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 .
DETAILED ACTION
This application is a US national phase of PCT/US2020/037069, filed June 10, 2020, with provisional application 62/859580 filed June 10, 2019.
Applicant’s amendment filed February 20, 2026 is acknowledged. Claims 2-4, 7-64, 66-68, 71-76, 81-83, 85, and 87-90 are canceled, and claim 94 is newly added. Claims 1, 80, and 86 are amended. Currently claims 1, 5-6, 65, 69-70, 77-80, 84, 86, and 91-94 are pending and under examination.
Claim Objections
Claim 94 is objected to because of the following informalities: need to delete “. Appropriate correction is required.
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 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, 5-6, 65, 69-70, 77-79, 84, 86, and 91-94 are rejected under 35 U.S.C. 103 as being unpatentable over Ponath et al. (US 7,402,410 B2 cited in PTO-892 mailed 11/20/2024, hereinafter “Ponath”) in view of Shpreter Fon Kredenshtajn et al. (RU 2810540 C2, cited in PTO-892 mailed 8/20/2025, hereinafter “Shpreter”), as evidenced by Shukla et al. (BioProcess International, May, 2005, pgs. 36-44, cited in PTO-892 mailed 11/20/2024, hereinafter “Shukla”).
Regarding claims 1, 5-6, 69-70, 77-79, 84, 86, and 91-93, Ponath teaches humanized immunoglobulin reactive with α4β7 integrin, and host cells comprising the nucleotide sequence encoding the immunoglobulin (title, abstract). Ponath teaches the immunoglobulin produced retains at least one antigen binding function of a corresponding full-length antibody (e.g., specificity for α4β7 of Act-1 antibody), and preferably, retain the ability to inhibit the interaction of α4β7 with one or more of its ligands (e.g., MAdCAM-1, fibronectin) (col. 6, lines 45-50). Ponath teaches humanized immunoglobulin light chains (e.g., comprising CDR1, CDR2 and CDR3 of the light chain of the Act-1 antibody, and a human light chain FR), and to humanized immunoglobulin heavy chains (e.g., comprising CDR1, CDR2, CDR3 of the heavy chain of the Act-1 antibody (col. 2, lines 25-30). Ponath teaches the heavy chain variable region sequence SEQ ID NO: 55 has 100% identity to instant SEQ ID NO: 1, which also comprises instant SEQ ID NO’s: 2-4, which meets the limitations of claims 1, 69, and 86. Ponath teaches the light variable region sequence SEQ ID NO: 52 has 100% identity to instant SEQ ID NO: 5, which also comprises instant SEQ ID NO’s: 6-8, which meets the limitations of claims 1, 69, and 86. As evidenced by the instant specification, vedolizumab is a humanized antibody that comprises a human IgG1 framework and constant regions and antigen-binding CDRs from the murine antibody Act-1, and specifically binds to the α4β7 integrin, e.g., the α4β7 complex, and blocks the interaction of α4β7 integrin with mucosal addressin cell adhesion molecule-1 (MAdCAM-1), thus Ponath’s anti-α4β7 antibody inherently meets the limitations of claims 70 and 91 (pg. 19, lines 4-10).
Ponath teaches purification of humanized ACT-1 antibody from cell culture supernatants of transient or stable cell transfectant cultures were carried out by Protein A affinity chromatography, (Poros A/M 4.6/100 mm, 5 mL/min using a Bio-Cad workstation (Perseptive Biosystems, Inc.)), which meets the limitations of claims 1, 77-78, and 86. (col. 45, lines 39-41). Ponath teaches the cell culture supernatant was applied to the column and washed with PBS, then 0.1M sodium acetate at pH 5.0 which meets the limitations of claims 1 and 5 (col. 45, lines 46-54). Ponath teaches elution was accomplished by washing with 0.1 M NaCitrate at pH 3.5 (col. 45, lines 54-55). Ponath teaches no more than 15 mg of antibody were applied to the column in one given run, which inherently meets the limitations of the antibody solution is loaded more than 10 g/L in claim 79 (col. 45, lines 48-49).
