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 .
Applicant’s response on 12/08/2025 has been received and entered
Claims 1, 4-16, 20, 28-31, and 39-42 are pending, all of which have been considered on the merits.
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and the fee set forth in 37 CFR 1.17(e) has been timely paid, the finality of the previous Office action has been withdrawn pursuant to 37 CFR 1.114.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 8/15/2025 has been entered.
Status of Prior Rejections/Response to Arguments
RE: Rejection of claims 43-44 under 35 U.S.C. 102 over Dix (US20120097565A1).
Applicants have cancelled claims 43-44 rendering the rejection moot.
RE: Rejection of claims 1, 4-5, 8-9, 11-14, 20, 28-29, and 31 under 35 U.S.C. 103 over Irfan (New Castle University, 2017) in view of Xu (Biotechnol. Prog., 2017).
Applicants traversed the rejection of record on the grounds that Irfan and Xu fail to teach all the limitations of the claims as amended. Claims 1, 13, and 20 have been amended to comprise the limitation “wherein the proportion of acidic variants decreases as pCO2 conditions increase”.
In response, the argument has been fully considered but is not convincing. The newly added limitation of “wherein the proportion of acidic variants decreases as pCO2 conditions increase” does not limit the active steps of the claimed method. While the experiments of Irfan show a different trend in the percentage of acidic variants produced by altering pCO2 conditions, Irfan in view of Xu still teach a method that comprises the active steps of the claimed method.
Applicants further argue the method of Irfan produces the lowest level of acidic variants at 20 mmHg CO2, and the proportion of acidic variants increased over time with increasing CO2 partial pressure conditions. This is in contrast with Applicant’s data that shows a direct correlation between lowering pCO2 conditions and reducing acidic variants.
In response, this argument has been fully considered, but is not found persuasive. While the results of Irfan show a different overall trend, the overall trend does not limit the active steps of the claimed method. Irfan teaches culturing CHO cells (reads on mammalian cells) modified to express IgG mAbs at pCO2 of 140 mmHg, and report that cells cultured at this condition produced mAbs with fewer acidic variants than the cells cultured at standard pCO2 (reads on without the pCO2 conditions) (See Fig. (2.4)). The data point of Irfan teaches the same results as the claims. The difference in trends does not negate the results of the cited data point.
Additionally, applicants argue Xu teaches CO2 sparging generally increases CO2 levels resulting in increased culture pH but Xu does not teach how CO2 sparging reduces acidic charge variant.
In response to applicant's argument, the test for obviousness is not whether the features of a secondary reference may be bodily incorporated into the structure of the primary reference; nor is it that the claimed invention must be expressly suggested in any one or all of the references. Rather, the test is what the combined teachings of the references would have suggested to those of ordinary skill in the art. See In re Keller, 642 F.2d 413, 208 USPQ 871 (CCPA 1981). Xu teaches CO2 sparging can be used to increase pCO2 during antibody production. It would have been obvious to use CO2 sparging to increase pCO2 in the antibody production method of Irfan. Therefore, Irfan in view of Xu teach the limitations of the claims (See rejection below).
Furthermore, applicants argue the method of the instant application teaches the unexpected result that lower CO2 levels lead to an increase in acidic variants. Whereas Irfan does not teach this overall trend.
In response, Irfan teaches the claimed limitations of producing less acidic acid charge variants at 140 mmHg of CO2 than would be produced without the pCO2 conditions (See discussion of first argument above). Thus, Irfan teaches the results embodied by the claims.
The rejection is maintained.
RE: Rejection of claims 1, 4-6, 8-9, 11-15, 20, 28-29, and 31 under 35 U.S.C. over Irfan (New Castle University, 2017) in view of Xu (Biotechnol. Prog., 2017), and further in view of Papadopoulos et al (US9987500B2)
Applicants traverse the rejection of record on the grounds that Papadopoulos et al do not address the deficiencies in Irfan or Xu.
In response, the argument has been fully considered but is not persuasive. Irfan and Xu teach the limitations of claims 1, 4-5, 8-9, 11-14, 20, 28-29, and 31. Irfan, Xu, and Papadopoulos et al further teach the limitations of claims 6 and 15 (See rejection below).
The rejection is maintained.
RE: Rejection of claims 43-45 under 35 U.S.C. 103 over Irfan (New Castle University, 2017) in view of Martin et al (US20090074793A1).
Applicants have cancelled claims 43-45 rendering the rejection moot.
