DETAILED ACTION
Examiner acknowledges receipt of the reply filed 11/20/2025 and RCE filed 1/30/2026, in response to the final office action mailed 8/07/2025.
Claims 1, 6, 8, 12, 15, 16, 26, 29, 30, 51, 53, 56, 57, 61, 64-66, and 215-217 are pending. Claims 6, 8, 12, 16, 29, 30, 51, 53, 56, 57, 61, 64-66, and 217 remain withdrawn from further prosecution for the reasons made of record.
Claims 1, 15, 26, 215 and 216 are being examined on the merits in this office action.
Continued Examination Under 37 CFR 1.114
A request for continued examination under 37 CFR 1.114, including the fee set forth in 37 CFR 1.17(e), was filed in this application after final rejection. Since this application is eligible for continued examination under 37 CFR 1.114, and the fee set forth in 37 CFR 1.17(e) has been timely paid, the finality of the previous Office action has been withdrawn pursuant to 37 CFR 1.114. Applicant's submission filed on 1/30/2026 has been entered.
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 .
Claim Objections- withdrawn
The objection of claim 1 is withdrawn in view of the amendment filed 11/06/2025.
Claim Rejections - 35 USC § 112- withdrawn
The rejection of claims 1, 15, 26, 215 and 216 under 35 U.S.C. 112(b) or 35 U.S.C. 112 (pre-AIA ), second paragraph, is withdrawn in view of the amendment filed 11/06/2025.
Claim Rejections - 35 USC § 101- maintained
The rejection of claims 1, 15, 26, 215 and 216 under 35 U.S.C. 101 is withdrawn, but set forth herein as a new rejection, basis of rationale.
Response to Arguments
Applicant’s amendment, filed 11/25/2026, with to the above objection and rejection have been fully considered and are persuasive. The objection and rejection have been withdrawn.
Applicant's arguments filed 11/6/2025 have been fully considered but they are not persuasive.
Upon further consideration, a new ground(s) of rejection is made in view of the amendment filed 11/06/2025.
An action on the merits is presented herein.
Specification
Please note, the specification has not been checked to the extent necessary to determine the presence of all possible error. Applicant's cooperation is required in correcting any errors of which applicant may become aware in the specification. MPEP § 608.01.
Maintained Rejections
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.
Claims 1, 15, 26, 215, and 216 remain/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 pre-AIA the inventor(s), at the time the application was filed, had possession of the claimed invention. The rejection is maintained from the office action mailed 8/07/2025, but has been amended to reflect claims filed 11/06/2025.
The courts have stated:
“To fulfill the written description requirement, a patent specification must describe an invention and do so in sufficient detail that one skilled in the art can clearly conclude that "the inventor invented the claimed invention." Lockwood v. American Airlines, Inc., 107 F.3d 1565, 1572, 41 USPQ2d 1961, 1966 (1997); In re Gosteli, 872 F.2d 1008, 1012, 10 USPQ2d 1614, 1618 (Fed. Cir. 1989) (" [T]he description must clearly allow persons of ordinary skill in the art to recognize that [the inventor] invented what is claimed."). Thus, an applicant complies with the written description requirement "by describing the invention, with all its claimed limitations, not that which makes it obvious," and by using "such descriptive means as words, structures, figures, diagrams, formulas, etc., that set forth the claimed invention." Lockwood, 107 F.3d at 1572, 41 USPQ2d at 1966.” Regents of the University of California v. Eli Lilly & Co., 43 USPQ2d 1398.
The MPEP lists factors that can be used to determine if sufficient evidence of possession has been furnished in the disclosure of the Application. These include “level of skill and knowledge in the art, partial structure, physical and/or chemical properties, functional characteristics alone or coupled with a known or disclosed correlation between structure and function, and the method of making the claimed invention. Disclosure of any combination of such identifying characteristics that distinguish the claimed invention from other materials and would lead one of skill in the art to the conclusion that the applicant was in possession of the claimed species is sufficient.” MPEP 2163.
