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
Applicant’s response filed on 07/30/2025 is duly acknowledged.
Claims 1-16, as presented on 03/16/2023 are currently pending in this application.
Change in Examiner
Applicants are advised that the assigned Examiner for this application has changed. All future communications regarding this application should be addressed to the new Examiner, Satyendra K. Singh, Art Unit 1657 (phone: 571-272-8790).
Election/Restrictions
Applicant’s election without traverse of Group VI (claims 8 and 9; directed to “An oxalate oxidase composition…”) in the reply filed on 07/30/2025 (see applicant’s remarks on second page, in particular with a request for rejoinder) is acknowledged. Regarding the request for re-joinder of groups V and VII, as noted in the previous office action (CTRS, paper dated 06/05/2025, page 3), once the product claims are found to be allowable, such re-joiner of withdrawn method claims (that require all the limitations of the allowable product) would be duly considered by the examiner.
It is also noted that applicant’s election of species from claims 12-13 and 15 (see REM, page 3) are not deemed to be pertinent because applicants have elected Group VI (claims 8-9) for examination that does not correspond to claims 12-13 and 15 (i.e. within non-elected inventions of Groups VII-VIII).
Claims 1-7 and 10-16 (non-elected inventions of Groups I-V and VII-VIII) have been withdrawn from further considerations.
Claims 8 and 9 (elected invention of Group VI, without traverse; directed to “An oxalate oxidase composition…”) have been examined on their merits in this office action, hereinafter.
Priority
This application claims domestic benefit from a US PRO 63/320,627 filed on 03/16/2022.
Objections to Specification
The disclosure is objected to because it contains an embedded hyperlink and/or other form of browser-executable code (see instant specification, for instance, page 15, 4th line; page 22, section 6d; pages 28-29, citations 12, 15, 22 and 23). Applicant is required to delete the embedded hyperlink and/or other form of browser-executable code; references to websites should be limited to the top-level domain name without any prefix such as http:// or other browser-executable code. See MPEP § 608.01. Appropriate correction is required.
Claims
Instant claims, as currently recited, have been interpreted as product-by-process claims (see entire instant specification regarding “Oxalate Oxidase” on page 9, [0041]-[0044], for instance).
"[E]ven though product-by-process claims are limited by and defined by the process,
determination of patentability is based on the product itself. The patentability of a product
does not depend on its method of production. If the product in the product-by-process
claim is the same as or obvious from a product of the prior art, the claim is unpatentable
even though the prior product was made by a different process." In re Thorpe, 777
F.2d 695, 698, 227 USPQ 964, 966 (Fed. Cir. 1985)
Claim Rejections - 35 USC § 112
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.
1. Claims 8 and 9 (as recited) 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 8 has been reproduced below:
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It is to be noted that instant claim 8 recites the limitations of “a specific activity of at least about 9 enzyme units per 100 g of starting leaves”, wherein the term “starting leaves” of “American chestnut tree plants expressing wheat oxalate oxidase” has not been specifically defined by the applicants (see instant specification, page 9, for instance). Applicants have stated that “A unit of OxOx activity is defined as “micromoles of substrate degraded per minute” (it is not clear as to how many micromoles of substrate has to be degraded per minute to represent “one unit” of activity per se; see SPEC, page 9, [0042]), whereas the “specific activity” of an enzyme is generally expressed in the art as a measure of enzyme activity per unit mass or weight of the total enzyme protein, the activity being the amount of product formed (or substrate converted) per unit of time. However, in the instant case, the “amount/weight of enzyme” preparation is being termed as being equivalent to the weight of the source tissue expressing said enzyme (i.e. the host tissue, or leaves of American chestnut tree expressing said enzyme), wherein it is unclear as to what exactly is being considered as “starting leaves” of “American chestnut tree plants expressing wheat oxalate oxidase”. Although, applicants can be their own lexicographer, they must clearly set forth a special definition of a claim term in the specification that differs from the plain and ordinary meaning it would otherwise possess (see MPEP 211.01(iv)). Thus, to a person of ordinary skill in the art, the metes and bounds of the claimed activity for the enzyme “wheat oxalate oxidase’ expressed in the American chestnut tree (ACT) leaves (as a host tissue; i.e. the product-by-process as claimed) is not deemed to be properly defined.
