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
Claims 1-5, 8-11, 13-14, and 19-22 are pending and under examination on their merits. Claims 6-7, 12, and 15-18 were cancelled previously.
Response to Arguments
Applicant's arguments filed 8/10/2026 have been fully considered but they are not persuasive.
Applicant argues against the written description rejection of claims 1-5, 8-11, 13-14, and 19-20 under 35 U.S.C. 112(a) on the grounds that the person of ordinary skill in the art would understand the term “non-denaturing conditions” and the specification provides sufficient written description for the non-denaturing conditions in paragraphs [0096], [0098], [0106], [0101]-[0102], [0106]-[0107], [0127], [0135], and [0136] of the published application US 2022/0074950 A1 (Arguments, page 6, paragraph 1-2).
In response, this argument is unpersuasive because the grounds of rejection is based on the genus of non-denaturing conditions that selectively digest contaminating proteins, but not antibodies, in an antibody sample. The cited paragraphs merely recite the words “non-denaturing conditions.” The specification does not disclose any other conditions besides ultra-low concentration of trypsin in the absence of urea or DTT (compare [0069], [0072], and [0075] of the PGPub). This is a very narrow set of method conditions compared to the breadth of the claimed genus of method conditions. The person of ordinary skill in the art would have been unable to reasonably predict and visualize all species of the claimed genus.
Applicant argues against the rejection of claims under 35 U.S.C. 103 on the grounds that Fonslow’s process includes a first digestion with a 25,000: 1 protein:trypsin ratio under denaturing and reducing conditions in order to digest high-abundance proteins and remove them from the sample by filtration, followed by digesting the residual proteins under at a 100:1 protein:trypsin ratio under denaturing and reducing conditions (Arguments, paragraph 1 on page 8). Applicant argues that Fonslow’s digestion conditions change the principle of operation of Huang because Huang teaches a non-denaturing digest under conditions to maintain a nearly intact antibody whereas Fonslow teaches denaturing and reducing conditions to digest and remove high abundance proteins (Arguments, paragraph 2 on page 8). Applicant argues that the high abundance proteins that Fonslow teaches should be removed from the sample prior to analysis are the type of host cell proteins Huang seeks to analyze (Arguments, paragraph 3 on page 8). Applicant argues that the person of ordinary skill in the art would not have had a reasonable expectation of success in reducing the trypsin concentration 62.5 times (from 400:1 to 25,000:1) to digest the host cell proteins Huang seeks to analyze (Arguments, paragraph 1 on page 9).
In response, the rejection of record is not based on applying the digestion steps of Fonslow to the method of Huang. Rather the rejection of record is based on optimizing by routine experimentation the trypsin concentration for a given amount of protein (i.e. protein:trypsin ratio). Fonslow teaches the parameters that control the digestion of proteins based on their abundance profiles and optimizes these parameters, which include the protein lysate concentration, trypsin concentration, and digestion depletion time (Supplementary Materials, bottom paragraph on page 24 and paragraph bridging pages 25-26). Thus, both digestion depletion time and trypsin concentration for a given amount of protein are variables that the person of ordinary skill in the art would have considered for optimization. The person of ordinary skill in the art would thus have considered a range of both protein: trypsin ratios as well as digestion times.
Applicant argues that the combination of applied references do not suggest "separating the digested contaminating protein with long gradient chromatography to thereby form a separated, digested contaminating protein" as set out in independent claims 1 and 9 (Arguments, paragraph 3 on page 9).
This argument is unpersuasive because Huang teaches separating digested contaminating proteins with chromatography and Thakur is relied on to teach separating by long gradient chromatography. Huang performs UPLC-MS/MS analysis of the tryptic digests (page 5437, right column, bottom paragraph), which comprises separating the peptides (UPLC is an acronym for ultra-performance liquid chromatography). Thakur teaches long gradient chromatography (Experimental Procedures, LC-MS Analysis, lines 1 and 5-6).
