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 .
Status of Application, Amendments and/or Claims
The amendment and Applicant’s arguments, filed 01 May 2026, have been entered in full. Claims 47, 54-57 are withdrawn from consideration as being drawn to a non-elected invention. Claims 12, 13, 24, 26, 29, 45 and 46 are canceled. Claims 1, 14-19, 25, 27, 30-35, 42, 49-53 are amended. Claims 1-11, 14-23, 25, 27, 28, 30-44, 48-53 are under examination.
Information Disclosure Statement
The information disclosure statement(s) (IDS), filed 01 May 2026, was received and complies with the provisions of 37 CFR §§1.97, 1.98 and MPEP § 609. It has been placed in the application file and the information referred to therein has been considered as to the merits.
Withdrawn Objections And/Or Rejections
The duplicate claim warning, as set forth at pages 3-4 of the previous Office Action (01 December 2025), is withdrawn in view of the amendment (01 May 2026).
The objection to claims 1, 29, 49, 50 and 52, as set forth at pages 4-5 of the previous Office Action (01 December 2025), is withdrawn in view of the amendment (01 May 2026).
The rejection to claims 27 and 49-53 under 35 U.S.C. 112(b) or 35 U.S.C. 112 (pre- AIA ), second paragraph, as set forth at pages 5-6 of the previous Office Action (01 December 2025), is withdrawn in view of the amendment (01 May 2026).
The rejection to claims 13, 25, 26 and 29 under 35 U.S.C. 112(d) or pre-AIA 35 U.S.C. 112, 4th paragraph, as set forth at pages 7-8 of the previous Office Action (01 December 2025), is withdrawn in view of the amendment (01 May 2026).
The rejection to claims 1, 3, 13, 15, 25, 26, 29, 31, 45, 48, 49 and 52 under 35 U.S.C. 102(a1) and 35 U.S.C. 102(a2) as being anticipated by Bergquist et al. (US 2010/0151518; published June 17, 2010), as set forth at pages 8-9 of the previous Office Action (01 December 2025), is withdrawn in view of the amendment (01 May 2026).
The rejection to claims 1-3, 8-15, 20-31, 36, 39-44, 48-53 under 35 U.S.C. 102(a1) and 35 U.S.C. 102(a2) as being anticipated by Lee et al. (US 2016/0264618; published Sep 15, 2016), as set forth at pages 9-10 of the previous Office Action (01 December 2025), is withdrawn in view of the amendment (01 May 2026).
The rejection to claims 1, 3, 13-18, 20-26, 29, 31, 45, 46, 48, 49 and 52 under 35 U.S.C. 103 as being unpatentable over Bergquist et al. (US 2010/0151518; published June 17, 2010) in view of Wang et al. (US 2019/0046956; published Feb 14, 2019, priority date June 21, 2017), as set forth at pages 11-14 of the previous Office Action (01 December 2025), is withdrawn in view of the amendment (01 May 2026).
Claim Rejections - 35 USC § 103
In the event the determination of the status of the application as subject to AIA 35 U.S.C. 102 and 103 (or as subject to pre-AIA 35 U.S.C. 102 and 103) is incorrect, any correction of the statutory basis (i.e., changing from AIA to pre-AIA ) for the rejection will not be considered a new ground of rejection if the prior art relied upon, and the rationale supporting the rejection, would be the same under either status.
The following is a quotation of 35 U.S.C. 103 which forms the basis for all obviousness rejections set forth in this Office action:
A patent for a claimed invention may not be obtained, notwithstanding that the claimed invention is not identically disclosed as set forth in section 102, if the differences between the claimed invention and the prior art are such that the claimed invention as a whole would have been obvious before the effective filing date of the claimed invention to a person having ordinary skill in the art to which the claimed invention pertains. Patentability shall not be negated by the manner in which the invention was made.
The factual inquiries for establishing a background for determining obviousness under 35 U.S.C. 103 are summarized as follows:
1. Determining the scope and contents of the prior art.
2. Ascertaining the differences between the prior art and the claims at issue.
3. Resolving the level of ordinary skill in the pertinent art.
4. Considering objective evidence present in the application indicating obviousness or nonobviousness.
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 1-11, 14-23, 25, 27, 28, 30-44, 48-53 remain rejected under 35 U.S.C. 103 as being unpatentable over Lee et al. (US 2016/0264618; published Sep 15, 2016). The basis for this rejection is set forth at pages 14-16 of the previous Office Action. The Examiner notes an inadvertent typo which left out claims 36 and 37.