Further, for a broad generic claim, the specification must provide adequate written description to identify the genus of the claim. In Regents of the University of California v. Eli Lilly & Co., the court stated:
“A written description of an invention involving a chemical genus, like a description of a chemical species, 'requires a precise definition, such as by structure, formula, [or] chemical name,' of the claimed subject matter sufficient to distinguish it from other materials. Fiers, 984 F.2d at 1171, 25 USPQ2d at 1606; In re Smythe, 480 F.2d 1376, 1383, 178 USPQ 279, 284-85 (CCPA 1973) ("In other cases, particularly but not necessarily, chemical cases, where there is unpredictability in performance of certain species or subcombinations other than those specifically enumerated, one skilled in the art may be found not to have been placed in possession of a genus. . . ."). Regents of the University of California v. Eli Lilly & Co., 43 USPQ2d 1398.
The MPEP further states that if a biomolecule is described only by a functional characteristic, without any disclosed correlation between function and structure of the sequence, it is “not sufficient characteristic for written description purposes, even when accompanied by a method of obtaining the claimed sequence.” MPEP 2163. The MPEP does state that for generic claim the genus can be adequately described if the disclosure presents a sufficient number of representative species that encompass the genus. MPEP 2163. If the genus has a substantial variance, the disclosure must describe a sufficient variety of species to reflect the variation within that genus. See MPEP 2163. Although the MPEP does not define what constitute a sufficient number of representative, the Courts have indicated what do not constitute a representative number species to adequately describe a broad generic. In Gostelli, the Court determined that the disclosure of two chemical compounds within a subgenus did not describe that subgenus. In re Gostelli, 872 F.2d at 1012, 10 USPQ2d at 1618.
In the instant case, the claims are drawn to a pharmaceutical composition in unit dose form comprising: (a) a RAF proto-oncogene serine/threonine-protein kinase (RAF1) peptide or salt thereof wherein the peptide or salt thereof consists of the amino acid sequence selected from the group consisting of SEQ ID NOs: 3465-3467, 4641-4654, 8340-8403, 9530, and 9531; and (b) at least one of a pharmaceutically acceptable excipient, diluent, or carrier. Claim 1 further recites functional properties of the recited peptides, e.g., kills a cancer cell in an in vitro assay, and/or inhibits cancer cell proliferation as determined by an in vitro assay.
Given the broadest claim interpretation, ALL of the recited SEQ ID NOs: of variable amino acid sequences/chemical composition would be capable of each of the functional properties recited in claim 1. Examiner expressly notes that the specification does not set forth any structure/function correlation of the claimed SEQ ID NOs.
Of the recited SEQ ID NOs, it appears that only SEQ ID NO:9530 and SEQ ID NO:9531 were reduced to practice (Table 6 referred to as RAF1-73 and RAF1-78). Figs 3A-3C indicate that RAF1-73 and RAF1-78 inhibited the growth of cancer cells in vitro. See also Table 8.
The issue at question is the identity of recited SEQ ID NOs and functional properties that correlate with the respective SEQ ID NO(s); e.g., structures of a recited peptide and correlation with a functional property recited in claim 1 (kills a cancer cell in an in vitro assay, and/or inhibits cancer cell proliferation as determined by an in vitro assay).
Human RAF proto-oncogene serine/threonine-protein kinase (RAF1) (UniProtKB Accession No. P04049, accessed 3/20/2025 at URL: uniprot.org/uniprot/P04049; hereinafter “P04049”, is 648 amino acids in length.
Instant SEQ ID NO: 9530 has 98.2% identity with amino acid positions 72-112 of the human RAF1 protein sequence.
Instant SEQ ID NO: 9531 has 100% identity with amino acid positions 76-117 of the human RAF1 protein sequence.
Instant SEQ ID NO: 8341 has 100% identity with amino acid positions 59-98 of the human RAF1 protein sequence.
