CTNF 18/602,268 CTNF 101360 DETAILED ACTION Notice of Pre-AIA or AIA Status 07-03-aia AIA 15-10-aia The present application, filed on or after March 16, 2013, is being examined under the first inventor to file provisions of the AIA. Claims Status Claims 1-14 and 16-20 are pending. Claim 15 is canceled. Election/Restrictions Applicant’s election without traverse of: Species Group 1 : protein A chromatography Species Group 2 : Applicant did not select a species; Applicant has canceled claim 15. Species Group 3 : ultrafiltration/diafiltration Species Group 4 : high molecular weight species of the recombinant protein in the reply filed on 05/19/2026 is acknowledged. Information Disclosure Statement The information disclosure statement (IDS) submitted on 05/19/2026 and 10/22/2025 is acknowledged. The submission is in compliance with the provision of 37 CFR 1.97. Accordingly, the information disclosure statement has been considered. Claim Rejections - 35 USC § 112 07-30-02 AIA 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. 07-34-01 Claim 9 is 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. With regards to claim 9 , the claim recites “a low pH viral inactivation unit operation one or more unit operations ..”. As written, it is unclear what one or more unit operations means. In the interest of advancing prosecution, the Examiner is interpretating this to mean on or more unit operations of a low pH viral inactivation operation. Claim Rejections - 35 USC § 102 07-06 AIA 15-10-15 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. 07-07-aia AIA 07-07 The following is a quotation of the appropriate paragraphs of 35 U.S.C. 102 that form the basis for the rejections under this section made in this Office action: A person shall be entitled to a patent unless – 07-08-aia AIA (a)(1) the claimed invention was patented, described in a printed publication, or in public use, on sale, or otherwise available to the public before the effective filing date of the claimed invention. 07-12-aia AIA (a)(2) the claimed invention was described in a patent issued under section 151, or in an application for patent published or deemed published under section 122(b), in which the patent or application, as the case may be, names another inventor and was effectively filed before the effective filing date of the claimed invention. 07-15 AIA Claim s 1, 3, 6, 9, 11-14, and 18-20 are rejected under 35 U.S.C. 102( a)(1 ) as being anticipated by Woo et al. (Journal of Chromatography A, Vol. 1218, pg. 5386-5392; PMID: 21511263 ; published online April 4, 2011), hereinafter referred to as Woo . With regards to claim 1 , Woo discloses a method for impurity removal ( purification ) in mAb (recombinant protein) feedstocks (see Abstract, pg. 5386). Woo discloses a novel anion exchange membrane absorber, ChromaSorb, which shows excellent impurity removal under different buffer conductivities ranging from 2-27 mS/cm . Woo discloses that the anion exchange membrane absorber utilizes a primary amine ligand (see Abstract, pg. 5386 and pg. 5392, Conclusions). Woo further discloses that crude MVM (Minute viruses of mice) was added to pools of mAb A (recombinant protein) at a conductivity of 6 mS/Cm . Woo discloses that the mAb feed stock was in 20 mM Tris buffer at pH 7.2 (see pg. 5387, Protein feed stocks). Woo discloses that MVM retention by the ChromaSorb anion exchange absorber was compared at 6 mS/cm using a representative mAb A feed and that the ChromaSorb anion exchange absorber fully retained virus at mAB mass loadings of up to 6 kg/L of membrane (see pg. 5389, Section 3.3 Virus Removal). Woo discloses that once the fluid penetrates the membrane, impurities are absorbed and the purified fluid collects on a small channel (see pg. 5390). With regards to claim 3 , in addition to the teaching of Woo as applied to claim 1 above, Woo discloses that the ChromaSorb anion exchange absorber is coated with a primary amine ligand, polyallylamine (see pg. 5387, Section 2.1 Devices). With regards to claim 6 , in addition to the teachings of Woo as applied to claim 1 above, Woo discloses that crude MVM (Minute viruses of mice) was added to pools of mAb A (recombinant protein) at a conductivity of 6 mS/cm. With regards to claim 9 , in addition to the teachings of Woo as applied to claim 1 above, Woo discloses the elution of product under low pH conditions , followed by a low pH hold to inactivate viruses , after which the pH of the protein pool is adjusted and processed through a polishing step, typically ion exchange (see Introduction, pg. 5386). With respect to claims 11-14 , in addition to the teachings of Woo as applied to claim 1 above, Woo discloses that the mAb feed stock obtained for virus spiking experiments was processed through a Protein A chromatography column (affinity chromatography) and then processed through a CEX column prior to loading onto the ChromaSorb anion exchange absorber (see pg. 5387, Section 2.3. Protein