Since, the dependent claim 9 does not clarify this point, it is also rejected as being indefinite for the same reasons as discussed above. Appropriate correction and/or explanation is required.
Claim Rejections - 35 USC § 101
35 U.S.C. 101 reads as follows:
Whoever invents or discovers any new and useful process, machine, manufacture, or composition of matter, or any new and useful improvement thereof, may obtain a patent therefor, subject to the conditions and requirements of this title.
1. Claims 8 and 9 (as presented) are rejected under 35 U.S.C. 101 because the claimed invention is directed to a judicial exception without significantly more. The claims recite judicial exceptions in the form of natural product (i.e. product of nature, an enzyme composition comprising “oxalate oxidase”, naturally existing wheat plant-derived product; see discussion below) as depicted below:
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The claimed product is interpreted as a composition comprising wheat oxalate oxidase (OxOx) enzyme preparation (that has been expressed in American chestnut tree (ACT) leaves) obtained “after extraction” process, as recited in claims 8 and 9 (see 112-b rejection above regarding the “specific activity” recited in claim 8).
The aforementioned judicial exception has not been integrated into any meaningful practical application(s), and the instant claims do not include additional elements that are sufficient to amount to significantly more than the judicial exception itself (see also dependent claim 9). The analysis under 35 UCS 101 guide lines (USPTO October, 2019) is as follows:
Step 1. Does the claim fall within any of the statutory categories ?
Under BRI in light of the disclosure of record (see instant specification, [0003], [0006], [0011]-[0012], [0041]-[0044], for instance), instant claims 8 and 9 are directed to a composition of matter- in the form of an enzyme composition, presumably extracted from ACT leaves (that expresses wheat oxalate oxidase enzyme; which has a known and disclosed amino acid sequence set forth in SEQ ID NO. 1; see disclosure in the instant specification, page 9, [0043]-[0044]), that falls under the statutory category of products or composition of matter.
Step 2A. (Prong one)- Does the claim recite a judicial exception ?
Claims 8 and 9, as currently presented, specifically pertains to plant-derived enzyme composition (i.e. nature-based product) in the form of wheat oxalate oxidase (obtained by extracting ACT leaves that express said enzyme using sodium dodecyl sulfate, an ionic detergent, and ammonium sulfate fractionation to precipitate/purify said enzyme) having a “specific activity of at least about 9 enzyme units per 100g of starting leaves” of the ACT. It is to be noted that applicant’s own disclosure provides the evidence of the fact that the extracted product composition having aforementioned activity has the same amino acid sequence (SEQ ID NO: 1; see instant specification, [0044]) as already known in the prior art by Dratewka-Kos et al, 1989 (also cited in applicant’s IDS dated 12/04/2023, NPL citation no. 9), albeit as wheat “germin”.
See the sequence homology search result below:
SEQ ID NO: 1 (Database PIR) - SEQUENCE HOMOLOGY SEARCH
RESULT 1
A33268
germin precursor - wheat
C;Species: Triticum aestivum (common wheat)
C;Date: 22-Nov-1989 #sequence_revision 22-Nov-1989 #text_change 09-Jul-2004
C;Accession: A40391; A33268
R;Lane, B.G.; Bernier, F.; Dratewka-Kos, E.; Shafai, R.; Kennedy, T.D.; Pyne, C.; Munro, J.R.; Vaughan, T.; Walters, D.; Altomare, F.