Ponath teaches characterizing the purity of the antibody preparation with SDS-PAGE, the molecular weight of one of the components was approximately 55,400 Daltons and represented 68.6% of the total stained bands visualized in the gel lane, while the second component corresponding to slightly less than 31,000 Daltons, represented 30.5% of the total stained bands, which means approximately 99% of the preparation consisted of either intact antibody or single heavy or light chain immunoglobulin chains (col. 47, lines 19-29), thus inherently meets the limitations of claim 84, because the examiner interprets high molecular weight (HMW) aggregates to have a weight greater than a monomer antibody and greater than 147 kDa according to the Specification (pg. 17, lines 29-30). Similarly, Ponath teaches a 13 μI aliquot of the 0.243 mg/ml solution, containing 3.16 μg of protein, was loaded onto the designated sample lanes of the SDS gel, which calculates to total protein concentration at approximately 243 ppm, wherein HCP impurities were less than 1% calculating to less than 2.43 ppm, thereby meeting the limitations of claims 92-93 (col. 46, lines 62-65).
Ponath does not explicitly teach utilizing Chinese hamster ovary (CHO) cells to produce the anti-α4β7 antibody in the working examples as recited in instant claims 1 and 86, however, Ponath teaches CHO cells are suitable host cells that can express the humanized immunoglobulin of his invention (col. 12, line 7).
Ponath does not explicitly teach the wash solution is a pH of about 7, nor the elution solution has a pH of 3.7-4.0.
However, Schpreter teaches purification of Fc constructs based on human IgG1 and contain modified CH3 domains including amino acid modifications compared to the wild-type CH3 domain polypeptide (abstract). Schpreter teaches purification of these heterodimeric antibodies was achieved with a Protein A chromatography and washed with 10 column volumes of PBS buffer at pH 7.2, then the antibody was eluted with 10 column volumes of citrate buffer at pH 3.6, and the resulting pooled fractions containing the antibody were neutralized with Tris at pH 11, which provided greater than 90% purity (pg. 60, Example 2; pg. 68, sec. 1.1).
Although neither Ponath nor Schpreter teach the elution solution is pH 3.7-4.0, differences in concentration or temperature will not support the patentability of subject matter encompassed by the prior art unless there is evidence indicating such concentration or temperature is critical. "[W]here 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." In re Aller, 220 F.2d 454, 456, 105 USPQ 233, 235 (CCPA 1955). Similarly, as evidenced by Shukla, monoclonal antibodies purification utilizing Protein A columns typically bind at neutral pH and can be eluted at low pH (typically between pH 3 and 4) (pg. 36, col. 2, para 2). Therefore, the selection of specific pH concentrations clearly would have been a routine matter of optimization using standard laboratory techniques available at the time of filing on the part of the artisan of ordinary skill, said artisan recognizing that the effectiveness of the composition would have been affected by these concentrations. "[W]here 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." In re Aller, 220 F.2d 454, 456, 105 USPQ 233, 235 (CCPA 1955).
Schpreter also teaches after Protein A chromatography in the next step of the purification process, a low pH soak was utilized to inactivate the viruses, by incubating elution at pH 3.6 with 10% acetic acid for 90 minutes, and was assessed on SEC-HPLC (pg. 68, sec. 1.2). Purity assessment using size exclusion HPLC after three column chromatography steps revealed a single peak within the expected 150 kDa region for native IgG1 and was assessed to be greater than 98% (pg. 69, sec. 1.7).
Therefore, one of ordinary skill in the art would have a reasonable expectation of success to modify the method taught by Ponath by adjusting the pH of the elution solution to be between 3.7-4.0, since the prior art discloses pH 3.5 and 3.6 as an effective elution pH, which would have been obvious for one skilled in the art to try eluting at other pH concentrations for optimal antibody purification, such as the presently claimed purification yield of greater than 97% monomer antibody determined by size exclusion chromatography as taught by Schpreter.
Regarding claims 65 and 94, Ponath teaches the humanized immunoglobulins can be used as therapeutic agents in humans (col. 3, lines 28-29).
Claim 80 is rejected under 35 U.S.C. 103 as being unpatentable over Ponath in view of Schpreter, and Shukla as applied to claims 1, 5-6, 65, 69-70, 77-79, 84, 86, and 91-94 above, and further in view of Noh et al. (Scientific Reports, 2018, 8:5361, pgs. 1-11, cited in PTO-892 mailed 11/20/2024, hereinafter “Noh”).
