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
Claim status
Claims 1-31 are pending
Claims 20-22 are withdrawn
Claims 1-19, 23-31 are under examination
Election/Restrictions
Applicant’s election of the following species in the reply filed on 7/06/2026 is acknowledged.
Applicant elects an anion exchange chromatography step of Claims 16-19.
Applicant's election with traverse is acknowledged. The traversal is on the ground(s) that steps of anion exchange and cation exchange can occur sequentially.
This is not found persuasive because the examiner was able to provide art which satisfied the limitations of the anion exchange chromatography step, thereby demonstrating that the special technical feature lacks novelty. Therefore, a lack of unity exists between the restricted species.
The requirement is still deemed proper and is therefore made FINAL.
Claims 20-22 drawn to a cation exchange chromatography step are withdrawn from further consideration pursuant to 37 CFR 1.142(b) as being drawn to a nonelected species, there being no allowable generic claim.
Information Disclosure Statement
The information disclosure statement (IDS) submitted on 1/10/2024 is in compliance with the provisions of 37 CFR 1.97. Accordingly, the information disclosure statement is being considered by the examiner.
However, Applicant is reminded that the listing of references in the specification is not a proper information disclosure statement. 37 CFR 1.98(b) requires a list of all patents, publications, or other information submitted for consideration by the Office, and MPEP § 609.04(a) states, "the list may not be incorporated into the specification but must be submitted in a separate paper." Therefore, unless the references have been cited by the examiner on form PTO-892, they have not been considered.
Claim Objections
Claims 1-19 and 23-31 are objected to because of the following informalities: instant claims are replete with grammatical errors (e.g., Claim 1 “at a pH range” and “to capture the monoclonal antibody”). It is recommended the claims be checked by a native English speaker.
Claims 1, 4, 5, 6, 8, 10, 11 are objected to because of the following informalities: instant claim uses the abbreviations “CHO” and “AEX” hybrid filter, which has not been spelled out upon first use. Although claims are allowed abbreviations, if an abbreviation is not spellout upon first use in a claim, Applicant should only use abbreviations that would be clear to someone who had not read the invention description. As a related matter, Claims 4-6, 8, 10, 11 are object to for being inconsistent with their terminology using interchangeably “AEX-filtration” (no hybrid), “AEX-hybrid” (with hyphen), or “AEX hybrid” (no hyphen).
Claim 1, 12, 13, 14, 23, 25 are objected to because of the following informalities: instant claims use the term “Protein A” in step (c), yet uses the term “protein A” in step (d). Applicant should be consistent with capitalization. In addition, Claim 14 is further objected to as a related matter because instant claim capitalizes the term “Synthetic”.
Claim 24 is objected to because of the following informalities: instant claim is improperly marked twice as “(Original)”.
Appropriate correction is required.
Claim Rejections - 35 USC § 112(b)
The following is a quotation of 35 U.S.C. 112(b):
(b) CONCLUSION.—The specification shall conclude with one or more claims particularly pointing out and distinctly claiming the subject matter which the inventor or a joint inventor regards as the invention.
The following is a quotation of 35 U.S.C. 112 (pre-AIA ), second paragraph:
The specification shall conclude with one or more claims particularly pointing out and distinctly claiming the subject matter which the applicant regards as his invention.
Claims 1, 6, 9, 15, 17, 20, 25 are rejected under 35 U.S.C. 112(b) or 35 U.S.C. 112 (pre-AIA ), second paragraph, as being indefinite for failing to particularly point out and distinctly claim the subject matter which the inventor or a joint inventor (or for applications subject to pre-AIA 35 U.S.C. 112, the applicant), regards as the invention.
Claim 1 recites the broad recitation in step (c)(i) of “an affinity chromatography resin”, and the claim also recites “Protein A affinity chromatography” which is the narrower statement of the limitation.
Furthermore, Claim 1 recites the broad recitation in step (c)(ii) wherein elution in affinity chromatography is performed using a “pH range from 2.00 to 5.00 or a salt based gradient”, and the claim also recites eluting the captured antibody using a buffer in “pH range from 2.00 to 5.00 with conductivity more than 0.5 mS/cm” which is the narrower statement of the limitation. A broad range or limitation together with a narrow range or limitation that falls within the broad range or limitation (in the same claim) is considered indefinite, since the resulting claim does not clearly set forth the metes and bounds of the patent protection desired. See MPEP § 2173.05(c).