J. Biol. Chem. 266, 10461-10469, 1991
A;Title: Homologies between members of the germin gene family in hexaploid wheat and similarities between these wheat germins and certain Physarum spherulins.
A;Reference number: A40391; MUID:91244822; PMID:2037593
A;Accession: A40391
A;Status: preliminary
A;Molecule type: DNA
A;Residues: 1-224 <LAN>
A;Cross-references: UNIPROT:P15290; UNIPARC:UPI000012B3CB; GB:M63223; NID:g170697; PIDN:AAA34270.1; PID:g170698
A;Note: clone gf-3.8
R;Dratewka-Kos, E.; Rahman, S.; Grzelczak, Z.F.; Kennedy, T.D.; Murray, R.K.; Lane, B.G.
J. Biol. Chem. 264, 4896-4900, 1989
A;Title: Polypeptide structure of germin as deduced from cDNA sequencing.
A;Reference number: A33268; MUID:89174765; PMID:2925674
A;Accession: A33268
A;Status: preliminary
A;Molecule type: mRNA
A;Residues: 1-224 <DRA>
A;Cross-references: UNIPARC:UPI000012B3CB; GB:M21962; NID:g170693; PIDN:AAA34268.1; PID:g170694; GB:J04592
C;Superfamily: germin
Query Match 100.0%; Score 1150; Length 224;
Best Local Similarity 100.0%;
Matches 224; Conservative 0; Mismatches 0; Indels 0; Gaps 0;
Qy 1 MGYSKTLVAGLFAMLLLAPAVLATDPDPLQDFCVADLDGKAVSVNGHTCKPMSEAGDDFL 60
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 1 MGYSKTLVAGLFAMLLLAPAVLATDPDPLQDFCVADLDGKAVSVNGHTCKPMSEAGDDFL 60
Qy 61 FSSKLAKAGNTSTPNGSAVTELDVAEWPGTNTLGVSMNRVDFAPGGTNPPHIHPRATEIG 120
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 61 FSSKLAKAGNTSTPNGSAVTELDVAEWPGTNTLGVSMNRVDFAPGGTNPPHIHPRATEIG 120
Qy 121 IVMKGELLVGILGSLDSGNKLYSRVVRAGETFLIPRGLMHFQFNVGKTEASMVVSFNSQN 180
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 121 IVMKGELLVGILGSLDSGNKLYSRVVRAGETFLIPRGLMHFQFNVGKTEASMVVSFNSQN 180
Qy 181 PGIVFVPLTLFGSNPPIPTPVLTKALRVEARVVELLKSKFAAGF 224
||||||||||||||||||||||||||||||||||||||||||||
Db 181 PGIVFVPLTLFGSNPPIPTPVLTKALRVEARVVELLKSKFAAGF 224
Notwithstanding the recitation of an amount of specific activity in claim 8, and the extraction and fractionation steps (i.e. 30% and 60% ammonium sulfate cuts), it is clear that the claimed composition is essentially a nature-based product composition. No disclosed genetic modifications and/or variations, substitutions in amino acids (i.e. mutational changes, for instance), deletion, additions, etc., have been provided in order to distinguish the OxOx enzyme from the naturally occurring wheat OxOx enzyme having the same characteristic structural-functional features, i.e. physical form as hexamer and the oxalate-degrading enzymatic activity (see applicant’s own disclosure on page 9, [0042]). Thus, the product as claimed is not markedly different or possess any distinct structural features and/or characteristics than the naturally existing wheat oxalate oxidase enzyme per se. It is to be noted that cloning and/or heterologous expression of a natural gene in order to obtain (i.e. using isolation/fractionation, etc.) a naturally occurring protein product in a host (such as American chestnut tree plants, and plant parts thereof) does not in itself constitute imparting markedly different characteristics on the protein product per se (see disclosure of Zhang et al, 2013 for cloning and expressing the wheat OxOx enzyme in American chestnut tree, and leaf bioassay for measuring its activity in vivo; see Abstract and page 975, section “Leaf assay”; also cited by applicants in IDS dated 12/04/2023, NPL citation no. 28; and instant disclosure [0042], for instance). Likewise, the steps of extraction and/or concentration using appropriate isolation/purification steps do not in essence impart any structural difference in the structure/function of the polypeptide and/or amino acid sequence of the wheat OxOx enzyme protein, which still remains the same, i.e. a nature-based product, or preparation thereof. Since, instant claims 8 and 9, as currently presented, are directed solely to a nature-based product composition (that do not recite any markedly different structural features and/or characteristics than the product existing in nature), they are deemed to recite a judicial exception.