Instant SEQ ID NO: 8370 has 100% identity with amino acid positions 318-357 of the human RAF1 protein sequence.
Instant SEQ ID NO: 4654 has 100% identity with amino acid positions 567-606 of the human RAF1 protein sequence.
Thus, the recited SEQ ID NOs represent disparate sequences of RAF1.
As stated earlier, the MPEP states that a written description for a genus can be achieved by a representative number of species within a broad generic. The claims encompass 78 peptide sequences with distinct chemical/structural and functional properties. The specification fails to provide sufficient variety of species to reflect this variance in the genus since the specification does not provide any examples of the claimed SEQ ID NOs, beyond peptides of SEQ ID NO:9530 and SEQ ID NO:9531 which share amino acids positions 76-112 of human RAF1. Examiner further notes that functional properties of the two peptide with common backbone sequence cannot be extrapolated to peptides of other sequences/chemical compositions.
The description requirement of the patent statute requires a description of an invention, not an indication of a result that one might achieve if one made that invention. See In re Wilder, 736 F.2d 1516, 1521, 222 USPQ 369, 372-73 (Fed. Cir. 1984) (affirming rejection because the specification does "little more than outlin[e] goals appellants hope the claimed invention achieves and the problems the invention will hopefully ameliorate"). Accordingly, it is deemed that the specification fails to provide adequate written description for the genus of the claims and does not reasonably convey to one skilled in the relevant art that the inventor(s), at the time the application was filed, had possession of the entire scope of the claimed invention.
Response to arguments
Applicant traverses the rejection at pages 10-11 of the reply filed 11/06/2025. Applicant asserts that the specification reduced to practice peptides of SEQ ID NOs:9530 and 9531. Applicant states “as is readily apparent, the peptides are described both in the application and sequence listing of the application. Moreover, that the recited biological for the peptides is also described in the specification” (reply at p. 11). Applicant states “the claimed invention is in-fact described in the specification, figures and sequence listing”.
Examiner has reviewed and considered applicants arguments but is not persuaded.
Examiner acknowledges that two peptides, SEQ ID NOs:9530 and 9531, were reduced to practice. SEQ ID NOs:9530 and 9531 share 100% homology with amino acid positions 72-112 of human RAF1. As noted in the above rejection, peptides recited in SEQ ID NOs represent disparate amino acid sequences of the human RAF1 protein. Contrary to Applicant’s assertion, the specification does not disclose/identify which peptide sequence(s) correlate with the recited function(s) of claim 1, e.g., kills a cancer cell in an in vitro assay, and/or inhibits cancer cell proliferation as determined by an in vitro assay).
Thus, the skilled artisan cannot extrapolate from two peptides of SEQ ID NOs:9530 and 9531 to other variable amino acid sequences for structure/functions of the other claimed peptides.
The rejection is maintained for at least reasons and those previously made of record.
New Rejection
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.
Embodiments of the claimed peptides read on natural products.
Claims 1, 15, 26, 215 and 216 are rejected under 35 U.S.C. 101 because the claimed invention is directed to natural phenomenon without significantly more.
The rejection is new in view of consultation with a TC1600 Myriad §101 specialist. Examiner cites new references in this rejection.
Claims 1, 15, 26, 215 and 216 are directed to a pharmaceutical composition in unit dose form comprising: (a) a RAF proto-oncogene serine/threonine-protein kinase (RAF1) peptide or salt thereof wherein the peptide or salt thereof consists of the amino acid sequence selected from the group consisting of SEQ ID NOs: 3465-3467, 4641-4654, 8340-8403, 9530, and 9531; and (b) at least one of a pharmaceutically acceptable excipient, diluent, or carrier wherein the RAF1 peptide or salt thereof kills a cancer cell in an in vitro assay; and/or inhibits cancer cell proliferation as determined by an in vitro assay.