Ponath nor Schpreter do not explicitly teach the host cell can be a glutamine synthase knockout CHO cell (GS-CHO).
However, Noh teaches characterizing GS-knockout CHO cells in their monoclonal antibody production (abstract). Noh teaches the use of the GS-knockout CHO host cell line facilitates the rapid generation of high producing clones with reduced production of lactate and ammonia in the absence of MSX (abstract).
Therefore, it would have been prima facie obvious to one of ordinary skill in the art to utilize the method of producing anti-α4β7 antibody in a CHO cell line taught by Ponath and Schpreter, and substitute the CHO with a GS-knockout CHO cell line taught by Noh with a reasonable expectation of success. One of ordinary skill in the art would have been motivated to utilize a GS-knockout CHO cell line as these are high-producing clones and provide an improved selection stringency as taught by Noh (abstract).
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, 5-6, 65, 69-70, 77-79, 84, 86, and 91-94 are provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claims 22, 25-26, 31, 44-45, 90, and 113 of copending Application No. 17/596421 in view of Ponath and Schpreter as evidenced by Shukla.
Regarding instant claims 1, 5-6, 69, 77-79, 84, 86, and 91-92, claim 22 of ‘421 recites a method of purifying a humanized anti-α4β7 antibody, wherein the antibody is exposed to a pH at or below 4.0 and comprises a heavy chain variable region as set forth in SEQ ID NO: 1, which has 100% identity to instant SEQ ID NO: 1, and light chain variable region as set forth in SEQ ID NO: 5, which has 100% sequence identity to instant SEQ ID NO: 5. Instant SEQ ID NO’s: 2-4 & 6-8 are inherently present in the SEQ ID’s recited in ‘421. Claim 31 recites purifying the composition using one or more chromatographic separation steps selected from the group consisting of affinity chromatography, inter alia. Claim 22 of ‘421 recites the composition in the method is derived from a CHO mammalian cell culture expressing vedolizumab. ‘421 does not explicitly recite the antibody is purified with Protein A, or the method steps utilized in the Protein A chromatography recited in the instant claims.
However, Ponath teaches purification of humanized ACT-1 antibody from cell culture supernatants of transient or stable cell transfectant cultures were carried out by Protein A affinity chromatography, (Poros A/M 4.6/100 mm, 5 mL/min using a Bio-Cad workstation (Perseptive Biosystems, Inc.) (col. 45, lines 39-41). Ponath teaches the cell culture supernatant was applied to the column and washed with PBS, then 0.1M sodium acetate at pH 5.0 which meets the limitation of instant claims 1 and 5 (col. 45, lines 46-54). Ponath teaches elution was accomplished by washing with 0.1 M NaCitrate at pH 3.5 which meets the limitations in instant claims 1, 6, 81, and 82 (col. 45, lines 54-55). Ponath teaches no more than 15 mg of antibody were applied to the column in one given run, which inherently meets the limitation that the antibody solution is loaded more than 10 g/L in instant claim 79 (col. 45, lines 48-49). Ponath teaches in characterizing the purity of the antibody preparation with SDS-PAGE, the molecular weight of one of the components was approximately 55,400 Daltons and represented 68.6% of the total stained bands visualized in the gel lane, while the second component corresponding to slightly less than 31,000 Daltons, represented 30.5% of the total stained bands, which means approximately 99% of the preparation consisted of either intact antibody or single heavy or light chain immunoglobulin chains (col. 47, lines 19-29), thus inherently meeting the limitations of the instant claims, because the examiner interprets high molecular weight (HMW) aggregates to have a weight greater than a monomer antibody and greater than 147 kDa according to the Specification (pg. 17, lines 29-30). Ponath also teaches CHO cells are suitable host cells that can express the humanized immunoglobulin of his invention (col. 12, line 7).
Schpreter teaches purification of Fc constructs based on human IgG1 and contain modified CH3 domains including amino acid modifications compared to the wild-type CH3 domain polypeptide (abstract). Schpreter teaches purification of these heterodimeric antibodies was achieved with a Protein A chromatography and washed with 10 column volumes of PBS buffer at pH 7.2, then the antibody was eluted with 10 column volumes of citrate buffer at pH 3.6, and the resulting pooled fractions containing the antibody were neutralized with Tris at pH 11, which provided greater than 90% purity (pg. 60, Example 2; pg. 68, sec. 1.1).
