Prosecution Insights
Last updated: April 19, 2026
Application No. 16/328,061

A Novel Method for Stabilization of a Biopharmaceutical Drug Product During Processing

Non-Final OA §103§112§DP
Filed
Feb 25, 2019
Examiner
REYNOLDS, FRED H
Art Unit
1658
Tech Center
1600 — Biotechnology & Organic Chemistry
Assignee
Leukocare AG
OA Round
10 (Non-Final)
33%
Grant Probability
At Risk
10-11
OA Rounds
2y 10m
To Grant
72%
With Interview

Examiner Intelligence

Grants only 33% of cases
33%
Career Allow Rate
269 granted / 815 resolved
-27.0% vs TC avg
Strong +40% interview lift
Without
With
+39.5%
Interview Lift
resolved cases with interview
Typical timeline
2y 10m
Avg Prosecution
104 currently pending
Career history
919
Total Applications
across all art units

Statute-Specific Performance

§101
3.9%
-36.1% vs TC avg
§103
33.3%
-6.7% vs TC avg
§102
13.2%
-26.8% vs TC avg
§112
26.5%
-13.5% vs TC avg
Black line = Tech Center average estimate • Based on career data from 815 resolved cases

Office Action

§103 §112 §DP
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 . 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. 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and the fee set forth in 37 CFR 1.17(e) has been timely paid, the finality of the previous Office action has been withdrawn pursuant to 37 CFR 1.114.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 7 July, 2025 has been entered. Election/Restrictions Applicants elected group I (purification and filling of an antibody in a formulation with glycine, histidine, methionine, and trehalose) with traverse in the reply filed on 8 April, 2020. The traversal was found unpersuasive, and the election/restriction requirement made final in the office action of 1 May, 2020. Applicants have since amended the claims so they no longer read on the method elected. Claims Status Claims 1-16, 18, 20, and 21 are pending. Claim 1 has been amended. Claims 2-10, 12-16, 18, 20, and 21 have been withdrawn due to an election/restriction requirement. Maintained Objections Specification The disclosure is objected to because of the following informalities: Applicants have listed the ingredients in the formulation of Herceptin, as supplied by the manufacturer, as trehalose, histidine buffer, methionine, polysorbate 20, and recombinant human hyaluronidase at pH 5 (example 9, p80, example 10, p82). This is not correct. According to the package insert, Herceptin is sold as a two vial formulation. The first vial contains 440 mg of the antibody, 400 mg trehalose, 9.9 mg histidine HCl, 6.4 mg histidine, and 1.8 mg polysorbate 20 (Herceptin, package insert, 2010 revision, section 11, p20, 7th paragraph). The second vial contains 20 mL of water containing 1.1% benzyl alcohol (section 2.3, p3, 9th paragraph). Upon mixing the two vials, the solution is 21 mg/mL antibody at about pH 6 (section 11, p20, 7th paragraph). Note that the concentrations are different than applicants have stated, and there is no methionine or hyaluronidase. Appropriate correction is required. response to applicant’s arguments Applicants state that they will amend this part of the specification to change Herceptin to Herceptin Hylecta®. Applicant's arguments filed 7 July, 2025 have been fully considered but they are not persuasive. The specification has not been amended. Applicants have stated that they will amend the specification, but until the amendment is made, it is merely theoretical. Please note that an amendment must state where support for the amendment lies. If there is no support, then the amendment will be new matter, and objected to. Withdrawn Rejections The rejection of claims 1 and 11 under 35 U.S.C. 103 as being unpatentable over Vazquez-Rey et al (Biotechnol. Bioeng. (2011) 108 p1494-1508, previously cited) in view of Ball (Chemistry World (2009) p58-62, previously cited), Chen et al (Biosci. Biotechnol. Biochem. (2016, available 2 June) 80(10) p1874-1878, previously cited), Arakawa et al (J. Biophys. Soc. (1985) 47 p411-414), Reeg et al (Antiox. Redox Sig. (2015) 23(3) p239-255, previously cited), Hada et al (Int. J. Biol. Macromol. (2016) 82 p192-200, available online Oct, 2015, previously cited), and Nayak et al (J. Compl. Integr. Med. (2015) 13(2) p129-136) is hereby withdrawn due to amendment. The provisional rejection of claims 1 and 11 on the ground of nonstatutory double patenting as being unpatentable over claims 1 and 11 of copending Application No. 18/057,627 is hereby withdrawn due to the abandonment of the competing application. Maintained/Modified Rejections 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 and 11 are provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1 and 10 of copending Application No. 18/591,399 (reference application). Although the claims at issue are not identical, they are not patentably distinct from each other because the competing claims render obvious the instant claims. Competing claim 1 is very similar to examined claim 1, save that it specifies the amino acids as a positively charged amino acid, an anti-oxidant amino acid, and an amino acid with an osmolytic function. The number of amino acids that fit these definitions are limited, rendering at least one of the claimed compositions obvious. Competing claim 10 requires that the biopharmaceutical be an antibody, which reads on examined claim 11. While none of the competing claims specify the viscosity, as it’s the same formulation, it will inherently have the same viscosity. This is a provisional nonstatutory double patenting rejection because the patentably indistinct claims have not in fact been patented. response to applicant’s arguments Applicants request that this rejection be held in abeyance until the application is otherwise in condition for allowance. However, until this rejection is overcome, it will remain valid. New Rejections Claim Rejections - 35 USC § 112(b) The following is a quotation of 35 U.S.C. 112(b): (b) CONCLUSION.