Step 2A. (Prong two)- Does the claim as a whole integrates the recited judicial exception into a practical application of the exception ?
As currently presented, none of the claims 8 and 9 recite any structural and/or functional features or any additional limitations (other than specific activity and extraction-fractionation steps) that would provide and/or integrate the recited nature-based judicial exception into a meaningful practical application of the wheat oxalate oxidase enzyme composition, as claimed. No practical application of the nature-based product has been recited with specificity in the claims, and therefore, the claims as a whole do not integrate the judicial exception to a practical application of the exception, and therefore are directed to the nature-based judicial exception.
Step 2B. Does the claim as a whole amounts to significantly more than the recited exception ?
As discussed above, instant claims 8 and 9 do not recite any other structural and/or functional features, and/or provide any other limitation(s) that amount to “significantly more” than the recited judicial exceptions itself. As noted before, the steps of extraction, and/or fractionation using ammonium sulfate precipitation as recited in claims would be taken by an artisan of ordinary skill in the art as being routine steps required in order to obtain plant-based enzyme protein (as evidenced by the disclosure form Mans et al, US 5,776,701 (cited USPAT in applicant’s IDS dated 12/04/2023; see disclosure for stepwise fractionation of barley oxalate oxidase enzyme using ammonium sulfate; see Abstract, column 6, 2nd paragraph, and claims 1-10, for instance). Moreover, such extraction/fractionation steps do not materially change the structure/function of the wheat oxalate oxidase enzyme per se, i.e. does not make it non-natural. No evidence has been provided on record to show that the wheat OxOx enzyme obtained as per claims is structurally any different than the naturally occurring wheat oxalate oxidase enzyme protein. In fact, it is evidenced by applicant’s own disclosure that states the following (see specification [0042], reproduced in part):
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It is clear that the enzyme obtained by the applicant is structurally and functionally the same as its naturally occurring counter-part (i.e. as it is expressed in wheat plant). Thus, taken as a whole, instant claims 8 and 9 are deemed to be patent ineligible for reciting nature-based product as a judicial exception, for the reasons discussed above.
Appropriate correction is required.
Claim Rejections - 35 USC § 103
NOTE: 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.
1. Claims 8 and 9 (as presented) are rejected under 35 U.S.C. 103 as being unpatentable over Zhang et al (2013; NPL cited in IDS dated 12/04/2023, citation No. 28) taken with Mans et al (1998; US 5,776,701 A; USPAT cited in IDS dated 12/04/2023, citation no. 1) and Zhou et al (1998; NPL cited as ref. [U] on PTO 892 form).
Claims 8 and 9 as recited have been reproduced hereinbelow:
“8. An oxalate oxidase composition having a specific activity of at least about 9 enzyme units per 100 g of starting leaves of American chestnut tree plants expressing wheat oxalate oxidase after extraction in the presence of 0.1 % sodium dodecyl sulfate at 60°C and ammonium sulfate precipitation.”