Applicant argues that Huang developed this method specifically for high throughput sample analysis and to achieve a short cycle time. Thus, a skilled artisan would not have diluted the protein:trypsin ratio, which would result in longer digestion periods, or used long gradient chromatography in the methods disclosed by Huang (Arguments, paragraph 4 on page 9).
In response, this argument is unpersuasive because Thakur teaches that long gradient chromatography achieves high sensitivity at the sub-femtomole level (Abstract). Thus, the person of ordinary skill in the art would have turned to Thakur’s long gradient chromatography for the higher sensitivity. There is nothing of record to suggest that the person of ordinary skill in the art would not have made the modifications to Huang by Fonslow and Thakur for the benefit of increased method sensitivity, even at the cost of longer cycle time.
Applicant argues against the rejection of claims under 35 U.S.C. 103 on the grounds that the person of ordinary skill in the art would not have had a reasonable expectation of success in replacing the chromatography steps of Huang with the chromatography steps of Thakur (Arguments, paragraph 6 on page 9 through paragraph bridging pages 9-10).
In response, this argument is not persuasive. Like Huang, Thakur’s long-gradient chromatography is applied to a protein sample (see title of Thakur: “proteome” indicating a protein sample). Applicant has not provided any objective evidence that the chromatography method of Thakur is not applicable to the method of Huang.
Applicant argues that one of ordinary skill in the art would not be motivated to modify the methods of Huang with the BoxCar MS taught by Meier because there is no overlap in their technologies: Huang teaches shotgun proteomics, whereas Meier teaches Boxcar MS (Arguments, paragraph 4 on page 10).
In response, this argument is not persuasive because Meier teaches BoxCar mass spectrometry (a data-acquisition method) and demonstrates its application in proteomics (Discussion, paragraph 3, line 1).
Applicant argues against the rejection of claim 14 under 35 U.S.C. 103 on the grounds that Chen does not teach or suggest the claimed digestion conditions (Arguments, page 11, paragraph 2).
However, this argument is not pertinent to the claimed rejection, which only requires replacing Huang’s monoclonal antibody with any of the monoclonal antibodies taught by Chen.
Applicant argues against the rejection of claims under 35 U.S.C. 103 on the grounds that Applicant’s results are unexpected because compared to Huang, Applicant detects 296 host cell proteins whereas Huang detects 60 host cell proteins. (Arguments, bottom paragraph on page 10). Applicant argues that per MPEP 716.02(e), Applicant is not required to compare the claimed invention with subject matter that does not exist in the prior art (Arguments, paragraph 3 on page 12). Applicant argues that the Office cannot require an applicant to compare the claimed subject matter to matter suggested by the combination of references relied upon in the rejection of the claimed invention under 35 U.S.C. 103 (MPEP 716.02(e)) (Arguments, paragraph 3 on page 12).
In response, this argument is not persuasive. There is nothing in the prosecution record to suggest that the Office has required Applicant to compare the claimed subject matter to the matter suggested by the combination of references relied upon in the rejection of the claimed invention under 35 U.S.C. 103. Rather, the examiner has explained in the action why the results are not unexpected in light of the teachings of the prior art. As explained previously, a greater than additive effect of detected host cell proteins would have been expected because Meier’s BoxCar MS data acquisition method has sensitivity improvements that are orders of magnitude better than Huang. Applicant’s results are also obvious in view of the prior art of Huang, Thakur, Fonslow, and Meier. The resulting improvement in HCP identification would have been predictable. Thakur’s long-gradient chromatography achieves high sensitivity (Abstract and page 2, left column, middle of second full paragraph). The optimization of the ratio of protein: trypsin in the digestion, which would have been obvious in light of the work of Fonslow, would likewise have been expected to increase HCP detection. Meier teaches that the sensitivity of BoxCar mass spectrometry is in the low atto-molar range (Abstract). Therefore, application of Meier’s BoxCar MS would also have increased HCP identification. In summary, the person of ordinary skill in the art would have expected that the method of Huang modified by Thakur, Fonslow, and Meier would have increased HCP identification by at least an order of magnitude given the sensitivity of BoxCar MS taught by Meier.
