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 .
Priority
This application is a 371 of PCT/CN2021/071497 filed 01/13/2021. Applicant’s claim for the benefit of a prior-filed application under 35 U.S.C. 119(e) or under 35 U.S.C. 120, 121, 365(c), or 386(c) is acknowledged.
Acknowledgment is made of applicant’s claim for foreign priority under 35 U.S.C. 119 (a)-(d) based on CN 202010036519.0 filed 01/14/2020 and CN 202010036500.6 filed 01/14/2020. Receipt is acknowledged of certified copies of papers required by 37 CFR 1.55.
Status of the Claims
Claims 1-15 and 19-26 are pending. Claims 1-8, 14 and 20 are amended. Claims 9-13 and 19-25 are withdrawn. Claims 16-18 are cancelled. Claim 26 is new.
Claims 1-8, 14, 15 and 26 (claim set filed 08/28/2025) are examined on the merits herein.
Withdrawal of Rejections
The response and amendment filed on 08/28/2025 are acknowledged. All of the amendment and arguments have been thoroughly reviewed and considered.
For the purposes of clarity of the record, the reasons for the Examiner's withdrawal and/or maintaining if applicable, of the substantive or essential claim rejections are detailed directly below and/or in the Examiner's response to arguments section.
The previous objection to duplicate claims 16 and 18 has been withdrawn necessitated by cancellation of claims 16 and 18.
The previous claims 4, 7, 8 and 14-18 rejections under 35 U.S.C. 112(b) have been withdrawn necessitated by amendment of claim 4, 7, 8 and 14 and cancellation of claims 16-18.
The previous claim 17 rejection under 35 U.S.C. 101 has been withdrawn necessitated by cancellation of claim 17.
The previous claims 1-8, 16 and 18 rejection under 35 U.S.C. 102(a)(1) has been withdrawn necessitated by amendment of claim 1-8 and cancellation of claims 16 and 18.
New Rejection
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 1-8, 14, 15 and 26 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.
Claim 1 is directed to a polypeptide composition comprising polypeptide A and polypeptide B. Claim 1 recites: “the polypeptide A comprises the amino acid sequence shown in SEQ ID NO: 103 or a functional variant thereof, and the functional variant has xanthine amide hydrolase activity”. The specification describes that “the polypeptide B comprises the amino acid sequence shown in SEQ ID NO: 103 or a functional variant thereof, and the functional variant has xanthine amide hydrolase activity” (paragraph 0020). Therefore, the recitation “the polypeptide A comprises the amino acid sequence shown in SEQ ID NO: 103 or a functional variant thereof, and the functional variant has xanthine amide hydrolase activity” is not supported by the specification. Thus, since the support for the claim 1 is not provided, claim 1 contains new matter. One of ordinary skill in the art would not conclude that the applicant would have been in possession of the subject matter of claim 1 at the time of filing application.
Claims 2-8, 14, 15 and 26 do not resolve the issue mentioned above and are rejected.
Under the broadest reasonable interpretation claim 17 is examined as directed to a polypeptide composition comprising polypeptide A with SEQ ID NO: 1 or a functional variant thereof and polypeptide B with SEQ ID NO: 103 or a functional variant thereof.
Maintained/Modified Rejections
The following rejections are maintained and/or modified taking into consideration amendment to claims filed on 08/28/2025.
Claim Rejections - 35 USC § 103
The text of those sections of Title 35, U.S. Code not included in this action can be found in a prior Office action.
Claims 1-6 are rejected under 35 U.S.C. 103 as being unpatentable over GenBank 1 (GenBank KMT22110.1, 2015 [retrieved on 01/13/2025]. Retrieved from the Internet:< isochorismatase-like protein [Clostridium cylindrosporum DSM 605] - Protein - NCBI>) in view of Rabinowitz (Rabinowitz and Pricer J. Biol. Chem., 1956, 218, 189-199 on record in IDS) and GenBank 2 (GenBank AND39904.1, 2016 [retrieved on 11/30/2025]. Retrieved from the Internet <allantoinase [Cytobacillus oceanisediminis 2691] - Protein - NCBI>).
