limitations from the Specification are not read into the claims. See In re Van Geuns, 988 F.2d 1181, 26 USPQ2d 1057 (Fed. Cir. 1993). The instant claims neither recite nor require effectiveness against pathological forms of alpha-synuclein. Further, as previously noted, Ugen already demonstrated effective humoral immune response (antibody production) upon stimulation with a peptide fragment B and peptide fragment C (instant SEQ ID NO: 15) (“Epitope mapping of the anti-sera generated from the vaccinated animals revealed that antibodies produced…”, see pages 923-924). Further, Igelsson teaches a fragment of the α-Syn protein consisting of amino acids 126-135 (EMPSEEGYQD) as identified by immunohistochemistry studies of Lewy bodies present in brain stem and neocortex sections of patients with Parkinson’s disease (PD) (page 1, Figure 1). Therefore, on the contrary, the precise sequence of the α-Syn peptide (amino acids 126-135) was well recognized in the art as a B cell epitope capable of stimulating an antibody response. Hence, the prior art provides clear teachings, suggestions and motivation to combine all elements of the claimed invention into a single construct, as recited in instant claims. Accordingly, the claimed construct represents an obvious embodiment of the teachings of the cited prior art. See MPEP 2144.07. The selection of a known material based on its suitability for its intended use supported a prima facie obviousness determination in Sinclair & Carroll Co. v. Interchemical Corp., 325 U.S. 327, 65 USPQ 297 (1945).
Response to Declaration under 37 C. F. R. § 1.132
Applicant’s Rule 132 Declaration filed on 05/29/206 has been thoroughly reviewed and considered.
The Declaration under 37 CFR 1.132 filed on 05/29/206 is insufficient to overcome the rejection of instant claims as set forth in this Office Action because of the reasons explained below.
Turning to the arguments and data provided in Applicant’s Declaration:
Mr. Dodart notes on page 3 of the Declaration “These data do not show any treatment effect of the antibody directed against amino acids 126-135 of α-synuclein or suggest any therapeutics, much less the peptide immunogen construct therapeutics specified in the claims of the above-referenced patent application. This disclosure would not have informed a practitioner of ordinary skill in the field as to whether the fragment of amino acids 126-135 of α-synuclein can be effectively used in any peptide immunogen construct therapeutics.” This argument is not persuasive because as noted previously Ingelsson demonstrated that amino acids 126-135 of the α-Syn protein are mostly accessible for binding by the antibody when the protein is in the aggregated form in Lewy bodies and/or Lewy neurites, and not when the protein is in its native unfolded monomer conformation (Ingelsson, Fig. 1). The precise sequence of the α-Syn peptide (amino acids 126-135) was well recognized in the art as a B cell epitope capable of stimulating an antibody response. Further, Ingelsson already teaches neurotoxic properties and represents an appropriate molecular target for therapeutic intervention in Parkinson's disease (Abstract). Further, it is well within the purview of one of ordinary skill in the art, based on the teachings of the cited prior art, to reasonably select such fragment of the α-Syn protein as a potential target in drug development. Further, as noted above and previously, instant rejection is in view of instant claim language. Although the claims are interpreted in light of the Specification, limitations from the Specification are not read into the claims. See In re Van Geuns, 988 F.2d 1181, 26 USPQ2d 1057 (Fed. Cir. 1993). The instant claims neither recite nor require effective use of the fragment in question in peptide immunogen construct therapeutics.
Mr. Dodart notes on page 3 of the Declaration “Ugen does not disclose any peptide immunogen constructs appropriate for administering to a subject or any dendritic cell-independent peptide immunogen inoculation approach. The disclosure of α-synuclein peptide fragments in Ugen would not have informed a practitioner of ordinary skill in the field (such as a neuroscientist with a Ph.D.), and certainly not with a reasonable expectation of success, which α-synuclein B cell epitope peptides would be effective in the context of UBITh-containing peptide immunogen constructs”. This argument is not persuasive because as noted previously, Ugen was cited for teaching a peptide termed “Peptide Fragment C” (MPVDPDNEAYEMPSEEGYQDY) comprises a sequence that shares 100% sequence identity with instant SEQ ID NO: 15 (see alignment of record - Peptide Fragment C with instant SEQ ID NO: 15); and Wang was cited for teaching the construct design or platform. Further Ugen teaches an effective humoral immune response upon stimulation with Peptide Fragment B and Peptide Fragment C (page 923-924). Together, Wang and Ugen teach all components of the construct as recited in claim 26.