The claims recite fragments of natural products. The claim(s) does/do not include additional elements that are sufficient to amount to significantly more than the judicial exception for the following reasons. This judicial exception is not integrated into a practical application because the peptide being claimed is naturally occurring. The claim(s) does/do not include additional elements that are sufficient to amount to significantly more than the judicial exception because for the following reasons.
Step 1: Is the claim to a process, machine, manufacture or composition of matter? The instant claims are directed to a statutory patent-eligible subject matter category, a composition of matter.
Step 2a Prong 1: Is the claim directed to a law of nature, a natural phenomenon (Product of nature), or an abstract idea? The claims are directed to a natural phenomenon, specifically a natural-based product limitation.
As evidenced by the human RAF proto-oncogene serine/threonine-protein kinase (RAF1) (UniProtKB Accession No. P04049, accessed 3/20/2025 at URL: uniprot.org/uniprot/P04049; hereinafter “P04049”- previously cited), instant SEQ ID NO: 9530 has 98.2% identity with amino acid positions 72-112 of the human RAF1 protein sequence. Instant SEQ ID NO: 9531 has 100% identity with amino acid positions 76-117 of the human RAF1 protein sequence. Instant SEQ ID NO: 8342 has 100% identity with amino acid positions 69-112 of the human RAF1 protein sequence. Instant SEQ ID NO: 3466 has 100% identity with amino acid positions 82-121 of the human RAF1 protein sequence. Instant SEQ ID NO: 3467 has 100% identity with amino acid positions 83-122 of the human RAF1 protein sequence.
Chuang et al (Mol Cell Biol 14:5318-5325 (1994)) identifies that the Ras-binding domain (RBD) of Raf-1 (specifically residues 51–131, improved by 132–149) forms a small, stable N-terminal region responsible for high-affinity, GTP-dependent binding to Ras (abstract, pp. 5323-5324, Fig 4).
De Rooij et al (Oncogene 14:623-625 (1997)) confirm that the Ras-binding domain (RBD) of Raf1 correlates with aa 51-131 of Raf-1 (abstract, p 623).
Athuluri-Divakar et al (Cell 165(3): 643–655 (2016)) teach that a RAS mimetic disrupts RAS association with Raf1 [blocks Ras binding at the Ras-binding domain (RBD) of Raf-1] and impairs tumorigenic cell proliferation (abstract, pp 643-644, Figs 6-7, S6).
Thus, the prior art taught that the Ras-binding domain (RBD) of Raf-1 is located at positions 51-131 of 648 amino acids of human RAF1, and disruption of this region inhibits tumor cell growth. Instant SEQ ID NOs: 9530, 9531, 8342, 3466, and 3467 are each found within the RBD of RAF1 (aa 51-131 of RAF1).
Table 8 indicate that RAF1-73 (aa 72-112, instant SEQ ID NO:9530) and RAF1-78 (aa 76-117; instant SEQ ID NO:9530) inhibited the growth of cancer cells in vitro. Thus, Applicant’s data of Table 8 (instant SEQ ID NOs:9530 and 9531) is consistent with what was known in the prior art, e.g., disruption of RAS binding at the RAF1 RBD inhibits tumor cell growth.
MPEP §2106.04(c) makes it clear that all natural products (including both DNA and peptides/protein) should be evaluated using the markedly different characteristics test.
Fragmentation of a protein does not constitute a feature that renders the recited products markedly different from what exists in nature. Even though fragmentation or truncation structurally changes a protein from its natural state, the resultant difference (e.g., “broken” bonds) is not significant enough to render the isolated protein markedly different, because the sequence of the protein has not been altered. See, e.g., Myriad, 133 S. Ct. at 2116-18. Myriad clarified that not every change to a product will result in a marked difference, and that the mere recitation of particular words in the claims does not automatically confer eligibility. Id. at 2119. See also Mayo, 132 S. Ct. at 1294 (eligibility does not “depend simply on the draftsman's art”).