Regarding claim 1, GenBank 1 provides sequence for isochorismatase-like protein from Clostridium cylindrosporum DSM 605 genome. The sequence from GenBank 1 is 100% identical to instant SEQ ID NO:1 of the polypeptide A. Since GenBank teaches polypeptide with the claimed sequence, this polypeptide will necessarily possess 4-ureido-5-carboxyimidazole amide hydrolase activity. MPEP 2112.01 states: “Products of identical chemical composition cannot have mutually exclusive properties." In re Spada, 911 F.2d 705, 709, 15 USPQ2d 1655, 1658 (Fed. Cir. 1990). A chemical composition and its properties are inseparable. Therefore, if the prior art teaches the identical chemical structure, the properties applicant discloses and/or claims are necessarily present.”
GenBank does not teach a polypeptide B with SEQ ID NO: 103 or a functional variant thereof with xanthine amide hydrolase activity.
Rabinowitz teaches purine fermentation by Clostridium cylindrosporum (Title). Rabinowitz describes degradation of xanthine to glycine, formic acid and ammonia by extracts of Clostridium cylindrosporum (p. 189, 1st paragraph and p. 190 – scheme). Rabinowitz mentions that another biochemical transformation of xanthine is to uric acid (p. 198, 2ndparagraph). Rabinowitz discloses that xanthine incubated with Clostridium cylindrosporum extracts is converted to 4-ureido-5-carboxyimidazole carboxylic acid and in vitro incubation of 4-ureido-5-carboxyimidazole carboxylic acid with the extracts of Clostridium cylindrosporum results in its degradation (hydrolysis) to 4-amino-5 imidazole carboxylic acid (p. 196, 3rd paragraph, pp. 198-199 - Summary). Rabinowitz mentions that hydrolysis to 4-ureido-5-carboxyimidazole carboxylic acid is similar to conversion of allantoin to allantoic acid (p. 198, 2nd paragraph). Thus, Rabinowitz indicated presence of another enzyme in the xanthine degradation pathway catalyzing reaction of formation of 4-ureido-5-carboxyimidazole carboxylic acid.
GenBank 2 teaches the sequence for allantoinase from Cytobacillus oceanisediminis 2691. That polypeptide has 100% identity to instant SEQ ID NO: 103 and hence necessarily has the claimed activity of xanthine amide hydrolase.
It would have been obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to follow teaching of Rabinowitz and identify the polypeptide of GenBank 1 teaching isolated from Clostridium cylindrosporum as the enzyme of the xanthine degradation pathway and confirm its enzymatic activity in vitro by hydrolysis of 4-ureido-5-carboxyimidazole carboxylic acid. One would have been motivated to do so since Rabinowitz identified intermediates in the xanthine degradation pathway in Clostridium cylindrosporum and measured hydrolysis of 4-ureido-5-carboxyimidazole carboxylic acid which is the inherent functional property of the polypeptide from GenBank 1 teaching isolated from the same species. A skilled artisan would have reasonably expected success in this combination because GenBank 1 and Rabinowitz teach the enzyme with the same activity.
It would have been obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to add another enzyme of the xanthine degradation pathway, xanthine amide hydrolase, taught by GenBank 2 and preceding the 4-ureido-5-carboxyimidazole amide hydrolase in the xanthine degradation pathway as was shown by Rabinowitz. One would have been motivated to do so since Rabinowitz identified intermediates in the xanthine degradation pathway and predicted presence of xanthine amide hydrolase producing in 4-ureido-5-carboxyimidazole carboxylic acid and having reaction similar to allantoin conversion to allantoic acid and xanthine amide hydrolase activity is the inherent functional property of the polypeptide from GenBank 2 identical to claimed polypeptide B and this polypeptide is referred as allantoinase in GenBank 2. A skilled artisan would have reasonably expected success in this combination because GenBank 1, GenBank 2 and Rabinowitz teach the enzymes with the same activities, GenBank 1 and GenBank 2 provided the sequences and Rabinowitz identified pathway and intermediates and described the instructions for the enzymatic reactions. Thus, GenBank 1, Rabinowitz and GenBank 2 teachings render claim 1 obvious.