feed stocks, and pg. 5388, Section 2.8 Virus retention experiments). With respect to claims 18-19 , in addition to the teachings of Woo as applied to claim 1 above, Woo discloses a recombinant protein in the composition that is monoclonal antibody mAb A ( antigen-binding protein, antibody ) (see pg. 5389, Section 3.3 virus removal). With respect to claim 20 , in addition to the teachings of Woo as applied to claim 1 above, it is inherent during the anion exchange chromatography step using the ChromoSorb anion exchange absorber or other chromatography steps disclosed by Woo such as Protein Chromatography A, that high molecular weight species of the recombinant protein is an impurity in the composition as the mAB disclosed by Woo is prepared in mammalian cells and would inherently contain other high molecular weight proteins as evidenced by LeBarre et al. (Journal of Chromatography A, Vol. 1762: 466375; PMID: 409724431; published September 12, 2025). The Examiner is defining a high molecular weight recombinant protein as any protein produced during recombinant expression as the claim does not specify a specific species of the recombinant protein. Therefore, claims 1, 3, 6, 9, 11-14, and 18-20 are rejected under 35 U.S.C. 102(a)(1) as being anticipated by Woo et al. (Journal of Chromatography A, Vol. 1218, pg. 5386-5392; PMID: 21511263 ; published online April 4, 2011) . Claim Rejections - 35 USC § 103 07-06 AIA 15-10-15 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. 07-20-aia AIA 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. 07-103 AIA The text of those sections of Title 35, U.S. Code not included in this action can be found in a prior Office action. 07-23-aia AIA 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. 07-20-02-aia AIA 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. 07-27-aia AIA Claim s 1, 3, 6, 9, 11-14, and 17-20 are rejected under 35 U.S.C. 102( a)(1 ) as anticipated by or, in the alternative, under 35 U.S.C. 103 as obvious over Woo et al. (Journal of Chromatography A, Vol. 1218, pg. 5386-5392; PMID: 21511263 ; published online April 4, 2011), hereinafter referred to as Woo . With regards to claims 1 and 3 , Woo teaches a method for impurity removal ( purification ) in mAb (recombinant protein) feedstocks (see Abstract, pg. 5386). Woo teaches a novel anion exchange membrane absorber, ChromaSorb, which shows excellent impurity removal under different buffer conductivities ranging from 2-27 mS/cm . Woo teaches that the anion exchange absorber utilizes a primary amine ligand (see Abstract, pg. 5386 and pg. 5392, Conclusions). Woo teaches that the ChromaSorb anion exchange absorber is coated with a primary amine ligand, polyallylamine (see pg. 5387, Section 2.1 Devices). Woo further teaches that crude MVM (Minute viruses of mice) was added to pools of mAb A (recombinant protein) at a conductivity of 6 mS/Cm . Woo teaches that the mAb feed stock was in 20 mM Tris buffer at pH 7.2 (see pg. 5387, Protein feed stocks). Woo teaches that MVM retention by the ChromaSorb anion exchange absorber was compared at 6 mS/cm using a representative mAb A feed and that the ChromaSorb anion exchange absorber fully retained virus at mAb mass loadings of up to 6 kg/L of membrane (see pg. 5389, Section 3.3 Virus Removal). Woo teaches that once the fluid penetrates the membrane, impurities are absorbed and the purified fluid collects on a small channel (see pg. 5390). It would have been obvious to one of ordinary skill in the art of protein purification before the effective filing date of the current instant application to follow the teachings of Woo to design a method for purifying a recombinant protein from a composition comprising the recombinant protein and at least one impurity by loading a mAb pool with added MVM to an ion exchange material comprising a primary amine such as the ChromaSorb anion exchange absorber, taught by Woo , wherein the composition has a pH of about 7.0 to about 8.0 and a conductivity of less than 10 mS/cm. One of ordinary skill in the art of protein purification would be motivated to do so as Woo teaches that ChromaSorb (having a primary amine anion exchange material) shows excellent impurity removal. One of ordinary skill in the art would have expectations of success in designing such a purification method as the teachings of Woo provide all the methods and guidance needed to do so. With regards to claim 6 , in addition to the teachings of Woo as applied to claim 1 above, Woo discloses that crude MVM (Minute viruses of mice) was added to pools of mAb A (recombinant protein) at a conductivity of 6 mS/cm. It would have been obvious to one of ordinary skill in the art of protein purification before the effective filing date of the current instant application to follow the teachings of Woo to apply a conductivity of 6 mS/cm to the composition being purified. One of ordinary skill in the art of protein purification would be motivated to do so as