Claims 6 and 9 recite the limitation "to an affinity chromatography" in regard to the steps of claim 1. As a first matter, there is insufficient antecedent basis for this limitation in the claims because claim 1 is directed to “Protein A” affinity chromatography. As a second matter, the phrase "to an affinity chromatography" at the end of the claims is indefinite as to what step in the process the >0.5 mS/cm conductivity solution is being used for. Note that for claim 6 in particular, the AEX hybrid filtration step of claim 1 is followed by the diafiltration step, not the affinity chromatography step.
Claims 11 and 12 recite the broad recitation of “SPTFF and/or ILC”, and the claims also recites the inlet and outlet, respectively, of “both”, which is the narrower statement of the limitation. Again, a broad range or limitation together with a narrow range or limitation that falls within the broad range or limitation (in the same claim) is considered indefinite, since the resulting claim does not clearly set forth the metes and bounds of the patent protection desired. See MPEP § 2173.05(c).
Claim 15 contains the trademark/trade names MabSelect SuRe™, MabSelect SuRe™ LX, MabSelect SuRe™ pcc, MabSelect™ PrismA, Fibro PrismA, Praesto® Jetted A50, Amsphere™ A3, TOYOPEARL®, AF-rProtein A HC-650F, KANEKA KanCapA™, KANEKA KanCapA™ 3G, Eshmuno® A, Praesto® AP, and MabSpeed™ rP202, which refer to types of chromatography matrix.
Claim 17 contains the trademark/trade names DEAE Sepharose® Fast Flow, Q Sepharose® Fast Flow, SOURCE™ 15Q, SOURCE™ 30Q, Fractogel® EMD DEAE, POROS® 50 HQ, Nuvia™ Q, Capto™ ImpRes Q., Capto™ Q, Capto™ DEAE, Fractogel® EMD TMAE, Fractogel® EMD DMAE, Natrix® Q, Sartobind® Q, and Mustang® Q, which refer to types of anion exchange chomatography matrix.
Claim 20 contains the trademark/trade names Fractogel® EMD SO3- (M), Capto™ SP ImpRes, POROS® XS, Nuvia™ S, SOURCE™ 15S, SOURCE™ 30S, SP Sepharose® Fast Flow, Natrix® HD-Sb, Sartobind® S, and Mustang® S, which refer to types of cation exchange chomatography matrix.
Where a trademark or trade name is used in a claim as a limitation to identify or describe a particular material or product, the claim does not comply with the requirements of 35 U.S.C. 112(b) or 35 U.S.C. 112 (pre-AIA ), second paragraph. See Ex parte Simpson, 218 USPQ 1020 (Bd. App. 1982). The claim scope is uncertain since the trademark or trade name cannot be used properly to identify any particular material or product. A trademark or trade name is used to identify a source of goods, and not the goods themselves. Thus, a trademark or trade name does not identify or describe the goods associated with the trademark or trade name.
Claim 24 recites the broad recitation where the columns are “radial flow chromatography columns”, and the claims also recites the columns are selected from “axial or radial flow chromatography columns”, which is the broader statement of the limitation. Again, a broad range or limitation together with a narrow range or limitation that falls within the broad range or limitation (in the same claim) is considered indefinite, since the resulting claim does not clearly set forth the metes and bounds of the patent protection desired. See MPEP § 2173.05(c). In instant case, the claim is being interpreted as being directed to an axial flow column.
Claim 25 recites the limitation "anion exchange chromatography and cation exchange chromatography” in regard to the ion exchange chromatography step of claim 1. There is insufficient antecedent basis for these limitations in the claim. In light of the specification, and for the sake of compact prosecution, Claim 25 is being interpreted as being directed to ion exchange chromatography.
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 of this title, if the differences between the claimed invention and the prior art are such that the claimed invention as a whole would have been obvious before the effective filing date of the claimed invention to a person having ordinary skill in the art to which the claimed invention pertains. Patentability shall not be negated by the manner in which the invention was made.