Regarding claim 2-6, claim 2 is directed to a catalytic site of the polypeptide A and claim 5 is directed to the binding site of the polypeptide A. Claims 2 and 5 recite the properties of the structure which is the polypeptide A with the SEQ ID NO:1. Claims 3 and 4 recite further limitation of claim 2 property and claim 6 recites further limitation for claim 5 property.
Pursuant to MPEP 2112.01(I), 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. In re Best, 562 F.2d 1252, 1255, 195 USPQ 430, 433 (CCPA 1977). Therefore, since the polypeptide of GenBank 1 teaching has the claimed structure, the polypeptide of the prior art inherently has property of a catalytic site including catalytic triads close to each other in spatial conformation further comprising a divalent metal ion and further comprising four amino acid residues coordinated with metal ion and the polypeptide of GenBank 1 teaching inherently has property of a binding site with the defined amino acid residues close to each other and the distance between the catalytic site and the binding site of not more than 5 angstroms. Thus, GenBank 1, Rabinowitz and GenBank 2 teachings render claims 2-6 obvious.
Claims 7, 8 and 26 are rejected under 35 U.S.C. 103 as being unpatentable over GenBank 1 (GenBank KMT22110.1, 2015 [retrieved on 01/13/2025]. Retrieved from the Internet:< isochorismatase-like protein [Clostridium cylindrosporum DSM 605] - Protein - NCBI>) in view of Rabinowitz (Rabinowitz and Pricer J. Biol. Chem., 1956, 218, 189-199 on record in IDS) and GenBank 2 (GenBank AND39904.1, 2016 [retrieved on 11/30/2025]. Retrieved from the Internet <allantoinase [Cytobacillus oceanisediminis 2691] - Protein - NCBI>) as applied to claim 1 above, and further in view of UniProt (UniProt A0A1M5YT22, 2017 [retrieved on 11/30/2025]. Retrieved from the Internet <https://www.uniprot.org/uniprotkb/A0A1M5YT22/entry>).
The teachings of GenBank1, Rabinowitz and GenBank 2 have been set forth above.
GenBank 1, Rabinowitz and GenBank 2 do not teach the functional variant of the polypeptide A, a natural isoenzyme from the recited species and modifications of the sequence of which do not occur in the catalytic and/or binding site of polypeptide A.
UniProt teaches polypeptide from Sporanaerobacter acetigenes DSM 13106 having isochorismatase-like domain (p. 4) and sequence that has 68.3% identity to SEQ ID NO:1. Additionally, the claimed catalytic site residues, C134, D10, K101, H61, H74, E59 and D67 and the claimed binding site residues, F15, R71, V129, H104 and W130 are not modified in the UniProt sequence and hence modifications (substitutions and deletions) do not occur in the catalytic and binding sites of polypeptide A.
It would have been obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to assume that the polypeptide from Sporanaerobacter acetigenes DSM 13106 taught by UniProt is a natural isoenzyme of the polypeptide of GenBank 1 from Clostridium cylindrosporum DSM 605 identical to claimed polypeptide A. One would have been motivated to do that since the sequence of UniProt polypeptide has 68.3% identity to polypeptide of GenBank 1 and SEQ ID NO:1 of the claimed polypeptide A and has unmodified claimed amino acid residues of catalytic and binding sites and hence can be predicted to have the same functional properties. A skilled artisan would have reasonably expected success in that because GenBank 1 polypeptide is called isochorismatase-like protein and UniProt polypeptide has isochorismatase-like domain indicating similar functional properties and these polypeptides have the same amino acid residues critical for the function of 4-ureido-5-carboxyimidazole amide hydrolase. Thus, teachings of GenBank 1, Rabinowitz, GenBank 2 and UniProt render claims 7, 8 and 26 obvious.