Mr. Dodart’s argument that the claimed peptide immunogen construct elicits antibodies “with surprising and superior specificity to pathological aggregates of α-synuclein” is not persuasive because as indicated previously, Ugen already demonstrated an effective humoral immune response upon stimulation with Peptide Fragment B and Peptide Fragment C (page 923-924). Accordingly, it is not clear why the antibody response referred to by Mr. Dodart is surprising. In fact, such response would be considered entirely expected and consistent with the prior art. It is not clear why Mr. Dodart refers to such a result as surprising. More importantly, as indicated above, the generation of specific antibodies against pathological aggregates of α-synuclein or any other protein target is not a limitation of the instant claims and therefore it is of no relevance to overcome the rejections of record.
With respect to the data provided in the Declaration, it is noted that the assay supervised by Mr. Dodart which draws a comparison of the performance of antibodies generated by a peptide immunogen residues 126-135 of α-synuclein versus a longer fragment of residues 85-140 of α-synuclein, such results appear to be consistent with the teachings of the cited prior art also cited in the instant rejections of record. The fragment in question as indicated above in detail was already known in the art and there is no evidence in the prior art to suggest that a longer fragment, such as one comprising residues 85-140 of α-synuclein would elicit a similar or better antibody response. It is not clear why Mr. Dodart cites such results as surprising and/or unexpected, nor why a longer fragment 56 residues long would provide evidence of surprising and/or unexpected results. Given that the fragment in question comprising residues 126-135 of α-synuclein was already taught and recognized in the prior art, the cited results are not considered surprising nor unexpected. Further, Mr. Dodart has not provided any baseline or basis for the comparison tested in regards to expected versus unexpected results in view of the instant claim language, rather merely stating or asserting or concluding that results are unexpected. The arguments of counsel cannot take the place of evidence in the record. In re Schulze, 346 F.2d 600, 602, 145 USPQ 716, 718 (CCPA 1965). Further, the fact that Applicant has recognized another advantage which would flow naturally from following the suggestion of the prior art cannot be the basis for patentability when the differences would otherwise be obvious. See Ex parte Obiaya, 227 USPQ 58, 60 (Bd. Pat. App. & Inter. 1985; … See also MPEP 2112: 2112.01 Composition, Product, and Apparatus Claims: I. PRODUCT AND APPARATUS CLAIMS — WHEN THE STRUCTURE RECITED IN THE REFERENCE IS SUBSTANTIALLY IDENTICAL TO THAT OF THE CLAIMS, CLAIMED PROPERTIES OR FUNCTIONS ARE PRESUMED TO BE INHERENT: Where the claimed and prior art products are identical or substantially identical in structure or composition, or are produced by identical or substantially identical processes, a prima facie case of either anticipation or obviousness has been established. Therefore, if the prior art teaches the identical chemical structure, the properties applicant discloses and/or claims are necessarily present. Id.). Further, it is noted that the peptides taught by Ugen are 20 or less residues long, while the longer fragment used in Mr. Dodart’s assay is 56 residues long, and as such these are not considered analogous nor comparable in the context of the assay as described by Mr. Dodart.
As indicated above, applicant’s 37 CFR 1.132 Declaration has been thoroughly reviewed and considered but in view of the foregoing, when all of the evidence is considered, the totality of the rebuttal evidence of nonobviousness fails to outweigh the evidence of obviousness.
Conclusion
No claims are allowed.
Any inquiry concerning this communication or earlier communications from the examiner should be directed to MARLENE V BUCKMASTER whose telephone number is (703)756-5371. The examiner can normally be reached M-R 8:00 AM - 5:00 PM.
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/MARLENE V BUCKMASTER/Examiner, Art Unit 1672
/NICOLE KINSEY WHITE/Primary Examiner, Art Unit 1672
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