The term “pharmaceutically acceptable” is not specifically defined in the specification. Although one of ordinary skill the art would construe the limitation to the isolated or purified or having additional components, this does not render the claim markedly different from what exists in nature, because the pharmaceutically acceptable carrier may be naturally occurring, e.g. water.
The term “unit dose form” is not specifically defined in the specification.
Accordingly, the claims encompass a naturally occurring peptide which is not markedly different from the naturally occurring counterpart because it conveys the same proteomic information, and exhibits the same functional properties of what was known about the same region within the full-length RAF1 protein (RAS-binding domain at aa 51-131); disruption of this domain correlates with inhibition of cancer cell proliferation.
Step 2a Prong 2: Does the claim recite additional elements that integrate the judicial exception into a practical application? This judicial exception is not integrated into a practical application because only a composition comprising naturally occurring components is claimed. Although the claims recite intended uses and/or inherent functional properties, kills a cancer cell and/or inhibits cancer cell proliferation, such information would not add a meaningful limitation as it would merely recite inherent functions of the naturally occurring peptide.
Step 2b: Does the claim recite additional elements that amount to significantly more than the judicial exception? The claims, as a whole, do not recite any additional elements that amount to significantly more than the judicial exception. Specifically, the claim 1 does not include any elements in addition to the natural product. Claim 1 recites inherent properties of the claimed composition which is not deemed to add significantly more to the claim. As noted above, the data of Table 8 is consistent with what was known in the prior art relating to the RAF1 RAS-binding domain (RBD) (aa 51-131), e.g. disrupting this domain correlated with inhibition of cancer cell proliferation. The term “unit dose form” is not deemed to add significantly more to the claim.
Claim 1 does not recite any elements that amount to anything significantly more than the judicial exception.
Regarding claim 15, the claim recites an inherent property of the peptide [kills a cancer cell in an in vitro assay]. Claim 15 does not recite any elements that amount to anything significantly more than the judicial exception.
Claim 26 recites the peptide comprises a recombinant peptide. As noted above, fragmentation of a protein does not constitute a feature that renders the recited products markedly different from what exists in nature. The claim encompasses a naturally occurring peptide which is not markedly different from the naturally occurring counterpart because it conveys the same proteomic information. Claim 26 does not recite any elements that amount to anything significantly more than the judicial exception.
Regarding claim 215, the claim recites an inherent property of the peptide [inhibits cancer cell proliferation in an in vitro assay]. Claim 215 does not recite any elements that amount to anything significantly more than the judicial exception.
Claim 216 recites the peptide is non-naturally occurring. As noted above, fragmentation of a protein does not constitute a feature that renders the recited products markedly different from what exists in nature. The claim encompasses a naturally occurring peptide which is not markedly different from the naturally occurring counterpart because it conveys the same proteomic information. Claim 216 does not recite any elements that amount to anything significantly more than the judicial exception.
In sum, when the relevant steps are analyzed, they weigh against a significant difference. Accordingly, claims 1, 15, 26, 215 and 216 do not qualify as eligible subject matter.
Response to arguments
Applicant traverses the rejection at pp. 7-10 of the reply filed 11/06/2025. Applicant asserts that the instant claims consist of the recited SEQ ID NOs, having 40 amino acids as being structurally and functionally different from a full protein (reply at p. 8). Applicant further asserts that Myriad is limited to DNA, not proteins/peptides (pp. 8-10). Applicant further sets forth the physical differences between DNA and protein (pp. 9-10). Applicant asserts that the elected species of SEQ ID NO:9530, aa 73-112 of human RAF1, does not have the same biological activity as full-length protein, e.g., kinase activity. Id.
Examiner has reviewed and considered applicants arguments but is not persuaded.
Examiner expressly notes that the 101 rejection is set forth following consultation with TC1600 Myriad 101 specialist/SPE.