RE: Rejection of claims 1, 4-5, 7-9, 10-14, 16, 20, 28-31, and 39-45 under 35 U.S.C. 103 over Irfan (New Castle University, 2017) in view of Xu (Biotechnol. Prog., 2017) and Martin et al (US20090074793A1).
Applicants have cancelled claims 43-45 rendering their rejection moot.
Applicants traverse the rejection of record on the grounds that Martin et al do not address the deficiencies in Irfan or Xu.
In response, the argument has been fully considered but is not persuasive. Irfan and Xu teach the limitations of claims 1, 4-5, 8-9, 11-14, 20, 28-29, and 31. Irfan, Xu, and Martin et al further teach the limitations of claims 7, 16, and 39-42 (See rejection below).
The rejection over claims 1, 4-5, 7-9, 10-14, 16, 20, 28-31, and 39-42 is maintained.
Maintained Rejections
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.
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 1, 4-5, 8-9, 11-14, 20, 28-29, and 31 are rejected under 35 U.S.C. 103 as being unpatentable over Irfan (New Castle University, 2017) in view of Xu (Biotechnol. Prog., 2017).
Irfan reports on the effect of pCO2 on mAb production in Chinese Hamster Ovary (CHO) cells (See abstract). Irfan discloses that CHO cells are a cell line commonly used as a mammalian production host for mAbs (See pg. 1 section 1.1 Introduction). CHO cells are able to produce antibodies with major glycoforms identical to glycoforms present in human antibodies (See pg. 5 section Glycosylation and Charge Variants (Product quality attributes)).
Irfan teaches that CO2 and carbonate base are used by most bioreactor processes to control the culture pH (See Pg. 13 Section culture pH) and the most prominent stirred bioreactor on the market controls pH through gas sparging (See pg. 9 section: Microbioreactors). In this study, Irfan reports a CHO-S cell line expressing a humanized IgG1 monoclonal antibody that binds Her2 (See pg. 28 section 2.2.1 Cell Line and Medium). The cells are inoculated to a working volume of 1.4L at a seeding density of 5x105 cells/mL (See pg. 29 section 2.2.2 Bioreactor Cell Culture Runs). The cells are cultured under various pCO2 conditions including baseline, 10, 60, 100, and 140 mmHg (See pg. 30 table 2.2) and harvested 312 hours (See pg. 29 section 2.2.2 Bioreactor Cell Culture Runs). The target mAb profile including mean target mAb, mean acidic variants and mean basic variants were quantified over time (See pg. 35-36, Fig. 2.4). Irfan discovers that increasing the pCO2 concentration has the desirable effect of reducing acidic variants. Charge variants in antibodies can have effects on stability, effect, and safety of mAbs (See pg. 5 Section Glycosylation and Charge Variants (Product quality attributes)).
Regarding claim 1: Irfan teaches culturing a CHO cell line and inoculating a working volume of 1.4L at a seeding density of 5x105 cells/mL which reads on seeding media with mammalian cells that produce antibodies.
Irfan teaches that culturing CHO cells with high CO2 condition (140 mmHg), for 312 hrs, results in a decrease in acidic charge variants compared to baseline (baseline: ~45% vs. 140 mmHg: ~37% see fig 2.4b). Therefore, culturing cells under 140 mmHg for 312 hrs reads on culturing the cells under pCO2 conditions that allow the mammalian cells to produce antibody products with less acidic acid variants than would be obtained without the pCO2.
Additionally, Irfan teaches culturing at 140mmHg pCO2 which reads on pCO2 conditions are 120 mmHg to 140 mmHg of CO2 in media.
Irfan does not disclose using CO2 sparging to attain pCO2 conditions.
Xu (Biotechnol. Prog., 2017) teaches a process for bioreactor scale-up in the production of monoclonal antibodies by CHO cells (See pg. 1147 section Cell line and inoculum expansion). In the disclosed experiments, bioreactor pH was controlled by CO2 sparging (see pg. 1147 section Bioreactor operations). Xu teaches that during process scale-up, lactate consumption increases resulting in pH changes (See pg. 1154 section CO2 removal efficiency). Since pH is largely controlled by lactate and pCO2, active CO2 sparging, which leads to a rapid pCO2 increase, is used to control the pH (See pg. 1152 section. Process scale-up using a combination of P/V and vvm as criterion and pg. 1154 section CO2 removal efficiency). Increasing pCO2 by active gas sparging reads on pCO2 conditions are attained by CO2 sparging.