Claim Rejections - 35 USC § 112
The following is a quotation of the first paragraph of 35 U.S.C. 112(a):
(a) IN GENERAL.—The specification shall contain a written description of the invention, and of the manner and process of making and using it, in such full, clear, concise, and exact terms as to enable any person skilled in the art to which it pertains, or with which it is most nearly connected, to make and use the same, and shall set forth the best mode contemplated by the inventor or joint inventor of carrying out the invention.
The following is a quotation of the first paragraph of pre-AIA 35 U.S.C. 112:
The specification shall contain a written description of the invention, and of the manner and process of making and using it, in such full, clear, concise, and exact terms as to enable any person skilled in the art to which it pertains, or with which it is most nearly connected, to make and use the same, and shall set forth the best mode contemplated by the inventor of carrying out his invention.
(Maintained Rejection) Claims 1-5, 8-11, 13-14, and 19-20 are rejected under 35 U.S.C. 112(a) or 35 U.S.C. 112 (pre-AIA ), first paragraph, as failing to comply with the written description requirement. The claim(s) contains subject matter which was not described in the specification in such a way as to reasonably convey to one skilled in the relevant art that the inventor or a joint inventor, or for applications subject to pre-AIA 35 U.S.C. 112, the inventor(s), at the time the application was filed, had possession of the claimed invention.
Independent claims 1 and 9 recite “A method for determining the identity or amount of a contaminating protein in an antibody preparation, comprising: incubating the antibody preparation with trypsin under nondenaturing conditions at a total protein:trypsin ratio of 2,500:1 w/w to 10,000:1 w/w to thereby digest the contaminating protein while the antibody in the antibody preparation remains intact.” The genus of non-denaturing trypsin digestion conditions is extremely broad, as the claim is not limited to an in-solution digestion and thus encompasses digestions performed on an immobilized support as well as those performed in solution. In addition, the duration of the incubation and the temperature required to digest the contaminating protein in the antibody preparation is not recited within the claim. Furthermore, the amount of the contaminating protein in the antibody preparation is not limited, thus the claim encompasses both low abundance and high abundance contaminating protein.
The person of ordinary skill in the art would not have recognized that the inventors had possession of the claimed genus of non-denaturing conditions that digest contaminating proteins, but not antibodies, in an antibody sample.
Applicant discloses a single set of conditions in which contaminating proteins in an antibody preparation are digested: Example 2, [00102]-[00104]. The only condition disclosed is the ratio of protein: trypsin, which ranges from 25,000:1 to 1,000:1 ([00102]). No other parameters of method conditions are disclosed (e.g. any necessary buffers, the required pH, any additional enzymes, the temperature of the incubation, or even the duration of the digest).
Huang (Analytical Chemistry 89.10 (2017): 5436-5444; cited in the Non-Final Action mailed on 4/17/2023) teaches mixing an antibody solution with 1 M tris-HCl buffer, pH 8, and 90 µL of pure water, adding 5 µL of 0l.5 mg/mL recombinant bovine trypsin, 0.05 mg/mL ADH1 (“contaminating protein”), and 0.02 mg/mL hPCSK9 solution (“contaminating protein”), and incubating the preparations at 37°C overnight (page 5437, right column, “Tryptic Digest of IgG1 and IgG4 Samples Spiked with CHO Null Strain or CHO Proteins”). Huang teaches that contaminating proteins are selectively digested (Abstract).
Thakur (cited in the Non-Final Action mailed on 4/17/2023) teaches first reducing proteins derived from HEK293 cells with 1 mM dithiotreitol and then alkylating with iodoacetamide (page 2, right column, In-Solution Digestion). HEK293 proteins are then digested with LysC for 3 h at a concentration of 1:50 (w/w) followed by overnight digestion with trypsin at a concentration of 1:50 (w/w) (page 2, right column, In-Solution Digestion).
Fonslow (cited in the Non-Final Action mailed on 4/17/2023) teaches denaturing and reducing protein samples, then digesting the proteins with trypsin at a 25,000:1 protein:protease mass ratio along with 1 mM CaCl2 for a 12h diffusion-limited digestion at 37 °C (page 57, “Digestion and depletion of abundant proteins”). Fonslow also teaches a 100:1 protein:protease mass ratio for digestion (Figure 1a).