The factual inquiries set forth in Graham v. John Deere Co., 383 U.S. 1, 148 USPQ 459 (1966), that are applied for establishing a background for determining obviousness under 35 U.S.C. 103 are summarized as follows:
1. Determining the scope and contents of the prior art.
2. Ascertaining the differences between the prior art and the claims at issue.
3. Resolving the level of ordinary skill in the pertinent art.
4. Considering objective evidence present in the application indicating obviousness or nonobviousness.
This application currently names joint inventors. In considering patentability of the claims the examiner presumes that the subject matter of the various claims was commonly owned as of the effective filing date of the claimed invention(s) absent any evidence to the contrary. Applicant is advised of the obligation under 37 CFR 1.56 to point out the inventor and effective filing dates of each claim that was not commonly owned as of the effective filing date of the later invention in order for the examiner to consider the applicability of 35 U.S.C. 102(b)(2)(C) for any potential 35 U.S.C. 102(a)(2) prior art against the later invention.
Claims 1-19, 23-27, and 29-31 are rejected under 35 U.S.C. 103 as being unpatentable over Keszey et al., (US Patent 12,600,748, filed 3/25/2020, patented 4/14/2026), in view of Arunkumar et al. (US2021/0253633, filed 6/06/2019, published 8/19/2021, see WIPO document cited in Applicant’s IDS)
Kesey claims a process for purifying an immunoglobulin comprising the steps of:
Depth filtration of a cell harvest material containing the antibody, followed by
Microfiltration/(b’) Diafiltration, followed by,
Protein A affinity chromatography (see claims 1, 6, and 7 of Keszey).
Note in regard to step (b), Keszey suggests a step (b’) to treat the sample prior to the affinity chromatography step by concentrating the sample by diafiltration, so as to adjust the supernatant to a specific immunoglobulin concentration, range of pH, conductivity, and buffer (col 9, 1st para.).
In regard to remainder of the steps (d) through (g), Keszey claims the method for purifying the immunoglobulin comprises the steps as defined in claim 1, and comprising oner or more further steps following the Protein A affinity chromatography selected from the groups consisting of (d) Viral inactivation, (e) Ion exchange chromatography, (f) Ultrafiltration/diafiltration, (g) Nanofiltration (claim 10 of Keszey).
However, Keszey is silent to a preferred embodiment of a method for producing a purified immunoglobulin according to steps (a)-(g) in that order.
Nevertheless, it would have been obvious to one having ordinary skill in the art at the time the invention was filed to practice said method to produce a purified immunoglobulin from cells because each of the individual elements of the instant claims are independently presented by Keszey as embodiments and are taught that they can be combined in various embodiments; therefore a combination of all the elements into a single embodiment would be apparent to an artisan skilled in antibody production in light of the Supreme Court’s KSR decision (see MPEP 2143 Exemplary Rationale (A)). Regarding the rationale for combining prior art elements according to known methods to yield predictable results, all of the claimed elements were known in the prior art and one skilled in the art could have combined the element as claimed by known methods with no change in their respective functions, and the combination would have yielded predictable results to one of ordinary skill in the art at the time of filing of the invention. Each of the following elements: (a) Depth filtration, (b) Diafiltration-TFF, (c) Protein A chromatography, (d) Viral inactivation, (e) Ion exchange chromatography, (f) Ultrafiltration/diafiltration, and (g) Nanofiltration, buffers and formulations are taught by Keszey and further they are taught in various combinations and are shown to be used in a method for producing purified immunoglobulins from cells. Furthermore, in regard to the order of the steps, as stated supra, Keszey suggests the order of (a) Depth filtration, (b) Diafiltration-TFF, (c) Protein A chromatography, which are followed by (d) Viral inactivation and (e) Ion exchange chromatographies (see Fig. 1 of Keszey). In regard to (f) Ultrafiltration/diafiltration followed by (g) Nanofiltration, Keszey teaches the nanofiltration steps for viral filtration are usually performed as the end (col 28, 3rd para.), and that viral removal is necessary because of accidental contamination from raw [AltContent: textbox ([img-media_image1.png])]materials or production steps (col 30, lines 54-62). It would have been therefore predictably obvious to use a combination of these steps (a) to (g) in that order in said method (see modified Fig. 1 of Keszey adjacent). See also, Ex parte Rubin, 128 USPQ 440 (Bd. App. 1959) (Prior art reference disclosing a process of making a laminated sheet wherein a base sheet is first coated with a metallic film and thereafter impregnated with a thermosetting material was held to render prima facie obvious claims directed to a process of making a laminated sheet by reversing the order of the prior art process steps.). See also In re Burhans, 154 F.2d 690, 69 USPQ 330 (CCPA 1946) (selection of any order of performing process steps is prima facie obvious in the absence of new or unexpected results); In re Gibson, 39 F.2d 975, 5 USPQ 230 (CCPA 1930) (Selection of any order of mixing ingredients is prima facie obvious.).