“9. The oxalate oxidase composition according to claim 8 wherein said oxalate oxidase is produced according to a process comprising the steps of preparing an extract from leaves of American chestnut tree plants expressing wheat oxalate oxidase, wherein the extract is prepared in the presence of 0.1 % sodium dodecyl sulfate at 60°C, precipitating proteins in said extract by bringing said extract to at least about 30% saturation (w/v) with ammonium sulfate, removing said precipitated proteins and bringing said extract to at least about 60% (w/v) saturation with ammonium sulfate to precipitate said oxalate oxidase present in said extract and recovering said oxalate oxidase.”
Claims have been taken as reciting a product-by-process (see also 112b rejection as discussed above regarding term “starting leaves”).
Zhang et al (2013), while teaching a threshold level of wheat oxalate oxidase (termed as Oxo) transgene expression in American Chestnut tree (ACT) leaves effective for reducing fungus-induced necrosis as measured using a leaf bioassay (see Abstract, Introduction on page 974, and “Materials and methods” on pages 974-975), disclose the composition comprising leaves of ACT having expressed wheat oxalate oxidase enzyme (see section “Results” on page 976, entire left column), wherein a threshold level of expression in five transgenic ACT samples were able to reduce the fungus-induced lesions to the same level as the blight-resistant species of the ACT (see Abstract, Fig. 1 on page 977, for instance) due to the expressed enzyme activity of wheat Oxo in said leaves (see Fig. 4 on page 980; page 981, left column, 1st and 2nd paragraphs, for instance). Although, they disclose variable levels of expression of wheat Oxo enzyme in leaves of ACT, and do not measure the activity in terms of “units per 100 g of starting leaves”, they nevertheless disclose the composition comprising active wheat oxalate oxidase enzyme that has been expressed in leaves of American Chestnut tree plants.
Zhang et al do not disclose composition comprising wheat oxalate oxidase that has been extracted using sodium dodecyl sulfate (SDS) treatment and ammonium sulfate fractionation steps, as currently recited in instant claims 8 and 9.
Mans et al (1998), while teaching materials and methods used for detecting oxalate (see Title, Abstract, and Claims on columns 11-12), disclose the process for preparing oxalate oxidase composition from germinated barley seeds, wherein the process utilizes the steps of heat extraction followed by ammonium sulfate precipitations using the 30% and 60% cutoff concentrations (see claims 1, 7-10, for instance) in order to obtain oxalate oxidase preparation; wherein said enzyme preparation can comprise a “specific activity of at least about 10 enzyme units per milligram of protein” after ammonium sulfate precipitation (see Table 1 on page 9; claim 8, for instance); wherein the “enzyme yield is in the range of about 0.5 to 0.9, or greater, enzyme units per gram of plant tissue” (i.e. more than 50-90 units per 100g plant tissue; see column 6, 2nd -4th paragraphs, for instance). However, Mans et al do not disclose the use of SDS for extracting the oxalate oxidase enzyme protein from plant tissues.
Zhou et al (1998), while characterizing the oxalate oxidase from barley plant leaves (see Title, Abstract, and introduction on page 33, right column, in particular), disclose the art-known fact that “Oxalate oxidases are known from a number of plant, fungal, and bacterial species (Pundir, 1991). Of these, only the wheat and barley enzymes have been classified as germin-like oxalate oxidases (Dumas et al., 1993; Lane et al., 1993)….The germin-like oxalate oxidases are homo-oligomeric, water-soluble, heat-stable, protease-resistant, SDS-tolerant glycoproteins originally known to be expressed in cell walls of cereal embryos at the onset of germination (Lane, 1994).” (see page 33, right column, 1st-2nd paragraphs; and page 34, section “Protein Purification, Preparation of Antibodies, and Amino Acid Sequencing”; and cited reference of Zhang et al, 1996 therein); wherein oxalate oxidase are known in the art to be SDS tolerant enzymes. Although, Zhou et al do not disclose the use of SDS for extraction of the oxalate oxidase enzyme protein from barley leaves, they nevertheless clearly suggest the fact that oxalate oxidases are known in the art as SDS-tolerant glycoproteins (as shown by SDS-PAGE gel assays for activity determinations in the cited prior art of Zhang et al, 1996 therein).