Woo teaches the mAb A/ MVM mixture to be purified has a conductivity of 6 mS/cm. One of ordinary skill in the art would have expectations of success in designing such a purification method as the teachings of Woo provide all the methods and guidance needed to do so. With regards to claim 9 , in addition to the teachings of Woo as applied to claim 1 , Woo teaches the elution of product under low pH conditions , followed by a low pH hold to inactivate viruses , after which the pH of the protein pool is adjusted and processed through a polishing step, typically ion exchange (see Introduction, pg. 5386). It would have been obvious to one of ordinary skill in the art of protein purification to include a low pH hold to inactivate viruses prior to loading in the anion exchange method as taught by Woo since Woo teaches it is a typical step in purification of monoclonal antibodies (see Introduction, pg. 5386). One of ordinary skill in the art would be motivated to incorporate a low pH inactivation step in order to inactivate any potential viral contaminants to ensure the safety of the purified monoclonal antibodies. One of ordinary skill in the art of protein purification would have expectations of success in doing so as Woo provides the necessary teachings and guidance. With respect to claims 11-14 , in addition to the teachings of Woo as applied to claim 1 above, Woo teaches that the mAb feed stock obtained for virus spiking experiments were processed through a Protein A chromatography column (affinity chromatography and then processed through a CEX column prior to loading on the ChromaSorb anion exchange absorber (see pg. 5387, Section 2.3. Protein feed stocks, and pg. 5388, Section 2.8 Virus retention experiments). It would have been obvious to one of ordinary skill in the art of protein purification before the effective filing date of the current instant application to follow the teachings of Woo to process the recombinant protein/impurity mixture through an additional chromatography step such as Protein A chromatography and CEX column as additional chromatography steps . One of ordinary skill in the art of protein purification would be motivated to do so as Woo teaches additional chromatography steps that can be used to improve the purification process. One of ordinary skill in the art would have expectations of success in incorporating the additional chromatography unit operations as the teachings of Woo provide all the methods and guidance needed to do so. With regards to claim 17 , in addition to the teachings of Woo as applied to claim 1 above, it would have been obvious to one of ordinary skill in the art of protein purification before the effective date of the current instant application to arrive at result of a purified composition of at least 85% w/w of the recombinant protein in the composition before loading as Woo teaches that the novel anion exchange absorber shows excellent impurity removal under different buffer conductivities ranging from 2 to 27 mS/cm (see Abstract, pg. 5386). It would be within the skill of a person of ordinary skill in the art of protein purification to modify the different buffer conductivities taught by Woo to arrive at a purified composition that comprises at least 85% of the recombinant protein in the composition prior to the loading. One of ordinary skill in the art would be motivated by the teachings of Woo to optimize the buffer conductivity conditions to arrive at such a purity level. One of ordinary skill in the art would also have expectation of success in arriving at such a purity level as Woo provides the teachings of the buffer conductivity range where the anion exchange absorber has excellent impurity removal and this further constitutes routine experimentation involving result-effective variables (see In re Aller , 220 F.2d 454, 42 CCPA824, 10 USPQ 233 (C.C.P.A., 1955) With respect to claims 18-19 , in addition to the teachings of Woo as applied to claim 1 above, Woo discloses a recombinant protein in the composition that is monoclonal antibody mAb A ( antigen-binding protein, antibody ) (see pg. 5389, Section 3.3 virus removal). It would have been obvious to one of ordinary skill in the art of protein purification before the effective filing date of the current instant application to follow the teachings of Woo to select a recombinant protein that is an antigen-binding protein such as an antibody since Woo teaches the purification of an mAb by anion-exchange chromatography. It would also be obvious to one of ordinary skill in the art of protein purification would be motivated to do so as Woo as teaches application of anion exchange material which shows excellent impurity removal as applied to the purification of an mAb from a mixture. One of ordinary skill in the art would have expectations of success of selecting an antigen-binding protein or antibody as the recombinant protein being subject to purification as the teachings of Woo provide