In regard to the preamble of claim 1, Keszey teaches the type of immunoglobulin to purified in a monoclonal antibody (col 12, line 32).
In regard to step (a) of claim 1, Keszey teaches the cells used to express the antibody are CHO cells (col 6, lines 58-59, col 32, Examples 1 & 2), and the depth filter to be used is an AEX hybrid filter from 3M (col 27, lines 30-32, Example 5, col 41, line 17).
In regard to step (b) of claim 1, Keszey teaches the filtration steps are performed via a tangential flow filtration (TFF) system (col 28, 1st para., col 48, Example 8.8). However, Keszey is silent to a single pass tangential flow filtration system.
In regard to step (b) of claim 1, Arunkumar et al. (US2021) teaches the diafiltration steps for concentrating monoclonal antibodies are performed with a series of single-pass tangential flow filtration (SPTFF) devices ([0050-0052] Behavior of Completely Retained Proteins (Mabs) Using SPTFF, [0071-0075, 0086-0092] Examples 1 & 4, see Claim 1, 4, and 12 of Arunkumar).
Accordingly, it would have been prima facie obvious to one of ordinary skill in the art at the time of filing to substitute the standard TFF step (b) of claim 1, as taught by Keszey for a SPTFF step as taught by Arunkumar with a reasonable expectation of success. The ordinary skilled artisan would have been motivated to do so as taught by Arunkumar because compared to conventional TFF systems, the use of SPTFF exhibited a much lower sieving coefficient ([0065-0066], Example 2, [0081] of Example 3), which would keep more of the large monoclonal antibody in the retentate while letting the small contaminants, salts, or water pass through.
In regard to step (c) of claim 1, Keszey teaches the step (c)(i) the loading of the monoclonal antibody to the protein A affinity resin in a 20 mM Tris-acetated buffer at pH 7.2, which would have a conductivity of between 1.1-1.3 mS/cm at room temperature (col 46, 1st para.). In regard to the amount loaded relative to breakthrough capacity, Keszey discloses that approximately 1.5 mg/ml IgG are loaded onto the Protein A resins and approximately 17 mg/ml IgG are eluted (col 44, Table 9a/b), and since the breakthrough capacity of protein A resin are in the range of 20-40 mg/ml, Keszey appears to have loaded greater than 0.1% of the breakthrough capacity. In regard to step (c)(ii), Keszey teaches the elution buffer in a 100 mM Na-citrate at pH 3.5, which would have a conductivity of about 5 mS/cm at room temperature (col 46, 1st para.).
In regard to step (d) of claim 1, as stated supra, Keszey teaches subjecting the elution form the Protein A chromatography to Viral inactivation, which occurs in the low pH elution buffer (col 30-31, Virus Inactivation).
In regard to step (e) of claim 1, as stated supra, Keszey teaches subjecting the post-viral inactivated liquid to at least one ion exchange chromatography step. Specifically, Keszey teaches the pH is raised after the virus inactivation step for subsequent ion exchange (col 31, lines 6-8).
In regard to step (f) of claim 1, as stated supra, Arunkumar et al. (US2021) makes obvious the diafiltration steps for concentrating monoclonal antibodies are performed with a series of SPTFF devices.
In regard to step (g) of claim 1, as stated supra, Keszey teaches the nanofiltration steps for viral filtration are performed as the end to remove any accidental contamination during the production steps.
In regard to claims 2 and 3, Keszey suggest continuous processing between devices such as the direct connections between the AEX hybrid depth filter and the Protein A affinity chromatography device (col 5, 3rd para.), as well as between the Protein A affinity chromatography device and the viral inactivation tank (col 42, 2nd para.). Furthermore, Arunkumar teaches continuous bioprocessing is the workhorse of the biopharma industry [0004, 0005, 0066].