Claims 14 and 15 are rejected under 35 U.S.C. 103 as being unpatentable over GenBank 1 (GenBank KMT22110.1, 2015 [retrieved on 01/13/2025]. Retrieved from the Internet:< isochorismatase-like protein [Clostridium cylindrosporum DSM 605] - Protein - NCBI>) in view of Rabinowitz (Rabinowitz and Pricer J. Biol. Chem., 1956, 218, 189-199 on record in IDS) and GenBank 2 (GenBank AND39904.1, 2016 [retrieved on 11/30/2025]. Retrieved from the Internet <allantoinase [Cytobacillus oceanisediminis 2691] - Protein - NCBI>) as applied to claim 1 above, and further in view of Percudani (WO 2007052326 A2).
The teachings of GenBank1, Rabinowitz and GenBank 2 have been set forth above. Since the polypeptide of GenBank 1 teaching has the identical structure to the claimed polypeptide A with SEQ ID NO:1 as described above, the polypeptide of the prior art inherently possesses the claimed functional property, i.e. 4-ureido-5-carboxyimidazole amide hydrolase activity. Since the polypeptide of GenBank 2 teaching has the identical structure to the claimed polypeptide A with SEQ ID NO:103 as described above, the polypeptide of the prior art inherently possesses the claimed functional property, i.e. xanthine amide hydrolase activity. However, GenBank 1, Rabinowitz and GenBank 2 do not teach the pharmaceutical composition comprising the polypeptide A and polypeptide B which is used for prevention, intervention and/or treatment of gout.
Regarding claims 14 and 15, Percudani teaches a pharmaceutical composition for treating uric acid related disorders by modulating uric acid conversion to allantoin (Abstract). Percudani describes oxidation of xanthine in the purine degradation pathway to uric acid by xanthine oxidase. The uric acid can be further oxidized to allantoin by urate oxidase in most mammals but not in humans. Humans do not have enzyme degrading uric acid and high level of uric acid (hyperuricemia) can lead to such condition as gout when crystals accumulate in joints (p. 1, lines 7-19). Percudani discloses two specific enzymes which can degrade uric acid to allantoin and describes that administration of these polypeptides together with urate oxidase can provide treatment of hyperuricemia (p. 3, lines 9-12, 22- 25). Percudani teaches pharmaceutical composition comprising at least one these polypeptides for treatment of uric acid related disorders (p. 4, lines 28-29).
It would have been obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to follow teaching of Percudani and prepare pharmaceutical composition for treatment of uric acid related disorders such as gout as described by Percudani with the polypeptides from GenBank 1 and GenBank 2 which are involved in degradation of xanthine as taught by Rabinowitz. One would have been motivated to do so since GenBank 1 provides the sequence of the polypeptide catalyzing hydrolysis of 4-ureido-5-carboxyimidazole carboxylic acid, GenBank 2 provides the sequence of the polypeptide catalyzing production of 4-ureido-5-carboxyimidazole carboxylic acid, Rabinowitz showed that activities to be involved in the degradation of xanthine and Percudani teaches that conversion of xanthine to uric acid leads to disorders such as gout and can be treated with removal of uric acid and hence hydrolysis of xanthine by the pathway described by Rabinowitz will decrease production of uric acid. A skilled artisan would have reasonably expected success in this combination because GenBank 1, GenBank 2, Rabinowitz and Percudani teach enzymes involved in xanthine degradation. Thus, GenBank 1, Rabinowitz, GenBank 2 and Percudani teachings render claims 14 and 15 obvious.