Although neither Ponath nor Schpreter teach the elution solution is pH 3.7-4.0, differences in concentration or temperature will not support the patentability of subject matter encompassed by the prior art unless there is evidence indicating such concentration or temperature is critical. "[W]here 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." In re Aller, 220 F.2d 454, 456, 105 USPQ 233, 235 (CCPA 1955). Similarly, as evidenced by Shukla, monoclonal antibodies purification utilizing Protein A columns typically bind at neutral pH and can be eluted at low pH (typically between pH 3 and 4) (pg. 36, col. 2, para 2). Therefore, the selection of specific pH concentrations clearly would have been a routine matter of optimization using standard laboratory techniques available at the time of filing on the part of the artisan of ordinary skill, said artisan recognizing that the effectiveness of the composition would have been affected by these concentrations. "[W]here 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." In re Aller, 220 F.2d 454, 456, 105 USPQ 233, 235 (CCPA 1955).
Schpreter also teaches after Protein A chromatography in the next step of the purification process, a low pH soak was utilized to inactivate the viruses, by incubating elution at pH 3.6 with 10% acetic acid for 90 minutes, and was assessed on SEC-HPLC (pg. 68, sec. 1.2). Purity assessment using size exclusion HPLC after three column chromatography steps revealed a single peak within the expected 150 kDa region for native IgG1 and was assessed to be greater than 98% (pg. 69, sec. 1.7).
Therefore it would have been prima facie obvious to one of ordinary skill in the art at the time of filing to purify the humanized anti-α4β7 antibody recited in ‘421, and utilize the method taught by Ponath as well as adjust the pH of the elution solution to be between 3.7-4.0, since the prior art discloses pH 3.5 and 3.6 as an effective elution pH, which would have been obvious for one skilled in the art to try eluting at other pH concentrations for optimal antibody purification, such as the presently claimed purification yield of greater than 97% monomer antibody determined by size exclusion chromatography as taught by Schpreter.
Regarding instant claims 65 and 94, claims 44 and 45 recite the composition is incorporated into a pharmaceutical formulation, which inherently anticipates a formulation suitable for human use.
Regarding instant claim 70, claims 24 and 27 of ‘421 recite the anti-α4β7 antibody is vedolizumab. Claim 113 of ‘421 recites a composition comprising vedolizumab obtainable by the method recited in claim 22 of ‘421, which is a product by process, thus falls under the scope of obviousness.
This is a provisional nonstatutory double patenting rejection.
Response to Arguments
Applicant's arguments filed February 20, 2026 have been fully considered but they are not persuasive.
Regarding remarks directed to the 103 rejection, Applicant argues the claimed invention provides a purification method for obtaining a composition comprising a CHO-cell produced anti- α4β7 antibody, where the composition has low level of impurity, i.e., less than 1% high HMW aggregates, and is achieved with an elution solution having a pH of about 3.7 to 4. Applicant points to the working examples of the specification, a composition comprising a combination of low level of HMW aggregates and high level of antibody monomer was achieved when the antibody produced in CHO cells was eluted from a Protein A matrix at a pH of 3.7 to 4, and revealed that elution pH had a significant impact on both monomer and HMW, and shows the significance of the pH range in Table 1 and Fig. 2, thus Applicant argues an unexpected effect. Applicant argues Ponath does not meet the limitations of purity in the claims, only showing intact antibody as 84.4% under non-reducing conditions. Applicant further argues Ponath does not meet the limitation of 10 g/L concentration in claim 79, because Ponath describes applying no more than 15 mg of antibody per run, and calculates the concentration to be 9.02 mg/mL based on the column size. Applicant further argues the Office incorrectly assumes that the 1% (which is not an intact antibody or single heavy or light chain Ig chains) represents HMW aggregates, and the remaining 1% is not characterized by Ponath, which could include other species, such as fragments smaller than heavy or light chains or other protein impurities. Thus, the uncharacterized 1% is not inherently HMW species and is not suggestive of claim 84. Applicant argues that Ponath does not teach the "HCP impurities were less than 1% calculating to less than 2.43 ppm" which allegedly meets the limitation of dependent claims 92 and 93. The Office provides no rationale as to how 243 ppm was determined from a protein concentration which is not characterized by the art as even containing HCPs. Further, the Office has provided no rationale as to how 2.43 ppm was calculated. Thus, Ponath does not inherently teach the subject matter of claims 92 and 93. Applicant argues Shpreter does not teach the method provides greater than 90% purity, but rather producing a composition of at least 90% heterodimers, which are not the same as HMW. Applicant argues Shukla also fails to remedy the deficient teachings of Ponath and Shpreter, teaching that such an elution pH is associated with problems, including aggregate formation, such as elution at pH 3.7 of a CHO-expressed Fc fusion protein from a protein A column resulted in up to 20% aggregate (see page 40, left col., first paragraph, and Figure 3A), which is above and outside the scope of the composition of the claimed invention.