—The specification shall conclude with one or more claims particularly pointing out and distinctly claiming the subject matter which the inventor or a joint inventor regards as the invention. The following is a quotation of 35 U.S.C. 112 (pre-AIA ), second paragraph: The specification shall conclude with one or more claims particularly pointing out and distinctly claiming the subject matter which the applicant regards as his invention. Claims 1 and 11 are rejected under 35 U.S.C. 112(b) or 35 U.S.C. 112 (pre-AIA ), second paragraph, as being indefinite for failing to particularly point out and distinctly claim the subject matter which the inventor or a joint inventor (or for applications subject to pre-AIA 35 U.S.C. 112, the applicant), regards as the invention. Claim 1, and claims that depend on it, have a limitation that the processing step is carried out “in the presence of a composition having a viscosity of below 10 mPa*s.” There are two issues with this limitation. First, it is not clear if the conditions under which the viscosity is measured are the same as the process is run or under some standard set of conditions. It has long been known that viscosity is a function of temperature (Misra et al, J. Chem. Eng. Data (1961) 6(2) p194-196, title). Thus, the conditions under which the test is run will affect the viscosity. Second, and related, many of the steps involve temperature changes. Re-buffering will involve a change in temperature unless the enthalpy of dissolution is zero. Freezing and thawing inherently involve changes in temperature, and chunks of frozen material will affect the viscosity (Reynolds et al (Anal. Chem. (2005) 77 p814-817, p815, 2nd column, 3d paragraph)). This means that, even if we restrict the viscosity measurement to the conditions used in the processing operation, there will be differences depending on when the viscosity is measured during the process. Claim Rejections - 35 USC § 103 The following is a quotation of 35 U.S.C. 103 which forms the basis for all obviousness rejections set forth in this Office action: A patent for a claimed invention may not be obtained, notwithstanding that the claimed invention is not identically disclosed as set forth in section 102, if the differences between the claimed invention and the prior art are such that the claimed invention as a whole would have been obvious before the effective filing date of the claimed invention to a person having ordinary skill in the art to which the claimed invention pertains. Patentability shall not be negated by the manner in which the invention was made. The factual inquiries set forth in Graham v. John Deere Co., 383 U.S. 1, 148 USPQ 459 (1966), that are applied for establishing a background for determining obviousness under 35 U.S.C. 103 are summarized as follows: 1. Determining the scope and contents of the prior art. 2. Ascertaining the differences between the prior art and the claims at issue. 3. Resolving the level of ordinary skill in the pertinent art. 4. Considering objective evidence present in the application indicating obviousness or nonobviousness. This application currently names joint inventors. In considering patentability of the claims the examiner presumes that the subject matter of the various claims was commonly owned as of the effective filing date of the claimed invention(s) absent any evidence to the contrary. Applicant is advised of the obligation under 37 CFR 1.56 to point out the inventor and effective filing dates of each claim that was not commonly owned as of the effective filing date of the later invention in order for the examiner to consider the applicability of 35 U.S.C. 102(b)(2)(C) for any potential 35 U.S.C. 102(a)(2) prior art against the later invention. Claims 1 and 11 are rejected under 35 U.S.C. 103 as being unpatentable over Vazquez-Rey et al (Biotechnol. Bioeng. (2011) 108 p1494-1508, previously cited) in view of Ball (Chemistry World (2009) p58-62, previously cited), Chen et al (Biosci. Biotechnol. Biochem. (2016, available 2 June) 80(10) p1874-1878, previously cited), Arakawa et al (J. Biophys. Soc. (1985) 47 p411-414), Reeg et al (Antiox. Redox Sig. (2015) 23(3) p239-255, previously cited), Hada et al (Int. J. Biol. Macromol. (2016) 82 p192-200, available online Oct, 2015, previously cited), Nayak et al (J. Compl. Integr. Med. (2015) 13(2) p129-136), Chang et al (US 20140127227), and Reynolds et al (Anal. Chem. (2005) 77 p814-817). Claims 1 and 11 discuss a method of producing a drug product. Vazquez-Rey et al discuss aggregation in monoclonal antibody manufacturing (title). These aggregates can affect the potency of a formulation (p1496, 2nd column, 4th paragraph), and can have negative biological effects (p1496, 2nd column, 5th paragraph). The aggregates can form during cell culture (p1497, 2nd column, 4th paragraph), purification (p1498, 1st column, 4th paragraph), mixing (p1499, 1st column, 2nd paragraph), buffering (p1499, 1st column, 7th paragraph), due to equipment contact (p1500, 1st column, 1st paragraph), fluids handling (p1500, 2nd column, 2nd paragraph), ultrafiltration for concentration (p1500, 1st column, 3d paragraph), filling (p1501, 1st column, 2nd paragraph), and storage (p1501, 1st column, 6th paragraph). In other words, aggregation of monoclonal antibodies can form at any and all steps in the manufacturing process. This is dealt with by optimizing the manufacturing process, removal of aggregates during downstream processing, and selection of appropriate buffers (p1502, 2nd column, 1st paragraph). The difference between this reference and the instant claims is that this reference doesn’t teach the buffer used by applicants, or the viscosity. Ball discusses protein denaturing (title). A denatured protein can, in principle, find its way back to its folded conformation by thermal fluctuations, but the exposed hydrophobic groups tend stick together and cause aggregation, which is more or less irreversible (p59, 1st column, 3d paragraph). This reference teaches that denaturing is a step before aggregation in the aggregation of polypeptides. This implies that preventing denaturization will prevent (or at least reduce) aggregation. Chen et al discusses an assay system for protein stabilization (title). Protein stabilizers enhance the stability of proteins and prevent denaturation (p1874, 1st column, 1st paragraph), which, as implied by Ball, will reduce aggregation. Trehalose is among the best known protein stabilizers, but amino acids such as histidine are also known in the art for this purpose (p1874, 1st column, 1st paragraph). The effect of combining different stabilization reagents is not clear, with some combinations proving synergistic, while others are merely cooperative (p1874, 1st column, 1st paragraph, continues to 2nd column). This reference teaches trehalose, glycine, and betaine as stabilizing excipients. Arakawa et al discuss stabilization of proteins by osmolytes (title). Among the compounds tested is Ala and β-Ala, both which protect against thermal denaturing (abstract). This reference discusses Ala as a stabilizing excipient in protein formulation. Reeg et al discuss protein oxidation (title). Oxidation of proteins leads to partial unfolding, and therefore, to aggregation (abstract). This reference teaches that oxidation induces aggregation, implying that preventing oxidation will help prevent aggregation. Hada et al examine various antioxidants in protein formulation (title). Oxidation of protein formulations should be minimized by adequate processes with stable formulations (p192, 2nd column, 2nd paragraph). Using a model protein, three common antioxidants were tested for their ability to prevent oxidative damage (p193, 1st column, 3d paragraph). Of the three antioxidants tested, methionine was the most efficient in suppressing oxidation (p199, 2nd column, 2nd paragraph). Nayak et al discusses the antioxidant properties of tryptophan (title). Tryptophan had a very high oxygen radical absorption capacity compared to controls (abstract). This reference teaches tryptophan is a powerful antioxidant. Chang et al discusses protein formulations with amino acids (title). While this will increase stability, as noted by other references cited in this rejection, it will also decrease viscosity (paragraph 10). This approach is effective for antibodies (paragraph 20). Viscosity can be reduced to below 20 mpas (paragraph 122). This reference shows that the amino acids used to improve stability will also reduce viscosity. Reynolds et al uses viscosity to determine parameters of particles, including proteins (abstract). Even at a concentration of 10% (w/v), bovine IgG has a viscosity that is less than 3x PBS (fig 3b, p816, 1st column, 3d paragraph). This reference shows that, even at fairly high concentrations, the viscosity of an immunoglobulin, even without viscosity modifiers, is well below 20 mpas. Therefore, it would be obvious to add the various amino acids of the cited references to the preparations of Vazquez-Rey et al at each step of the process to stabilize the material and reduce aggregation. As these compounds are known in the art for protein stabilization, an artisan in this field would attempt this modification with a reasonable expectation of success. Vazquez-Rey et al discuss aggregation at concentration and filling steps. Chen et al renders obvious the addition of trehalose and histidine to these formulations to reduce denaturing which leads to aggregation, as discussed by Ball. Arakawa et al teach that alanine can reduce thermal denaturing. Hada et al show that methionine is an effective antioxidiant, which, as suggested by Reeg et al, should also reduce denaturing and aggregation. Nayak et al teaches that tryptophan is also a powerful antioxidant, making it obvious to add that amino acid. While none of the references discuss the ratio of amino acids to sugar, finding the optimum ratio for stability is considered merely optimization. The MPEP states that “Where the general conditions of a claim are disclosed in the prior art, it is not inventive to discover the optimum or working ranges by routine experimentation" In re Aller, 220 F.2d 454, 456, 105 USPQ 233, 235 (CCPA 1955); see also Peterson, 315 F.3d at 1330, 65 USPQ2d at 1382 (“The normal desire of scientists or artisans to improve upon what is already generally known provides the motivation to determine where in a disclosed set of percentage ranges is the optimum combination of percentages.”) (MPEP2144.05.II). Furthermore, none of the cited references discuss glutamic acid, aspartic acid, or analogs of those amino acids as stabilizers. Reynolds et al shows that immunoglobulins, even at fairly high concentrations, will have a viscosity of less than 20 mpas, and Chang states that the amino acids added to improve stability will reduce viscosity, and explicitly state viscosities of less than 20 mpas. Thus, the combination of references renders obvious claim 1. The compounds of Vazquez-Rey et al are antibodies, a protein, rendering obvious claim 11. Conclusion Any inquiry concerning this communication or earlier communications from the examiner should be directed to FRED REYNOLDS whose telephone number is (571)270-7214. The examiner can normally be reached M-Th 9-3:30. Examiner interviews are available via telephone 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, Melissa Fisher can be reached at 571-270-7430. 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. /FRED H REYNOLDS/Primary Examiner, Art Unit 1658
Read full office action