APPLICANT’S ARGUMENTS: Applicant argues that amended claim 1 recites "a method of purifying a bispecific antibody" comprising "equilibrating a cation exchange chromatography medium with an equilibration buffer comprising 94-105 mM sodium chloride" and "loading the composition comprising the bispecific antibody on to the cation exchange chromatography medium in a load buffer comprising 94-105 mM sodium chloride."
Applicant argues that the Office Action alleges that Lee's statement "[t]he recognized antibody genes include the different constant region genes as well as the myriad antibody variable region genes" is evidence of a multispecific protein (citing Lee at [paragraph 0052]). Applicant argues that the cited portions merely state that antibodies include "variable region genes" and is silent regarding whether the variable regions bind with different antigens or epitopes. Applicant states that in contrast, as explained in the Instant Application, a bispecific antibody is a multispecific protein that "bind[s] two antigens (instant specification at paragraphs [0051]-[0052]).
Applicant argues that Lee does not disclose a "bispecific antibody," let alone a method of "purifying a bispecific antibody" as recited in the claims and that the Examples of Lee relate to separation of "Anti-EGFR Monoclonal Antibody Isoforms" and "Anti-CD20 Monoclonal Antibody Isoforms" by cation exchange chromatography. See Lee at [0068]-[0128].
Applicant argues that Lee provides no motivation to modify its teachings to arrive at the claimed method. Applicant submits that in the Examples of Lee, a monoclonal antibody was eluted from a protein A column "under acidic conditions (50 mM sodium acetate, 60 mM sodium chloride buffer, pH 3.5±0.05)" and "diluted with water to adjust the conductivity to 2 mS/cm or less" [para 0067]. Lee explains that this material is 'adjusted protein A eluate' prepared for loading onto a cation exchange chromatography column" [para 0067]. This "protein A eluate adjusted by the method of Example 1 was loaded onto weak cation exchange chromatography resin" equilibrated with an equilibration solution of "20 mM Na Acetate, pH 5.0 buffer." Lee at [0069], [0073]; see also Lee at [0085] [0089], [0100], [0104], [0115], [0119].
Applicant argues that in Lee, a protein A eluate of 60 mM sodium chloride is further diluted before loading onto a cation exchange chromatography column, and the column is equilibrated with an acetate buffer. Applicant argues that Lee provides no motivation to increase the sodium chloride concentration of the load buffer or to add sodium chloride to the equilibrium buffer to arrive at the claimed method. Applicant submits that Lee states that "[t]he antibody-containing sample in step a) may be adjusted to a conductivity of 10 mS/cm or lower before loading " [para 0030]. Applicant argues that Lee instead teaches to reduce the salt content of the load buffer.
Applicant argues that there is no reasonable expectation of success in modifying Lee to arrive at the claimed method. Applicant states that purification of multispecific proteins, including bispecific antibodies, "is complicated by the formation of product-related variants, such as homodimers, half-antibodies, aggregates, high and low molecular weight species and the like" that "share similar structural and physical properties, such as charge, with the multispecific protein of interest, making them difficult to separate from during purification." Applicant argues that Lee does not disclose methods that address the problem of product-related impurities that complicate purification of bispecific antibodies as the claimed methods do. Applicant submits that Lee discloses separation of 'Anti-EGFR Monoclonal Antibody Isoforms" and "Anti-CD20 Monoclonal Antibody Isoforms" by cation exchange chromatography. Applicant maintains that purification of monoclonal antibodies would not involve the same complications as purification of a bispecific antibody. Applicant submits that the "isoforms" separated in Lee are described as "proteins having forms slightly different from the desired form due to post-transcriptional modification, post-translational modification and cellular differences, among the same types of proteins expressed from the same gene” , rather than the product-related variants such as "homodimers, half-antibodies, aggregates, high and low molecular weight species" that complicate purification of bispecific antibodies (Instant Application at [0006]).
Applicant maintains that a person of ordinary skill in the art would not have been motivated or had a reasonable expectation of success in modifying the teachings of Lee to arrive at the claimed method.