all the methods and guidance needed to do so. With respect to claim 20 , in addition to the teachings of Woo as applied to claim 1 above, it is inherent during the anion exchange chromatography step using the novel anion exchange absorber (Chromasorb) or other chromatography steps disclosed by Woo such as Protein Chromatography A, that high molecular weight species of the recombinant protein is an impurity in the composition as the mAb disclosed by Woo is prepared in mammalian cells and would inherently contain other high molecular weight proteins as evidenced by LeBarre et al. (Journal of Chromatography A, Vol. 1762: 466375; PMID: 409724431; published September 12, 2025). The Examiner is interpreting a high molecular weight recombinant protein as any protein produced during recombinant expression as the claim does not identify a specific recombinant protein species. It would therefore be obvious to one of ordinary skill in the art that any high molecular weight species of the protein can be an impurity. Therefore, claims 1, 3, 6, 9, 11-14, and 17-20 are rejected under 35 U.S.C. 102(a)(1) as anticipated by or, in the alternative, under 35 U.S.C. 103 as obvious over Woo et al. (Journal of Chromatography A, Vol. 1218, pg. 5386-5392; PMID: 21511263 ; published online April 4, 2011) . 07-22-aia AIA Claim 2 is rejected under 35 U.S.C. 103 as being unpatentable over Woo et al. (Journal of Chromatography A, Vol. 1218, pg. 5386-5392; PMID: 21511263 ; published online April 4, 2011), hereinafter referred to as Woo , as applied to claim 1 above, and further in view of Mitterer et al. (US Patent Application No: US 2012/0108513 A1; published May 3, 2012), hereinafter referred to as Mitterer . The teachings of Woo as applied to claim 1 are summarized above. With regards to claim 2 , Woo is silent on the particle size of the ChromaSorb primary amine anion exchange material. However, Mitterer teaches an anion exchange chromatography method in which the anion exchange resin material carries a primary amine as a ligand such as benzamidine (see Paragraph 0017, pg. 2). Mitterer further teaches anion exchange materials such as benzamidine sepharose (see Paragraph 0035, pg. 0035). Benzamidine sepharose has an inherent bead size range between 45 -165 m m as evidenced by Cytiva (Instructions for use; published 2020, cited on form PTO-892). It would have been obvious to one of ordinary skill in the art of protein purification before the effective filing date of the current instant application to modify the anion exchange purification protocol taught by Woo by substituting the ChromaSorb primary amine anion exchange material with another anion exchange material such as benzamidine sepharose taught by Mitterer as benzamidine sepharose also carries a primary amine ligand and is used as an anion exchange material (see Paragraph 0035, pg. 3). One of ordinary skill in the art of protein purification would be motivated to do so as Mitterer teaches that benzamidine sepharose carries a primary amine in the anion exchange material and which has an inherent particle size between 45-165 m m as evidenced by Cytiva . One of ordinary skill in the art would find this as a suitable optional anion exchange material for use in anion exchange chromatography as taught by Mitterer . One of ordinary skill in the art would have expectations of success in doing so as teachings of Woo and Mitterer provide all the methods and guidance needed to do so. Therefore, claim 2 is rejected under 35 U.S.C. 103 as being unpatentable over Woo et al. (Journal of Chromatography A, Vol. 1218, pg. 5386-5392; PMID: 21511263 ; published online April 4, 2011) as applied to claim 1 above, and further in view of Mitterer et al. (US Patent Application No: US 2012/0108513 A1) . 07-22-aia AIA Claim s 4-5, are rejected under 35 U.S.C. 103 as being unpatentable over Woo et al. (Journal of Chromatography A, Vol. 1218, pg. 5386-5392; PMID: 21511263 ; published online April 4, 2011), hereinafter referred to as Woo , as applied to claim 1 above, and further in view of Chen et al. (US Patent Application Publication No: US 2021/0122783 A1; published April 29, 2021), hereinafter referred to as Chen . The teachings of Woo as applied to claim 1 are summarized above. With regards to claims 4-5, Woo does not teach that the loading density is less than about 600 g/L or that the loading density is about 250 g/L-resin to about 600 g/L-resin. However, Chen et al teach a method of purifying proteins from a mixture by performing anion exchange chromatography (see claim 1, pg. 15). Chen also teaches that the chromatography comprises an AEX resin (anion exchange) selected from a variety of resin options such as (see claim 52, pg. 17). Chen also teaches that the chromatography columns with anion exchange material are loaded from 50 g/L to 500 g/L of resin (see Paragraph 0073, pg. 9). It would have been obvious to one of ordinary skill in the art before the effective filing date of