Prosecution Timeline

Feb 25, 2019
Application Filed
Feb 25, 2019
Response after Non-Final Action
Jun 07, 2019
Response after Non-Final Action
Apr 28, 2020
Non-Final Rejection — §103, §112, §DP
Aug 27, 2020
Response Filed
Sep 15, 2020
Final Rejection — §103, §112, §DP
Feb 19, 2021
Request for Continued Examination
Feb 22, 2021
Response after Non-Final Action
Apr 26, 2021
Non-Final Rejection — §103, §112, §DP
Aug 26, 2021
Response Filed
Sep 13, 2021
Final Rejection — §103, §112, §DP
Mar 14, 2022
Request for Continued Examination
Mar 16, 2022
Response after Non-Final Action
Jun 21, 2022
Non-Final Rejection — §103, §112, §DP
Oct 26, 2022
Response Filed
Nov 21, 2022
Final Rejection — §103, §112, §DP
May 25, 2023
Request for Continued Examination
May 31, 2023
Response after Non-Final Action
Nov 27, 2023
Final Rejection — §103, §112, §DP
Mar 28, 2024
Request for Continued Examination
Apr 01, 2024
Response after Non-Final Action
Jun 03, 2024
Non-Final Rejection — §103, §112, §DP
Nov 27, 2024
Response Filed
Jan 02, 2025
Final Rejection — §103, §112, §DP
Jul 07, 2025
Request for Continued Examination
Jul 09, 2025
Response after Non-Final Action
Oct 20, 2025
Non-Final Rejection — §103, §112, §DP (current)

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Study what changed to get past this examiner. Based on 5 most recent grants.

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Prosecution Projections

10-11
Expected OA Rounds
33%
Grant Probability
72%
With Interview (+39.5%)
2y 10m
Median Time to Grant
High
PTA Risk
Based on 815 resolved cases by this examiner. Grant probability derived from career allow rate.

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