In summary, although the prior art teaches various conditions for tryptic digestion of proteins in solution, with the exception of Huang, the prior art does not teach selectively digesting the contaminating protein and not the antibody. The person of ordinary skill in the art would have been unable to predict the entirety of non-denaturing conditions that selectively digest a contaminating protein, but not any antibody, based on the state of the art.
Based on the above analysis, the person of ordinary skill in the art would not have recognized that the inventors had possession of the claimed invention at the time the application was filed because the claimed genus of reaction conditions for the digestion is not commensurate in scope with the level of disclosure provided in the specification.
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.
The following rejections are necessitated by amendment.
Claims 1-5, 8-11, 13, and 19-22 are rejected under 35 U.S.C. 103 as being unpatentable over Huang et al. (Analytical Chemistry 89.10 (2017): 5436-5444) in view of Thakur et al. (cited in the Non-Final Action mailed on 4/17/2023), Fonslow et al. (cited in the Non-Final Action mailed on 4/17/2023 and included with Supplementary Materials in this action), and Meier et al. (cited in the Non-Final Action mailed on 4/17/2023).
Huang teaches characterizing the identity and amount of the host cell proteins in an antibody sample by digesting the host cell proteins and leaving the antibody nearly intact (Abstract, Table 2, and Table 4). Huang teaches treating antibody samples with trypsin, followed by incubation with the reducing agent DTT, followed by heating in order to prepare antibody domains that precipitate and can be removed by centrifugation (page 5439, Results and Discussion, left column, second paragraph). Huang then performs UPLC-MS/MS analysis of the tryptic digests (page 5437, right column, bottom paragraph), which comprises separating the peptides (UPLC is an acronym for ultra-performance liquid chromatography) and analyzing them by mass spectrometry (MS/MS is an acronym for tandem mass spectrometry) to identify and quantify the host cell proteins (Tables 2 and 4). Huang also teaches that even if the antibody does not precipitate after incubating with DTT and heating, it is still possible to detect HCP because the reduced antibody is eluted later than most of the HCP tryptic peptides and does not interfere with detection (page 5443, left column, paragraph 1). Huang first performs the tryptic digest and does not include any denaturing agents (page 5437, right column, “Tryptic Digest of IgG1 and IgG4 Samples Spiked with CHO Null Strain or CHO Proteins”). Thus, Huang’s digestion is performed under non-denaturing conditions. Huang teaches that the trypsin digestion leaves the antibodies nearly intact while digesting the contaminating protein (Abstract).
Huang does not teach that the chromatography is long gradient liquid chromatography.
Thakur teaches that the combination of small particles, long columns, and long and shallow gradients (page 2, left column, middle of second full paragraph) achieves high sensitivity (sub-femtomole) and avoids the need for pre-fractionation (Abstract). Thakur teaches a column length of 50 cm and a gradient of 140 min or 480 min (Experimental Procedures, LC-MS Analysis, lines 1 and 5-6).
It would have been obvious to a person of ordinary skill in the art before the effective filing date of the claimed invention to apply the technique of long gradient liquid chromatography in order to improve the method of Huang. One of ordinary skill in the art would have been motivated to improve the method sensitivity for detecting contaminating proteins. One of ordinary skill would have had a reasonable expectation of success given that Thakur demonstrates the large dynamic range of single run proteomics with long gradient chromatography by a triplicate analysis of both yeast cells (page 4, third full paragraph, lines 1-3) and human cells (page 6, Evaluation of Single LC-MS/MS Runs on a Human Cell Line, paragraph 1).
Huang and Thakur do not teach that the total protein:trypsin ratio is 2,500:1 w/w to 10,000:1 w/w.