the current instant application to modify the anion exchange chromatography method taught by Woo by use of a loading density of a range of 250-600 g/L of anion exchange resin material as an option for the purification since Chen teaches that this is an optional value for the loading density used for an anion exchange resin chromatography column. One of ordinary skill in the art of protein purification would be motivated to do so as a way for testing for optimization of loading density conditions of the anion exchange resin. One of ordinary skill in the art of protein purification would have expectations of success in doing so since both Woo and Chen teach all the methods and protocols needed to do so. Therefore, claims 4-5, are rejected under 35 U.S.C. 103 as being unpatentable over Woo et al. (Journal of Chromatography A, Vol. 1218, pg. 5386-5392; PMID: 21511263 ; published online April 4, 2011) as applied to claim 1 above, and further in view of Chen et al. (US Patent Application Publication No: US 2021/0122783 A1; published April 29, 2021) . 07-22-aia AIA Claim s 7-8 are rejected under 35 U.S.C. 103 as being unpatentable over Woo et al. (Journal of Chromatography A, Vol. 1218, pg. 5386-5392; PMID: 21511263 ; published online April 4, 2011), hereinafter referred to as Woo , as applied to claim 1 above, and further in view of Genentech, Inc. (WIPO International Publication Number: WO 2011/150110 A1; published December 11, 2011), hereinafter referred to as Genentech . The teachings of Woo as applied to claim 1 are summarized above. With regards to claims 7-8, Woo does not teach the use of an equilibration buffer with the anion exchange material wherein the conductivity of the equilibration buffer is less than about 10 mS/cm or is about 2 mS/cm to about 4 mS/cm. However, Genentech teaches a method that comprises use of an equilibration buffer with an anion exchange material (see Paragraph 0015, pg.3) and the conductivity of the equilibration buffer is between 2 mS/cm and 8 mS/cm (see Paragraph 0014, pg. 3). It would have been obvious to one of ordinary skill in the art of protein purification to modify the anion exchange chromatography taught by Woo by incorporating an equilibrium buffer with a conductivity about 2 mS/cm to about 4 mS/cm as taught by Genentech in order to prepare the anion exchange resin for the chromatography step. One of ordinary skill in the art of protein purification would be motivated by the combined teachings of Woo and Genentech to apply such an equilibration buffer as it is common practice in the art of protein purification to equilibrate the chromatography column with an equilibration buffer before loading a sample composition onto the column. One of ordinary skill in the art of protein purification would have expectations of success in doing so as the combined teachings of Woo and Genentech provide all the teachings needed to do so. Therefore, claims 7-8 are rejected under 35 U.S.C. 103 as being unpatentable over Woo et al. (Journal of Chromatography A, Vol. 1218, pg. 5386-5392; PMID: 21511263 ; published online April 4, 2011) as applied to claim 1 above, and further in view of Genentech, Inc. (WIPO International Publication Number: WO 2011/150110 A1; published December 11, 2011) . 07-22-aia AIA Claim s 9 and 10 are rejected under 35 U.S.C. 103 as being unpatentable over Woo et al. (Journal of Chromatography A, Vol. 1218, pg. 5386-5392; PMID: 21511263 ; published online April 4, 2011), hereinafter referred to as Woo , as applied to claim 1 above, and further in view of Coffman et al. (US Patent No: 10,435,670 B2; published October 8, 2019), hereinafter referred to as Coffman . The teachings of Woo as applied to claim 1 are summarized above. With regards to claims 9-10, Woo does not teach that the low pH viral inactivation unit operation employs an acid titrant comprising formic acid. However, Coffman teaches that inactivation of viruses that may be present in a composition including a biological product that is intended for use in a biopharmaceutical product is an important aspect of quality control for ensuring that the biopharmaceutical product will work as intended and will not inadvertently cause disease or other harm (see Column 1, lines 39-53). Coffman further teaches that typical methods from the state of the art include adding a viral-inactivating reagent such as an acid to a composition including a biological product to accomplish inactivation of a viruses that may be present in the composition of the biological product (see Column 1, lines 54-60). Coffman teaches that the virus-inactivation reagent can be an organic acid having a titratable group having a pKa between 2.3 and 4.2 or formic acid or a combination thereof and the treatment of the composition can include a pH between 3.0 and 3.8 (low pH) (see Column 3, lines 35-43). It would have been obvious to one of ordinary skill in the art of protein purification before the effective filing date of the