Applicant’s argument have been fully considered but are not found persuasive for the following reasons:
1. Applicant directs the Examiner’s attention to the instant specification at paragraphs [0052-0053], which teaches:
[0052] The most common and most diverse of the multispecific proteins are those that bind two antigens, referred to interchangeably herein as “bispecific”, “bispecific proteins” and “bispecific antibody”.
[0053] “The formats for bispecific proteins, which include bispecific antibodies, are constantly evolving and include, but are not limited to, quadromas, knobs-in-holes, cross-Mabs, dual variable domains IgG (DVD-IgG), IgG-single chain Fv (scFv), scFv-CH3 KIH, dual action Fab (DAF), half-molecule exchange, κλ-bodies, tandem scFv, scFv-Fc, diabodies, single chain diabodies (scDiabodies), scDiabodies-CH3, triple body, miniantibody, minibody, TriBi minibody, tandem diabodies, scDiabody-HAS, Tandem scFv-toxin, dual-affinity retargeting molecules (DARTs), nanobody, nanobody-HSA, dock and lock (DNL), strand exchange engineered domain SEEDbody, Triomab, leucine zipper (LUZ-Y), XmAb®; Fab-arm exchange, DutaMab, DT-IgG, charged pair, Fcab, orthogonal Fab, IgG(H)-scFv, scFV-(H)IgG, IgG(L)-scFV, IgG(L1H1)-Fv, IgG(H)-V, V(H)-IgG, IgG(L)-V V(L)-IgG, KIH IgG-scFab, 2scFV-IgG, IgG-2scFv, scFv4-Ig, Zybody, DVI-Ig4 (four-in-one), Fab-scFv, scFv-CH-CL-scFV, F(ab′)2-scFv2, scFv-KIH, Fab-scFv-Fc, tetravalent HCAb, scDiabody-Fc, diabody-Fc, intrabody, ImmTAC, HSABody, IgG-IgG, Cov-X-Body, scFv1-PEG-scFv2, single chain bispecific antibody constructs, single chain bispecific T cell engagers (BITE), bi-specific T cell engagers, and half-life extended bispecific T cell engagers (HLE BITE)”.
The Examiner notes that the instant specification defines “bispecific proteins” and “bispecific antibody” as referred to interchangeably and binds two antigens.
2. The Examples from the instant specification teach a human bi-specific, engineered immunoglobulin. The Examples employ this “bi-specific” in the purification method in Examples 1 and 2 (see para 0107, Bi-specific #1). It is noted that there is no teaching of the structure of Bi-specific #1 or teachings of the two antigens that Bi-specific #1 binds.
The Examples from the instant specification teach an engineered IgG/Fab fusion protein as a bi-specific. The Examples employ this “bi-specific” in the purification methods in Examples 3-5 (see para 0013, Bi-specific #2). It is noted that the instant specification considers the IgG/Fab fusion protein (Bi-specific # 2) as a bispecific antibody. It is noted that there is no teaching of the structure of Bi-specific #2 or teachings of the two antigens that Bi-specific #2 binds.
Thus, the instant specification defines “bispecific proteins” and “bispecific antibody” as encompassing various formats (i.e., IgG/Fab fusion protein).
3. Regarding Applicant’s arguments that Lee does not suggest "a bispecific antibody," let alone the claimed method of "purifying a bispecific antibody”:
Lee et al. teach the use of cation exchange chromatography for the purification of a protein of interest, such as an antibody (see abstract).
Lee teaches the following:
[0041] In an embodiment of the present invention, the antibody may be anti-EGFR (epidermal growth factor receptor) antibody, anti-CD20 antibody, anti-HER2 antibody, anti-TNFα antibody, anti-VEGF (vascular endothelial growth factor) antibody, anti-influenza A virus antibody, anti-RSV (Respiratory Syncytial Virus) antibody, anti-HBV (Hepatitis B Virus) antibody, anti-rabies virus antibody, but is not limited thereto. In other words, the present invention may generally be carried out using immunoglobulins.