Fonslow teaches the technique of ultra-low concentration trypsin digestion (Figure 1a, arrow labeled “with 25,000:1 protein:trypsin ratio”) in which highly abundant proteins are digested and depleted, followed by a standard concentration trypsin digestion in which the remaining lower abundance proteins are digested (Figure 1a, arrow labeled “100:1 protein:trypsin”). Fonslow derives a formula to explain the protease digestion of proteins to peptides (paragraph bridging pages 54-55 and formula (2)). Fonslow teaches the parameters that control the digestion of proteins based on their abundance profiles and optimizes these parameters, which include the protein lysate concentration (units of mass/volume), trypsin concentration (units of mass/volume), and digestion depletion time (Supplementary Materials, bottom paragraph on page 24 and paragraph bridging pages 25-26).
It would have been obvious to a person of ordinary skill in the art before the effective filing date of the claimed invention to optimize by routine experimentation the ratio of protein to trypsin in Huang’s tryptic digest based upon the concentration of host cell proteins in Huang’s antibody preparation. The person of ordinary skill in the art would have been motivated to control the amount of digestion in order to maximize the number of detected host cell proteins. The person of ordinary skill in the art would have had a reasonable expectation of success given that Fonslow teaches the parameters that control protein digestion and also exemplifies two different protein:trypsin ratios that work for the enzymatic digestion of proteins with different abundance profiles (100:1 and 25,000:1 in Figure 1a).
Huang, Thakur, and Fonslow do not teach that the mass spectrometry is BoxCar MS (claims 1, 8-9, and 21).
Meier teaches BoxCar mass spectrometry (a data-acquisition method) and demonstrates its application in proteomics (Discussion, paragraph 3, line 1). Meier teaches that the sensitivity of BoxCar mass spectrometry is in the low atto-molar range (Abstract). Meier teaches that BoxCar MS does not require any changes to the instrument hardware (Discussion paragraph 1). Meier teaches optimizing the effect of acquisition parameters on the number of quantified peptide features during BoxCar MS (page 441, left column, bottom paragraph). Meier teaches that to achieve cycle times around 1 s for the full acquisition cycle of one full scan, BoxCar scans and data-dependent MS2 scans were limited to two or three per acquisition cycle (page 441, left column, bottom paragraph). Therefore, Meier teaches “two or more scans of BoxCar MS” (claims 8-9 and 21) as well as “two or more scans of mass spectrometry (MS), wherein at least one scan is BoxCar MS” (claim 1).
It would have been obvious to a person of ordinary skill in the art before the effective filing date of the claimed invention to apply Meier’s technique of BoxCar MS (a data-acquisition method for mass spectrometry) in order to improve the method of Huang modified by Thakur and Fonslow. One of ordinary skill would have been motivated by the high sensitivity. The results of the method of Huang, Thakur, and Fonslow modified by Meier would have been predictable, especially since the application of the BoxCar MS technique would not have required any changes to the mass spectrometry instrument hardware and would have represented only a change in data acquisition.
Pertaining to claim 2, Huang teaches identifying the contaminating proteins by size and sequence (page 5438, paragraph bridging left and right columns).
Pertaining to claim 3, Huang teaches that the amount of contaminating protein is on the order of less than 10 ppm (Table 4).
Pertaining to claim 22, Huang also detects contaminating proteins on the order of <0.5 ppm (Table 4). Meier teaches the detection of proteins on the order of attomoles as well as on the order of picomoles: “Protein abundance spanned more than six orders of magnitude and we estimated the amount of the 1,200 least abundant proteins to be < 10 attomoles” (see page 446, right column, paragraph 1, Figure 6c, and left chart of Supplementary Figure 8a). Therefore, the amount of contaminating protein that would have been detectable in the method of Huang modified by Thakur, Fonslow, and Meier would have been even less than the original method of Huang.
Pertaining to claims 5 and 10, Huang’s antibody is NIST monoclonal antibody standard RM 8670 (page 5441, right column “HCPs in NIST Monoclonal Antibody Standard RM 8670”), which is an antigen binding fragment.
Pertaining to claim 11, Huang’s contaminating proteins include cathepsin D (row 51 in Table 4).
Pertaining to claim 13, Huang does not teach the long gradient liquid chromatography comprises a 50 cm column and a gradient of 4 hrs.