Response to Arguments
Applicant's arguments filed 08/28/2025 have been fully considered but they are not persuasive.
Applicant argues (addressing pages 8-9 of the Remarks) that the amended claim 1 is directed to a polypeptide composition and recites polypeptide B in the polypeptide composition that is not taught by GenBank 1 reference and that Rabinowitz and Percudani do not cure the deficiencies of GenBank, as they also fail to teach or suggest the polypeptide composition of claim 1.
These arguments are not persuasive because the 35 U.S.C. 102(a)(1) has been withdrawn necessitated by amendment of claim 1 and the current 35 U.S.C. 103 rejection of claim 1 is based on the combination of prior art of GenBank 1, Rabinowitz and GenBank 2 as described in the rejection above, wherein GenBank 1 teaches the sequence of the polypeptide A inherently possessing 4-ureido-5-carboxyimidazole amide hydrolase activity, GenBank 2 provides the sequence of the polypeptide B inherently possessing xanthine amide hydrolase activity and Rabinowitz teaches xanthine degradation pathway including both functional activities of the polypeptide B, i.e. hydrolysis to produce 4-ureido-5-carboxyimidazole carboxylic acid and the polypeptide A, i.e. hydrolysis of the 4-ureido-5-carboxyimidazole carboxylic acid.
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 1, 14 and 15 are provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claim 18 of copending Application No. 17/793,009 in view of GenBank 1 (GenBank KMT22110.1, 2015 [retrieved on 01/13/2025]. Retrieved from the Internet:< isochorismatase-like protein [Clostridium cylindrosporum DSM 605] - Protein - NCBI>) and Rabinowitz (Rabinowitz and Pricer J. Biol. Chem., 1956, 218, 189-199 on record in IDS).
Claim 1 is directed to a polypeptide composition comprising polypeptide A and polypeptide B or functional variants thereof. Claims 14 and 15 are directed to a pharmaceutical composition comprising polypeptide composition of claim 1 used for prevention, intervention and/or treatment of gout.
Regarding claims 1, 14 and 15, reference claim 18 teaches a method for treating goat comprising the polypeptide functional variant of claim 1 which comprises amino acid sequence with SEQ ID NO:1 with xanthine amide hydrolase activity. The SEQ ID NO: 1 of reference application is 100% identical to instant SEQ ID NO:103 for polypeptide B. Although the reference application teaches method of treatment, it would be obvious to one of ordinary skill in the art that the method of treatment requires the pharmaceutical composition.
The reference claim 18 does not teach the polypeptide A. GenBank 1 teaches polypeptide from Clostridium cylindrosporum DSM 605 genome 100% identical to instant SEQ ID NO:1 of the instant polypeptide A. Since the Clostridium cylindrosporum polypeptide of GenBank teaching has the identical structure to the claimed polypeptide A with SEQ ID NO:1, the polypeptide of the prior art inherently possesses the claimed functional property, i.e. 4-ureido-5-carboxyimidazole amide hydrolase activity.
Rabinowitz teaches that xanthine incubated with Clostridium cylindrosporum extracts is converted to 4-ureido-5-carboxyimidazole carboxylic acid which is hydrolyzed to 4-amino-5-imidazole carboxylic acid (p. 196, 3rd paragraph, pp. 198-199 - Summary) and thus describes sequential reactions of the claimed polypeptide B with xanthine amide hydrolase activity and polypeptide A with 4-ureido-5- carboxyimidazole amide hydrolase activity in Clostridium cylindrosporum extracts.