Accordingly, it would have been prima facie obvious to one of ordinary skill in the art at the time of filing to practice continuous immunoprocessing as suggested by Keszey in view of Arunkumar with a reasonable expectation of success. The ordinary skilled artisan would have been motivated to do so as taught by Arunkumar because continuous bioprocessing improves capacity, selectivity, uniformity in product quality, and reduces cost [0004, 0005].
In regard to claims 4-6, as stated supra, Keszey teaches at least one depth filtration step using the AEX hybrid filter. Specifically in regard to claim 5, Keszey teaches filtration steps using “depth filters” (col 2, line 40), and explicitly discloses “one or more depth filtration steps” (col 27, 3rd para.), and the mere duplication of essential working parts of a device involves only routine skill in the art (see MPEP 2144.04VI(B)). Specifically in regard to claim 6, as stated supra, Keszey teaches the depth filtration step occurs after the cell harvesting and centrifugation of a flocculating agent from the culture media (col 5, step (a), col 6 step (b), col 8, Fig. 2A, legend, col 17, lines 41-51), thus the AEX hybrid filtration was performed in a standard culture media of about pH 7 and conductivity of more than 0.5 mS/cm.
In regard to claims 7-9, as stated supra, Arunkumar teaches that the SPTFF units are “in-series” [0033], and are operated with suitable residence times to achieve a continuous processing mode ([0005-0006], Background), and typically operate with a buffer at pH 7.2 and conductivity of more than 0.5 mS/cm ([0071] of Example 1).
In regard to claim 10, as stated supra, Arunkumar teaches that the SPTFF units are in series, while Keszey teaches at least one AEX hybrid filter.
In regard to claims 11-12, as stated supra, Keszey teaches direct connections between units, and Arunkumar teaches the advantages of continuous processing by connected units.
In regard to claims 13-15, Keszey teaches the Protein A chromatography step using MabSelect SuRe LX immobilized resin (col 41, line 3).
In regard to claims 16-19, Keszey teaches the ion exchange step comprising anion exchange using quaternary-ammonium resin such as CAPTO® Q (col 25, 5th para., to col 26, 2nd para., Polishing Chromatography Step: Anion Exchange Chromatography). In regard to claim 18, Keszey teaches the buffer for the CAPTO® Q resin is 25 mM Tris at pH 8, which would have a conductivity of about 1.4 mS/cm at room temperature (col 27, 1st para., col 47, last para.).
In regard to claims 23-24, Keszey teaches a simple cylindrical column packed with the Protein A resin (col 46, 1st para.), and an ion exchange resin packed by the user into a column with the usual dimensions (col 25, lines 41-47). In these cases, it appears Keszey is using the standard axial flow column (as these are the routine and conventional column design as a simple cylinder). Furthermore, from the genus of just two options, it would have been obvious for the affinity chromatography and ion exchange steps to use the axial flow columns.
In regard to claim 25, Keszey teaches flow rate through the Protein A column was 210 cm/hr (col 46, 1st para.), and since the column was at least 10 cm, there was a retention time of at least 15 sec for this step alone. Thus, the cumulative residence time for both the Protein A affinity chromatography and ion exchange chromatography would have been greater than 15 seconds.
In regard to claim 26, Arunkumar teaches that the SPTFF process exhibits a volumentric concentration factor of at least 1.1X (i.e., between 12X to about 80X) for the different mAbs ([0011, 0019, 0092], see Fig. 6).
In regard to claim 27, Arunkumar teaches that the SPTFF process produces a final high titer monoclonal antibody up to 243+/-40 g/L (Table 6). Furthermore, Keszey teaches the processing steps are relatively rapid, and indicates an acceptable time window of 8 hours for routine production (col 40, 2nd para.). Thus, Keszey in view of the SPTFF process of Arunkumar reasonably suggests the process yields monoclonal antibodies at about 30+/-5 g/L/hour. It would have been obvious to one having ordinary skill in the art at the time the invention was filed to conduct the process of Keszey in view of Arunkumar to yield 25.59 g/L/H. Notably, in the case where the claimed value "lie inside ranges disclosed by the prior art" a prima facie case of obviousness exists. In re Wertheim, 541 F.2d 257, 191 USPQ 90 (CCPA 1976); In re Woodruff, 919 F.2d 1575, 16 USPQ2d 1934 (Fed. Cir. 1990). It is routine procedure to optimize component amounts to arrive at an optimal product that is superior for its intended use, since it has been held where the general conditions of a claim are disclosed in the prior art, discovering the optimum or workable values involves only routine skill in the art. See M.P.E.P. §2144.05.