Given that Irfan teaches using high pCO2 conditions to change antibody charge variants in antibody production by CHO cells and Xu teaches using CO2 sparging to increase pCO2 during antibody production by CHO cells, it would have been prima facie obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to use the CO2 sparging method of Xu to increase pCO2 conditions of Irfan in order to regulate the culture pH which can be altered by lactate consumption. One would have a reasonable expectation of success because Xu teaches that CO2 sparging can be used to increase pCO2 in culture during antibody production. See MPEP 2143(I)(A).
Regarding claim 4: Following the discussion of claim 1 above, Irfan teaches that increasing pCO2 conditions causes a decrease in acidic charge variants (See fig 2.4b).
Irfan does not teach specific pCO2 conditions that result in 0.5% to 4% less acidic antibody variants compared to baseline.
Given that Irfan teaches fewer acidic charge variants can be produced by altering pCO2 conditions, routine optimization of pCO2 conditions needed to reach desired levels of acidic charge variants would have been prima facie obvious to one of ordinary skill in the art. Where the general conditions of a claim are disclosed in the prior art, it is not inventive to discover the optimum or workable ranges by routine experimentation. See MPEP2144.05(II).
Regarding claim 5: Following the discussion of claim 1 above Irfan teaches a humanized IgG1 monoclonal antibody which reads on the antibodies are monoclonal.
Regarding claim 8: Following the discussion of claims 1 and 5 above, Irfan teaches a humanized IgG1 monoclonal antibody which reads on the antibodies are human monoclonal antibodies.
Regarding claim 9: Following the discussion of claims 1, 5, and 8 above, Irfan teaches a humanized IgG1 monoclonal antibody which reads on the antibodies are human monoclonal antibodies are IgG antibodies
Regarding claim 11: Following the discussion of claim 1 above, Irfan teaches culturing CHO cells and harvesting the cells at 312 hrs (13 days) which reads on the cells are cultured for 10-15 days.
Regarding claim 12: Following the discussion of claim 1 above, Irfan discloses using a Chinese hamster ovary (CHO) cell line which reads on the mammalian cells are CHO cells.
Regarding claim 13: Irfan teaches culturing a CHO cell line and inoculating a working volume of 1.4L at a seeding density of 5x105 cells/mL which reads on seeding media with mammalian cells that produce antibodies.
Irfan teaches that culturing cells under 140mmHg pCO2 results in ~63% main target antibody (See Fig2.4a), ~ 22% acidic charge variants (See Fig 2.4b), and ~ 15% basic charge variants (See Fig2.4c) which reads on culturing the cells under pCO2 conditions that that allow the mammalian cells to produce antibodies, wherein the main peak form of antibodies produced by cells comprises between 38% to 65% of total antibodies, the acidic variant of the antibodies comprises 20% to 47% of total antibodies and the basic variant of the antibodies comprises up to 36% of total antibodies.
Irfan does not disclose using CO2 sparging to attain pCO2 conditions.
Xu teaches lactic acid consumption alters culture pH during antibody production. Xu further teaches active CO2 sparging, increase pCO2, and can be used to regulate culture pH during antibody production by CHO cells.
Given that Irfan teaches using high pCO2 conditions to change antibody charge variants in antibody production by CHO cells and Xu teaches using CO2 sparging to increase pCO2 during antibody production by CHO cells, it would have been prima facie obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to use the CO2 sparging method of Xu to increase pCO2 conditions of Irfan in order to regulate the culture pH which can be altered by lactate consumption. One would have a reasonable expectation of success because Xu teaches that CO2 sparging can be used to increase pCO2 in culture during antibody production. See MPEP 2143(I)(A).
Regarding claim 14: Following the discussion of claim 13 above, Irfan teaches a humanized IgG1 monoclonal antibody which reads on the antibodies are human monoclonal antibodies.
Regarding claim 20: Irfan teaches culturing a CHO cell line and inoculating a working volume of 1.4L at a seeding density of 5x105 cells/mL which reads on seeding media with mammalian cells that produce antibodies, antibody derivatives, or antibody fragments.
Irfan further teaches that culturing CHO cells under 140mmHg pCO2 for ~140 hrs results in ~63% main target antibody (See Fig2.4a), ~ 22% acidic charge variants (See Fig 2.4b), and ~ 15% basic charge variants (See Fig2.4c) which reads on culturing the cells under pCO2 conditions that that allow the mammalian cells to produce antibodies… wherein the main peak form of antibodies… produced by cells comprises between 50% to 70% of total antibodies, the acidic variant of the antibodies comprises 20% to 47% of total antibodies and the basic variant of the antibodies comprises up to 15% of total antibodies.