Thus, to a an artisan of ordinary skill in the art, it would have been obvious to extract the wheat oxalate oxidase enzyme protein from the leaves of ACT plant using SDS treatment as suggested implicitly in the cited prior art of Zhou et al using the steps for concentrating with ammonium sulfate fractionations as already disclosed by mans et al, albeit for the oxalate oxidase from barley plant tissue. Since, the OxOx is known to be generally tolerant of SDS treatments, and the process of ammonium sulfate fractionation using 30 and 60 percent cutoffs have already been known in the prior art, an artisan in the art would have been able to successfully extract the leaves of ACT expressing wheat oxalate oxidase enzyme (to a desired amounts and/or specific activity as already taught by Mans et al, above) in order to obtain suitable composition and/or enzyme preparation comprising wheat oxalate oxidase. Unless evidence and/or data provided to the contrary, such modifications in the disclosure from Zhang et al (when taken with teachings and/or suggestions from Mans et al and Zhou et al) would have been deemed obvious and fully contemplated by an artisan of ordinary skill in the art.
More importantly, it is noted that instant claims are directed to a product composition, and not to a method of preparing the composition per se, and therefore, unless evidence/data are presented that show structural difference(s) in the oxalate oxidase enzyme, such composition with specific activity of wheat OxOx would have been deemed obvious to a person of ordinary skill in the art given the combined teachings and/or suggestions from the cited prior art references, as discussed above.
Thus, the claim as whole would have been prima facie obvious to a person of ordinary skill in the art before the effective filing date of the invention as claimed..
As per MPEP 2111.01, during examination, the claims must be interpreted as broadly as their terms reasonably allow. In re American Academy of Science Tech Center, F.3d, 2004 WL 1067528 (Fed. Cir. May 13, 2004)(The USPTO uses a different standard for construing claims than that used by district courts; during examination the USPTO must give claims their broadest reasonable interpretation.). This means that the words of the claim must be given their plain meaning unless applicant has provided a clear definition in the specification. In re Zletz, 893 F.2d 319, 321, 13 USPQ2d 1320, 1322 (Fed. Cir. 1989).
Conclusion
NO claims are currently allowed.
Pertinent Prior Art:
1. Zhang et al. (1996; cited as ref. [V] on PTO 892 form)- “Ethanol increases sensitivity of Oxalate Oxidase Assays and facilitates direct activity staining in SDS gels”, Plant Molecular Biology Reporter, 1996, vol. 14, no. 3, pages 266-272 (disclose the fact that oxalate oxidases are normally SDS-tolerant and their activity can be detected using SDS-PAGE gels; see Abstract, disclosure on pages 266-267).
2. Hartman et al. (1992; WO 92/14824 A1; cited as ref. [N] on PTO 892 form)- “Newly characterized Oxalate Oxidase and uses therefor” (disclose detergent-based extraction procedure for barely oxalate oxidase purification and characterization, wherein use of 0.5% taurodeoxycholate is disclosed as the detergent used for extraction of the enzyme followed with 30-70 % cutoff with ammonium sulfate fractionation steps; wherein the enzymatically active protein was also purified using preparative SDS-PAGE gel electrophoresis; see pages 14-15, and 17, in particular).
Any inquiry concerning this communication or earlier communications from the examiner should be directed to SATYENDRA K. SINGH whose telephone number is (571)272-8790. The examiner can normally be reached M-F 8:00- 5:00.
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If attempts to reach the examiner by telephone are unsuccessful, the examiner’s supervisor, LOUISE W HUMPHREY can be reached at 571-272-5543. The fax phone number for the organization where this application or proceeding is assigned is 571-273-8300.
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SATYENDRA K. SINGH
Primary Examiner
Art Unit 1657
/SATYENDRA K SINGH/Primary Examiner, Art Unit 1657