Thakur teaches a column length of 50 cm and a gradient of 140 min or 480 min (Experimental Procedures, LC-MS Analysis, lines 1 and 5-6). Thakur compares the performance of the two different gradients (Figure 1).
It would have been obvious to a person of ordinary skill in the art before the effective filing date of the claimed invention to optimize by routine experimentation the gradient to achieve the desired peptide separation. The person of ordinary skill in the art would have had a reasonable expectation of success given that Thakur exemplifies gradients of both 140 min and 480 min and compares the performance of the two different gradients (Figure 1). The person of ordinary skill in the art would have been able to predict the effect of the gradient on the peptide separation based on Thakur’s teaching.
Regarding claims 19-20, Huang teaches removing the antibody from the sample by precipitation prior to analyzing the digested peptides by UPLC-MS/MS (page 5437, left column, second paragraph, page 5438, Results and Discussion, left column, second paragraph).
Claim 14 is rejected under 35 U.S.C. 103 as being unpatentable over Huang et al. (Analytical Chemistry 89.10 (2017): 5436-5444) in view of Thakur et al. (cited in the Non-Final Action mailed on 4/17/2023), Fonslow et al. (cited in the Non-Final Action mailed on 4/17/2023), and Meier et al. (cited in the Non-Final Action mailed on 4/17/2023), as applied to claims 1-5, 8-11, 13, and 19-22 above, further in view of Chen et al. (WO 2018/039499 Al; cited in the IDS filed on 4/3/2023).
See discussion of Huang, Thakur, Fonslow, and Meier above, which is incorporated into this rejection as well.
Pertaining to claim 14, Huang does not teach that the antibody is an anti-Ebola antibody, alirocumab, dupilumab, sarilumab, aflibercept, or rilonacept.
Chen teaches a method comprising digesting monoclonal antibody produced from RS001 CHO cells and injecting the digest into a reverse phase liquid chromatography column coupled to a triple quadrupole mass spectrometer (lines 3-5 of [00273]), thus quantifying the abundance of PLBD2 in the monoclonal antibody sample (lines 8-9 of [00273]). PLBD2 is a contaminating protein in the protein sample (see lines 1-5 of [00272]).
Chen teaches that the monoclonal antibody is selected from an anti-Ebola antibody, alirocumab, dupilumab, and sarilumab ([00172]) or an antibody fusion selected from aflibercept and rilonacept ([00173]).
It would have been obvious to a person of ordinary skill in the art before the effective filing date of the claimed invention to replace Huang’s monoclonal antibody standard with any of the monoclonal antibodies taught by Chen. The person of ordinary skill in the art would have been motivated to apply the improved method of Huang modified by Thakur, Fonslow, and Meier to commercially relevant products. The person of ordinary skill in the art would have had a reasonable expectation of success given the antibodies Chen teaches are also monoclonal antibodies.
Conclusion
Applicant's amendment necessitated the new ground(s) of rejection presented in this Office action. Accordingly, THIS ACTION IS MADE FINAL. See MPEP § 706.07(a). Applicant is reminded of the extension of time policy as set forth in 37 CFR 1.136(a).
A shortened statutory period for reply to this final action is set to expire THREE MONTHS from the mailing date of this action. In the event a first reply is filed within TWO MONTHS of the mailing date of this final action and the advisory action is not mailed until after the end of the THREE-MONTH shortened statutory period, then the shortened statutory period will expire on the date the advisory action is mailed, and any nonprovisional extension fee (37 CFR 1.17(a)) pursuant to 37 CFR 1.136(a) will be calculated from the mailing date of the advisory action. In no event, however, will the statutory period for reply expire later than SIX MONTHS from the mailing date of this final action.
Any inquiry concerning this communication or earlier communications from the examiner should be directed to CANDICE LEE SWIFT whose telephone number is (571)272-0177. The examiner can normally be reached M-F 8:00 AM-4:30 PM (Eastern).
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/LOUISE W HUMPHREY/Supervisory Patent Examiner, Art Unit 1657
/CANDICE LEE SWIFT/Examiner, Art Unit 1657
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