[0052] The terms “antibody” and “immunoglobulin”, which may interchangeably be used herein, generally include at least two light-chain polypeptides and two heavy-chain polypeptides. Each of the heavy-chain and light-chain polypeptides contains a variable region (generally the amino terminal portion of the polypeptide chain) which contains a binding region that is able to interact with an antigen. In addition, each of the heavy-chain and light-chain polypeptides includes a constant region (generally the carboxyl terminal portion) which may mediate the binding of the antibody to host tissue or factors including various cells of the immune system, some phagocytic cells and a first component (Clq) of the classical complement system. As used herein, the term “antibody” or “immunoglobulin” refers to a protein consisting of one or more polypeptides substantially encoded by antibody genes. The recognized antibody genes include the different constant region genes as well as the myriad antibody variable region genes. Antibodies may exist in a variety of forms, including, for example, Fv, Fab, and F(ab).sub.2 as well as single chains. For example, antibodies according to an embodiment of the present invention include monoclonal antibodies and fragments thereof, for example, isolated heavy or light chains, or heavy or light chains consisting only of constant regions, as well fragments thereof.
The limitation “at least two”, as taught by Lee et al., means 2 or more. Lee et al. teach that the term antibody includes an antibody with more than two light chain polypeptides and more than two heavy chain polypeptides, which encompasses a bispecific antibody.
Lee teaches binding through the variable region AND through the constant region. This would enable the antibody to bind to two different antigens.
The Lee reference includes “bispecific antibodies” as defined by the instant specification’s teachings at paras [0052-0053].
4. Regarding Applicant’s arguments that the Examples of Lee relate to separation of "Anti- EGFR Monoclonal Antibody Isoforms" and "Anti-CD20 Monoclonal Antibody Isoforms" by cation exchange chromatography and not a method of purifying a bispecific antibody as claimed.
MPEP 2123 teaches: disclosed examples and preferred embodiments do not constitute a teaching away from a broader disclosure or non-preferred embodiments (In re Susi, 440 F.2d 442, 169 USPQ 423 (CCPA 1971).
The Examiner has discussed how the Lee reference includes bispecific antibodies.
5. Regarding Applicant’s arguments that Lee provides no motivation to modify its teachings to arrive at the claimed method; that in the Lee reference, a protein A eluate of 60 mM sodium chloride is further diluted before loading onto a cation exchange chromatography column and the column is equilibrated with an acetate buffer and that Lee provides no motivation to increase the sodium chloride concentration of the load buffer or to add sodium chloride to the equilibrium buffer to arrive at the claimed method:
As was stated in the previous Office Action, Lee et al. teach the use of cation exchange chromatography for the purification of a protein of interest, such as an antibody. Lee et al. teach equilibrium buffers. Lee et al. teach the equilibrium buffer has a salt concentration of 10-300 mM or maybe 100 mM or less. Lee et al. teach the equilibrium buffer can comprise any one selected from the group consisting of sodium acetate and sodium chloride. Lee et al. teach wash buffers. Lee et al. teach the wash buffer has a salt concentration of 10-300 mM or maybe 100 mM or less. Lee et al. teach the wash buffer can comprise any one selected from the group consisting of sodium acetate and sodium chloride. Lee et al. teach more than one wash. Lee et al. teach that the pH and salt concentration conditions of the washing buffer are applied to the loading conditions of the cation exchange chromatography column (disclosed examples and preferred embodiments do not constitute a teaching away from a broader disclosure or non-preferred embodiments; In re Susi, 440 F.2d 442, 169 USPQ 423 CCPA 1971).
The Examiner notes that in Example 2 from the instant specification, Bi-specific #1 was combined with a load buffer (100 mM acetate, 350 mM sodium chloride) at a ratio of 1:0.378, giving a load concentration of 96 mM sodium chloride. Thus, there is a teaching to reduce the salt content of the load buffer (just like Lee et al).
The Examiner also notes that in the Examples from the instant specification, the cation exchange chromatography resin is pre-equilibrated with 1.75 M sodium chloride, which equals 1750 mM sodium chloride. This makes the salt content over 17 times higher than that used to equilibrate the cation exchange chromatography resin (i.e. 100 mM sodium chloride). This would be another teaching to reduce the salt content.