In response to applicant's arguments against the references individually, one cannot show nonobviousness by attacking references individually where the rejections are based on combinations of references. See In re Keller, 642 F.2d 413, 208 USPQ 871 (CCPA 1981); In re Merck & Co., 800 F.2d 1091, 231 USPQ 375 (Fed. Cir. 1986). Ponath teaches the overall method of purifying anti- α4β7 antibody produced from a mammalian cell line with Protein A chromatography, and after reducing the eluate, the composition comprised less than 1% HMW species (since the two bands of 55,400 Da and 31,000 Da accounted for 99% of composition, as stated by the author). Ponath also teaches the volume of cell culture supernatant applied per run varied according to the concentration of antibody, and normally no more than 15 mg of antibody were applied to the column in one given run (Flow rate was 5 ml/min throughout the purification procedure Example 3), thus the 15 mg concentration would still meet the claim’s limitation. Furthermore, the HCP is inferred as impurities in Ponath, and based on the analysis of the reducing conditions of the eluate which was 3.16µg/13µl aliquot equates to 243 mg/L, which is 243 ppm, 1% of 243 ppm is 2.43 ppm, thus meeting the limitation in claims 92-93. Schpreter also explicitly states “An initial capture and purification step using Protein A affinity chromatography yielded product with >90% purity.” (pg. 68, sec. 1.1).
Responding now to Applicant’s arguments that Shukla does not disclose successful elution at pH 3.7, Shukla teaches additional aggregate or particulate formation may occur following protein A elution during low pH viral inactivation or during neutralization of the eluate pool, as seen in Figure 3A, aggregation of an Fc fusion protein over time in the protein A eluate (not neutralized) and Figure 3B. After Shukla did observe 20% aggregates, Shukla found an even more effective solution to the aggregation problem was to operate the protein A column at cold temperatures (2–8 °C), wherein Figure 4 shows a comparison of the aggregation rate constants in protein A eluates from three experiments using 50 mM citrate, pH 3.7 as the elution buffer at room temperature; 50 mM citrate, 1 M urea, pH 3.7 at room temperature; and 50 mM citrate, pH 3.7, with the entire column step being operated at 2–8 °C. Operating the column step at cold temperatures gave the lowest rate constant for aggregation, which is an important parameter not identified in the claims.
Regarding Applicant’s arguments of unexpected results based on the pH elution of 3.7-4.0 with greater than 97% monomer purity in Table 1, it can be seen in the elution profile that pH as low as 3.34-3.60 results in greater than 97% monomer purity as well, which falls within scope of the expected results taught by the prior art, thus is not sufficient to overcome the claimed method as obvious over the prior art.
Regarding remarks directed to the provisional nonstatutory double patenting rejection, Applicant argues the ‘421 application was amended to now recite the vedolizumab is exposed to a pH of 4.6-5.5 for at least 2 hours, which is higher than the scope of the instantly claimed pH range.
Since the claimed method recites ‘comprising’, it is open ended to include pre-treatment conditions, such as exposing the solution to a higher pH, then eluting at the claimed pH based on the teachings of Ponath, Shpreter, and Shukla, especially considering claim 31 of ‘421 recites the antibody is purified with affinity chromatography, thus the provisional double patenting rejection is maintained.
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.
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/LOUISE W HUMPHREY/Supervisory Patent Examiner, Art Unit 1657
/JESSICA EDWARDS/
Examiner, Art Unit 1657