It would have been obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to add polypeptide from GenBank 1 teaching to the pharmaceutical composition for treatment of gout based on method taught in the reference application. One would have been motivated to do so since GenBank 1 provides the sequence of the polypeptide catalyzing hydrolysis of 4-ureido-5-carboxyimidazole carboxylic acid and the reference application teaches method comprising polypeptide of the same pathway hydrolyzing xanthine as shown by Rabinowitz and resulting in production of 4-ureido-5-carboxyimidazole carboxylic acid and hence the combination of polypeptides will decrease production of uric acid from xanthine resulting in prevention or treatment of gout. A skilled artisan would have reasonably expected success in this combination because the reference application, GenBank 1 and Rabinowitz teach enzymes involved in xanthine degradation. Thus, combination of the reference claim 18, GenBank 1 and Rabinowitz renders claims 1, 14 and 15 obvious.
Therefore, since instant claims 1, 14 and 15 encompass the subject matter of the reference claim 18, they are rejected under obviousness double patenting.
This is a provisional nonstatutory double patenting rejection.
Response to Arguments
Applicant's arguments filed 08/28/2025 have been fully considered but they are not persuasive.
Applicant argues (addressing p. 9 of the Remarks) that the amended claim 14 recites pharmaceutical composition including polypeptide B not covered by GenBank 1 and Rabinowitz teaching.
These arguments are not persuasive although GenBank 1 and Rabinowitz do not teach polypeptide B, the reference claim 18 does since it teaches treatment with the polypeptide of claim 1 having amino acid sequence with SEQ ID NO:1 identical to instant SEQ ID NO:103 for the polypeptide B and the same activity of xanthine amide hydrolase. Therefore the combination of the reference claim 18, GenBank 1 and Rabinowitz makes claims 1, 14 and 15 obvious as described above. Thus, the double patenting rejection is maintained and modified necessitated by amendment of claim 1.
Conclusion
No claims are allowed.
Applicant's amendment necessitated the new ground(s) of rejection presented in this Office action. Accordingly, THIS ACTION IS MADE FINAL. See MPEP § 706.07(a). Applicant is reminded of the extension of time policy as set forth in 37 CFR 1.136(a).
A shortened statutory period for reply to this final action is set to expire THREE MONTHS from the mailing date of this action. In the event a first reply is filed within TWO MONTHS of the mailing date of this final action and the advisory action is not mailed until after the end of the THREE-MONTH shortened statutory period, then the shortened statutory period will expire on the date the advisory action is mailed, and any nonprovisional extension fee (37 CFR 1.17(a)) pursuant to 37 CFR 1.136(a) will be calculated from the mailing date of the advisory action. In no event, however, will the statutory period for reply expire later than SIX MONTHS from the mailing date of this final action.
Any inquiry concerning this communication or earlier communications from the examiner should be directed to LIOUBOV G KOROTCHKINA whose telephone number is (571)270-0911. The examiner can normally be reached Monday-Friday: 8:00-5:30.
Examiner interviews are available via telephone, in-person, and video conferencing using a USPTO supplied web-based collaboration tool. To schedule an interview, applicant is encouraged to use the USPTO Automated Interview Request (AIR) at http://www.uspto.gov/interviewpractice.
If attempts to reach the examiner by telephone are unsuccessful, the examiner’s supervisor, Sharmila G Landau can be reached at (571)272-0614. The fax phone number for the organization where this application or proceeding is assigned is 571-273-8300.
Information regarding the status of published or unpublished applications may be obtained from Patent Center. Unpublished application information in Patent Center is available to registered users. To file and manage patent submissions in Patent Center, visit: https://patentcenter.uspto.gov. Visit https://www.uspto.gov/patents/apply/patent-center for more information about Patent Center and https://www.uspto.gov/patents/docx for information about filing in DOCX format. For additional questions, contact the Electronic Business Center (EBC) at 866-217-9197 (toll-free). If you would like assistance from a USPTO Customer Service Representative, call 800-786-9199 (IN USA OR CANADA) or 571-272-1000.
/L.G.K./Examiner, Art Unit 1653
/SHARMILA G LANDAU/Supervisory Patent Examiner, Art Unit 1653
Prosecution Insights