6. Regarding Applicant’s arguments that there is no reasonable expectation of success in modifying Lee to arrive at the claimed method; that purification of bispecific antibodies, "is complicated by the formation of product-related variants, such as homodimers, half-antibodies, aggregates, high and low molecular weight species and the like that share similar structural and physical properties, such as charge, with the multispecific protein of interest, making them difficult to separate from during purification” and that Lee discloses separation of isoforms, does not disclose methods that address the problem of product-related impurities that complicate purification of bispecific antibodies and that purification of monoclonal antibodies would not involve the same complications as purification of a bispecific antibody:
MPEP 2144 IV teaches: The reason or motivation to modify the reference may often suggest what the inventor has done, but for a different purpose or to solve a different problem. It is not necessary that the prior art suggest the combination to achieve the same advantage or result discovered by applicant. See, e.g., In re Kahn, 441 F.3d 977, 987, 78 USPQ2d 1329, 1336 (Fed. Cir. 2006) (motivation question arises in the context of the general problem confronting the inventor rather than the specific problem solved by the invention); Cross Med. Prods., Inc. v. Medtronic Sofamor Danek, Inc., 424 F.3d 1293, 1323, 76 USPQ2d 1662, 1685 (Fed. Cir. 2005) ("One of ordinary skill in the art need not see the identical problem addressed in a prior art reference to be motivated to apply its teachings."); In re Linter, 458 F.2d 1013, 173 USPQ 560 (CCPA 1972).
In the instant case, Lee teaches a method for separating antibody isoforms using cation exchange chromatography and a method for separating and purifying several antibody isoforms using cation exchange chromatography. Lee et al. teach that because product-related impurities have properties very similar to those of the desired product, it is very difficult to isolate these impurities by chromatography which is used in the purification process. Lee teaches that with the recent development of technology, attempts have been made to remove such product-related impurities through development of new purification processes. Lee teaches the term “isoforms” means proteins having forms slightly different from the desired form due to post-transcriptional modification, post-translational modification and cellular differences, among the same types of proteins expressed from the same gene. Lee teaches that such isoforms can be classified as product-related substances or product-related impurities according to the function and purpose of the original protein. Lee teaches the term “impurities” includes any substances other than the target protein. Examples of impurities include, but are not limited to, protein isoforms having no medicinal effect, protein aggregates, protein fragments, DNA contaminants, virus, protein A (eluted from a column), host cell proteins, endotoxins, medium components such as Hy-Fish (FL) and IGF, and the like.
The scientific reasoning and evidences as whole indicates that the rejection should be maintained.
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 1-3, 8-11, 14, 15, 20-23, 25, 27, 28, 30, 31, 36, 39-44, 48, 52 and 53 remain provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-5, 7-15, 17-19, 20, 21, 23, 24, 30-32, 37-40 and 50 of copending Application No. 17/773,892 in view of Lee et al. (US 2016/0264618).
The basis for this rejection is set forth at pages of the previous Office Action. It is noted that the claims in copending Application No. 17/773,892 have been amended to recite “bispecific antibody”.
APPLICANT’S ARGUMENTS: Applicant argues that the instant application recites "equilibrating a cation exchange chromatography medium with an equilibration buffer comprising 94-105 mM sodium chloride", "loading the composition comprising the bispecific antibody on to the cation exchange chromatography medium in a load buffer comprising 94-105 mM sodium chloride" and that the claims of copending Application 17/773,892 does not teach or suggest the instant claims or a concentration of sodium chloride of the equilibrium buffer or the load buffer.
Applicant argues that Lee does not remedy the deficiencies of copending Application No. 17/773,892. Applicant argues that as discussed above, Lee does not teach or suggest "equilibrating a cation exchange chromatography medium with an equilibration buffer comprising 94-105 mM sodium chloride" and "loading the composition comprising the bispecific antibody on to the cation exchange chromatography medium in a load buffer comprising 94-105 mM sodium chloride" as claimed.
Applicant’s arguments have been fully considered but are not found persuasive for reasons of record. Additionally, the Examiner has discussed above, the teachings of Lee et al. and how the Lee reference renders the instant claims obvious. The scientific reasoning and evidence as a whole indicates that rejection should be maintained.
Conclusion
No claims are allowed.
THIS ACTION IS MADE FINAL. 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.
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/R.M.D/Examiner, Art Unit 1647 7/22/2026
/BRIDGET E BUNNER/Primary Examiner, Art Unit 1647
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