Irfan does not disclose using CO2 sparging to attain pCO2 conditions.
Xu teaches lactic acid consumption alters culture pH during antibody production. Xu further teaches active CO2 sparging, increase pCO2, and can be used to regulate culture pH during antibody production by CHO cells.
Given that Irfan teaches using high pCO2 conditions to change antibody charge variants in antibody production by CHO cells and Xu teaches using CO2 sparging to increase pCO2 during antibody production by CHO cells, it would have been prima facie obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to use the CO2 sparging method of Xu to increase pCO2 conditions of Irfan in order to regulate the culture pH which can be altered by lactate consumption. One would have a reasonable expectation of success because Xu teaches that CO2 sparging can be used to increase pCO2 in culture during antibody production. See MPEP 2143(I)(A).
Regarding claim 28: Following the discussion of claim 20 above, Irfan teaches using CHO cells to produce humanized IgG1 monoclonal HER2 antibodies which reads on the mammalian cells produce human monoclonal antibodies.
Regarding claim 29: Following the discussion of claims 20 and 28 above, Irfan teaches using CHO cells to produce humanized IgG1 monoclonal HER2 antibodies which reads on the human monoclonal antibodies are IgG1 antibodies.
Regarding claim 31: Following the discussion of claim 20 above, Irfan discloses using pCO2 conditions of 60 mmHg, 100 mmHg and 140 mmHg which reads on pCO2 conditions are between 30 mmHg and 210 mmHg.
Claims 1, 4-6, 8-9, 11-15, 20, 28-29, and 31 are rejected under 35 U.S.C. 103 as being unpatentable over Irfan (New Castle University, 2017) in view of Xu (Biotechnol. Prog., 2017), and further in view of Papadopoulos et al (US9987500B2)
The teachings of Irfan and Xu are set forth above.
Irfan and Xu render claims 1, 4-5, 8-9, 11-14, 20, 28-29, and 31 obvious.
Regarding claims 6 and 15: Following the discussion of claims 1,5, 13, and 14 above, Irfan teaches using CHO cells to produce humanized IgG1 monoclonal HER2 antibodies. The antibodies are produced under increasing pCO2 conditions leading to a decrease in acidic variants. This is a desirable effect because charge variants can have an effect on an antibody’s stability, effect, and safety.
Irfan does not teach antibodies capable of binding to PD-1 factor.
Papadopoulos, et al. discloses antibodies and antigen binding fragments that bind PD-1. The antibodies are further described as recombinant monoclonal antibodies or antigen binding fragments that bind specifically to PD-1 and may bind human PD-1 (See col. 2 ln 55-58). The antibodies can be full-length (for example, an IgG1 or IgG4 antibody) or may comprise only an antigen binding portion and may be modified to affect functionality (See Col. 2 lns 48-51). PD-1 antibodies are useful in treating diseases or disorders such as cancer, viral infections, and autoimmune diseases (See Col. 2, lns 45-47). The PD-1 antibodies can be produced by any known method (See col. 21 lns 20-22) including using mammalian cells, such as CHO cells, to express an immunogen (See col. 21 lns 39-42).
Irfan and Papadopoulos, et al. both teach using CHO cells to produce human monoclonal IgG antibodies and that using CHO cells for antibody production is a known method in the field. Papadopoulos, et al. further teaches that CHO cells can specifically produce PD-1 antibodies. Therefore, it would have been prima facie obvious to modify the method of Irfan to produce the PD-1 antibody of Papadopoulos, et al. because the PD-1 antibody of Papadopoulos, et al. is useful in treating diseases such as cancer, viral infections, and autoimmune disorders. One would have a reasonable expectation of success that producing the PD-1 antibodies of Papadopoulos, et al. via the method of Irfan et al, specifically at a pCO2 level of 140 mmHg would similarly yield the lowered level of acidic variants as demonstrated by Irfan et al. Furthermore, would have a reasonable expectation of successfully producing the PD-1 antibodies via the method of Irfan et al because Papadopoulos, et al. teaches PD-1 antibodies can be produced using CHO cells.
Claims 1, 4-5, 7-9, 10-14, 16, 20, 28-31, and 39-42 are rejected under 35 U.S.C. 103 as being unpatentable over Irfan (New Castle University, 2017) in view of Xu (Biotechnol. Prog., 2017) and Martin et al (US20090074793A1).