In regard to claim 29, Keszey teaches that after the Protein A chromatography step, the residual host cell protein (HCP) concentrations were as low as 160 ppm, yet she indicates the need for further polishing steps, at least in case of a therapeutic monoclonal antibody for human use (col 44, lines 45-50). It would have been obvious to one having ordinary skill in the art at the time the invention was filed to lower the HCP concentration to less than 100 ppm, since it has been held that where the general conditions of a claim are disclosed in the prior art, discovering the optimum or workable ranges involves only routine skill in the art. In re Aller, 105 USPQ 233.
In regard to claim 30, Keszey teaches that after an initial pDADMAC pre-clearing step, the contaminating host cell DNA (HCDNA) is already below 10 ng/ml (col 36, Table 4a), and by the Protein A affinity chromatography step is complete, no HCDNA is detected (col 44, Table 9a). Thus the purified monoclonal antibody would have no more than 10 gn/mL DNA.
In regard to claim 31, Keszey teaches the monoclonal antibody is an IgG (see Bevacizumab IgG1 of Example 2, Denosumab IgG2 of Example 6, col 42)
Hence, the claimed invention as a whole was prima facie obvious in the absence of evidence to the contrary.
Claim 28 is rejected under 35 U.S.C. 103 as being unpatentable over Keszey et al., (US Patent 12,600,748, filed 3/25/2020, patented 4/14/2026), in view of Arunkumar et al. (US 2021/0253633, filed 6/06/2019, published 8/19/2021), as applied to claims 1 and 3, in further view of Shadle et al. (US Patent 5,429,746, filed 2/22/1994, patented 7/04/1995, see IDS filed 1/10/2024)
As discussed previously, Keszey and Arunkumar suggest a process for purifying a monoclonal antibody comprising the steps of (a) Depth filtration with an AEX hybrid filter, (b) Diafiltration by SPTFF, (c) Protein A chromatography, (d) Viral inactivation, (e) Ion exchange chromatography, (f) a second diafiltration by SPTFF(II) and (g) Nanofiltration of viral contamination to produce the purified monoclonal antibody.
However, although Keszey teaches a mixed-mode anionic/hydrophobic chromatography step that removes product aggregates (col 47, 2nd para.), they are silent to there being less than 0.3% soluble aggregates.
With respect to claim 28, Shadle teaches a process for purifying a IgG antibody comprising Protein A affinity chromatography, viral inactivation, ion exchange and diafiltration steps, wherein a hydrophobic column is used to separate IgG monomers from soluble aggregates (col 3, Brief Description of the Invention, see also Fig. 1). Specifically, Shadle teaches that purified IgG contains as little as 0.06% aggregates (col 21, Table 9).
Accordingly, it would have been prima facie obvious to one of ordinary skill in the art at the time of filing to prepare the monoclonal antibody as suggested by Keszey and Arunkumar, and combine a hydrophobic column to achieve below 0.3% soluble aggregates as taught by Shadle with a reasonable expectation of success. The ordinary skilled artisan would have been motivated to do so as taught by Shadle for the purposes of product purity and standardization the monomeric species should be separated from the higher molecular weight aggregates and other misfolded forms of the IgG (col 5, last para.).
Hence, the claimed invention as a whole was prima facie obvious in the absence of evidence to the contrary.
Conclusion
No claims are allowed.
Examiner Contact Information
Any inquiry concerning this communication or earlier communications from the examiner should be directed to ARTHUR S LEONARD whose telephone number is (571)270-3073. The examiner can normally be reached on Mon-Fri 9am-5pm.
If attempts to reach the examiner by telephone are unsuccessful, the examiner’s supervisor, James Doug Schultz can be reached on 571-272-0763. The fax phone number for the organization where this application or proceeding is assigned is 571-273-8300.
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/ARTHUR S LEONARD/Examiner, Art Unit 1631
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