Contrary to Applicant’s arguments, the Office - not merely Examiner’s “art unit” -construe DNA and protein, under §101 analysis in view of Myriad.
As noted in the above rejection, instant SEQ ID NOs: 9530, 9531, 8342, 3466, and 3467 are each found within the RAS-binding domain (RBD) of RAF1 (aa 51-131 of RAF1). Thus, the peptides have 100% identity with naturally occurring human RAF1 protein. The prior art shows that disruption of the RBD correlates with inhibition of tumor cell proliferation. Applicant reduced to practice instant SEQ ID NOs: 9530 and 9531. The peptides (located within the RBD of human RAF1) showed inhibition of tumor cell proliferation (Table 8).
Thus, the peptides of SEQ ID NOs: 9530 and 9531 not only have 100% identity with instant naturally occurring full-length RAF1- conveying the same amino acid sequence, they also have the same functional activity, e.g., located within RBD, inhibition of tumor cell proliferation. Thus, peptides of SEQ ID NOs: 9530 and 9531 do not convey anything markedly different than the naturally occurring counterpart.
The Office construes fragmentation of a protein or DNA as not constituting a feature that renders the recited products markedly different from what exists in nature. Even though fragmentation or truncation structurally changes a protein from its natural state, the resultant difference (e.g., “broken” bonds) is not significant enough to render the isolated protein markedly different, because the sequence of the protein has not been altered. See, e.g., Myriad, 133 S. Ct. at 2116-18.
The rejection is maintained for at least these reasons and those previously made of record. Please refer to the above 101 rejection for a complete analysis under the 101 eligibility guidelines.
Examiner further refers Applicant to Example 28 of the Subject Matter Eligibility Examples: Life Sciences available May 2016, relating to peptides.
Examiner recommends claim 1 be amended in a manner to recite a non-naturally occurring pharmaceutically acceptable carrier/excipient (or similar amendment, as supported by Applicant’s specification).
Closest Prior Art
Avruch et al (U.S. 5736337- previously cited) teach compositions comprising RAF1 peptides that can be administered to a patient intravenously in a pharmaceutically acceptable carrier such a physiological saline [reads on unit dose form for administration to a patient] (cols. 17-19). RAF1 peptides include SEQ ID NO:8 which correlates with amino acid positions 51-131 of RAF1 protein (cols. 2, 5, 17-19). Avruch et al teach that the peptides inhibit cell proliferation (e.g., abstract, cols. 2, 4, ll. 64 – col 5, l. 44). Instant SEQ ID NO:9530 has 98.2% identity with amino acid positions 23-62 of SEQ ID NO:8 of Avruch et al. Avruch et al teach a peptide comprising instant SEQ ID NO:8342. Instant SEQ ID NO:8342 has 100% identity with amino acid positions 19-58 of SEQ ID NO:8 of Avruch et al.
However, Avruch et al do not teach or suggest a peptide consisting of instant SEQ ID NO: 8342 or 9530 (40 amino acids in length).
Instant SEQ ID NO: 8375 has 100% identity with SEQ ID NO:9 of Langland et al (U.S. 20170067122). Each peptide consists of 40 amino acids in length. However, Langland et al do not teach or suggest a pharmaceutical composition comprising a peptide of SEQ ID NO:9.
Conclusion
No claims are allowed.
Claims 1, 6, 8, 12, 15, 16, 26, 29, 30, 51, 53, 56, 57, 61, 64-66, and 215-217 are pending. Claims 6, 8, 12, 16, 29, 30, 51, 53, 56, 57, 61, 64-66, and 217 remain withdrawn.
Claims 1, 15, 26, 215 and 216 are rejected.
Any inquiry concerning this communication or earlier communications from the examiner should be directed to KRISTINA M HELLMAN whose telephone number is (571)272-2836. The examiner can normally be reached M-F 9:00 am-5:30 pm.
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/KRISTINA M HELLMAN/Examiner, Art Unit 1654
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