The teachings of Irfan, Xu, and Martin are set forth above.
Irfan and Xu render claims 1, 4-5, 8-9, 11-14, 20, 28-29, and 31 obvious.
Regarding claims 7, 16, 39-42: Following the discussion of claims 1, 5, 13-14, and 20 above, Irfan teaches using CHO cells to produce humanized IgG1 monoclonal HER2 antibodies. The antibodies are produced under increasing pCO2 conditions, including 140 mmHg, leading to a decrease in acidic variants. The increase in pCO2 results in ~63% main target antibody, ~ 22% acidic charge variants, and ~ 15% basic charge variants (See Fig2.4). This is a desirable effect because charge variants can have an effect on an antibody’s stability, effect, and safety.
Irfan does not teach antibodies capable of binding IL-4 receptors or using CO2 sparging to attain pCO2 conditions.
Xu et al teaches CO2 sparging can be used to increase pCO2 conditions during antibody production by CHO cells.
It would have been prima facie obvious to use the CO2 sparging taught by CHO in the method of Irfan to increase pCO2 levels. See rejection of claim 1 above.
Martin, et al. teaches an IL-4R antibody which reads on dupilumab (See rejection of claims 43-45 above).
Martin further teaches, the antibodies can be full-length for example, an IgG1 or IgG4 antibody, may comprise only an antigen binding portion, and may be modified to effect functionality and can be produced using CHO cell lines (See pg. 1, ¶0006 and pg. 7, ¶0064). The Il-4R antibodies can be used to treat diseases or disorders which are improved, inhibited or ameliorated by reducing IL-4 activity such as arthritis, herpetiformis, chronic idiopathic urticaria, scleroderma, hypertrophic scarring, Whipple’s Disease, etc. (See pg. 7, ¶0060).
Given that Irfan and Martin, et al. both teach using CHO cells to produce human monoclonal antibodies, it would have been prima facie obvious to modify the method of Irfan to produce the Il-4R antibody of Martin et al. because the Il-4R antibody of Martin, et al. is useful in treating diseases or disorders which are improved, inhibited or ameliorated by reducing IL-4 activity. One would have a reasonable expectation of success that producing the IL-4R antibodies of Martin, specifically the dupilumab antibodies, via the method of Irfan et al, specifically at a pCO2 level of 140 mmHg would similarly yield the lowered level of acidic variants as demonstrated by Irfan et al.
Regarding claims 10, and 30: Following the discussion of claims 1, 5, 8, 9, 20, and 28 above, Irfan teaches using CHO cells to produce human monoclonal IgG1 antibodies.
Irfan does not teach the antibodies are IgG4 antibodies.
The teachings of Martin, et al. are set forth above.
Martin, et al. discloses human monoclonal Il-4R antibodies which can be full length IgG1 or IgG4 (reads on the antibodies are IgG4) antibodies and can be produced by CHO cells. Martin, et al. further discloses that during antibody production, mouse constant regions can be replaced with desired human constant regions (reads on antibody isotype) to generate… IgG4 or IgG1 antibodies and that constant regions selected may vary according to specific use (See pg. 6 ¶0048).
Irfan and Martin, et al. both teach using CHO cells to produce monoclonal IgG antibodies and that using CHO cells for antibody production is a known method in the field. Martin, et al. further teaches that CHO cells can specifically produce monoclonal Il-4R antibodies with an IgG4 isotype. It would have been prima facie obvious to modify the method of Irfan to produce the Il-4R antibody with an IgG4 isotype of Martin, et al because the Il-4R antibody of Martin, et al. is useful in treating diseases or disorders which are improved, inhibited or ameliorated by reducing IL-4 activity. One would have a reasonable expectation of success that producing the IL-4R antibodies of Martin via the method of Irfan et al, specifically at a pCO2 level of 140 mmHg would similarly yield the lowered level of acidic variants as demonstrated by Irfan et al. Furthermore, one would have a reasonable expectation of successfully producing the IgG4 antibodies via the method of Irfan et al because Martin teaches IL-4R IgG4 antibodies can be produced using CHO cells.
Conclusion
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 MARISOL A O'NEILL whose telephone number is (571)272-2490. The examiner can normally be reached Monday - Friday 7:30 - 5:00 EST.
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, Christopher Babic can be reached at (571) 272-8507. 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.
/MARISOL ANN O'NEILL/Examiner, Art Unit 1633
/ALLISON M FOX/Primary Examiner, Art Unit 1633