current instant application to modify the anion exchange chromatography method as taught by Woo by incorporating a low pH viral inactivation unit operation comprising formic acid and a low pH between 3.0 and 3.8 as taught by Coffman prior to loading. One of ordinary skill in the art of protein purification would be motivated by the teaching of Coffman that viral inactivation is an important step in the production of compositions comprising biological products to ensure safety from possible viral contamination. One of ordinary skill in the art would have expectations of success in doing so since the combined teachings of Woo and Coffman provide all the necessary teachings and guidance needed to do so. Therefore, claims 9 and 10 are rejected under 35 U.S.C. 103 as being unpatentable over Woo et al. (Journal of Chromatography A, Vol. 1218, pg. 5386-5392; PMID: 21511263 ; published online April 4, 2011), hereinafter referred to as Woo, as applied to claim 1 above, and further in view of Coffman et al. (US Patent No: 10,435,670 B2; published October 8, 2019), hereinafter referred to as Coffman . 07-22-aia AIA Claim 16 is rejected under 35 U.S.C. 103 as being unpatentable over Woo et al. (Journal of Chromatography A, Vol. 1218, pg. 5386-5392; PMID: 21511263 ; published online April 4, 2011), hereinafter referred to as Woo , as applied to claim 1 above, and further in view of Teeters et al. (Biotechnology and Bioengineering, Vol. 108, pg. 1338-1346, PMID: ; published February 15, 2011), hereinafter referred to as Teeters . The teachings of Woo as applied to claim 1 are summarized above. With regards to claim 16 , Woo does not teach performing an ultrafiltration/diafiltration unit operation after the loading. However, Teeters teaches that many liquid formations for monoclonal antibodies (mAbs) require the final ultrafiltration/diafiltration step to operate at high protein concentration (see Abstract, pg. 1338). Teeters teaches that high concentration protein formulations are necessitated by therapeutic indications that require high doses and that ultrafiltration/diafiltration is typically the final process step performed to concentrate and exchange the purified drug substance to the protein concentration, pH, and excipient concentrations needed for product formulation (See Introduction, pg. 1338). It would have been obvious to one of ordinary skill in the art of protein purification before the effective filing date of the current instant application to modify the anion exchange chromatography method as taught by Woo by incorporating an ultrafiltration/diafiltration unit operation as taught by Teeters after the loading. One of ordinary skill in the art of protein purification would be motivated to do so in order to concentrate and buffer exchange the purified protein product. One of ordinary skill in the art of protein engineering would have expectation of success in doing so as the combined teachings of Woo and Teeters provide all the necessary teachings to do so. Therefore, claim 16 is rejected under 35 U.S.C. 103 as being unpatentable over Woo et al. (Journal of Chromatography A, Vol. 1218, pg. 5386-5392; PMID: 21511263 ; published online April 4, 2011) as applied to claim 1 above, and further in view of Teeters et al. (Biotechnology and Bioengineering, Vol. 108, pg. 1338-1346, PMID: ; published February 15, 2011). Conclusion No claims are allowed. Any inquiry concerning this communication or earlier communications from the examiner should be directed to GEORGE T LOUNTOS whose telephone number is (571)272-0502. The examiner can normally be reached Monday-Friday 8:00 am - 5:00 pm. 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, Robert Mondesi can be reached at 408-918-7584. 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. /GEORGE THEMISTOCLIS LOUNTOS/ Examiner, Art Unit 1652 /ROBERT B MONDESI/ Supervisory Patent Examiner, Art Unit 1652 Application/Control Number: 18/602,268 Page 2 Art Unit: 1652 Application/Control Number: 18/602,268 Page 3 Art Unit: 1652 Application/Control Number: 18/602,268 Page 4 Art Unit: 1652 Application/Control Number: 18/602,268 Page 5 Art Unit: 1652 Application/Control Number: 18/602,268 Page 6 Art Unit: 1652 Application/Control Number: 18/602,268 Page 7 Art Unit: 1652 Application/Control Number: 18/602,268 Page 8 Art Unit: 1652 Application/Control Number: 18/602,268 Page 9 Art Unit: 1652 Application/Control Number: 18/602,268 Page 10 Art Unit: 1652 Application/Control Number: 18/602,268 Page 11 Art Unit: 1652 Application/Control Number: 18/602,268 Page 12 Art Unit: 1652 Application/Control Number: 18/602,268 Page 13 Art Unit: 1652 Application/Control Number: 18/602,268 Page 14 Art Unit: 1652 Application/Control Number: 18/602,268 Page 15 Art Unit: 1652 Application/Control Number: 18/602,268 Page 16 Art Unit: 1652 Application/Control Number: 18/602,268 Page 17 Art Unit: 1652 Application/Control Number: 18/602,268 Page 18 Art Unit: 1652
Prosecution Insights