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 .
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.
DETAILED ACTION
Election/Restrictions
Applicant’s election of Group I (ex vivo methods of determining the effect of an agent on catalysis by an MPS cell of a disease marker product where the product is Aß42 or Aß40) and the species election Aß residue 34 in the reply filed on 6/2/26 is acknowledged. Because Applicant did not distinctly and specifically point out the supposed errors in the restriction requirement, the election has been treated as an election without traverse (MPEP § 818.01(a)).
Applicant’s species election of α-synuclein 39, Tau 281, TDP 334, and MBP 70 are also acknowledged. The examiner appreciates the complete reply and acknowledges that these species are currently only relevant to the non-elected subject matter but will be utilized should they become relevant.
Claims 1-9, 11-22, and 26-27 are pending.
Claims 16-18 and 26-27 are withdrawn from further consideration pursuant to 37 CFR 1.142(b) as being drawn to a nonelected invention, there being no allowable generic or linking claim. Election was made without traverse in the reply filed on 6/2/26.
Claims 1-9, 11-15, and 19-22 are under examination.
Drawings
The drawings are objected to because:
Figure 11 contains a sequence that must be identified by a SEQ ID. This SEQ ID may be in the drawing itself or in the brief description of the drawings in the specification.
Figure 12 contains a sequence that must be identified by a SEQ ID. This SEQ ID may be in the drawing itself or in the brief description of the drawings in the specification.
Corrected drawing sheets in compliance with 37 CFR 1.121(d) are required in reply to the Office action to avoid abandonment of the application. Any amended replacement drawing sheet should include all of the figures appearing on the immediate prior version of the sheet, even if only one figure is being amended. The figure or figure number of an amended drawing should not be labeled as “amended.” If a drawing figure is to be canceled, the appropriate figure must be removed from the replacement sheet, and where necessary, the remaining figures must be renumbered and appropriate changes made to the brief description of the several views of the drawings for consistency. Additional replacement sheets may be necessary to show the renumbering of the remaining figures. Each drawing sheet submitted after the filing date of an application must be labeled in the top margin as either “Replacement Sheet” or “New Sheet” pursuant to 37 CFR 1.121(d). If the changes are not accepted by the examiner, the applicant will be notified and informed of any required corrective action in the next Office action. The objection to the drawings will not be held in abeyance.
Claim Objections
Claims 2, 5, 13, 15, 20 are objected to because of the following informalities:
The claims use the term “preferably”. A preference is not a claim limitation and does not serve the purpose of a claim in defining the invention. See MPEP § 2173.05(d) which states that “[d]escription of examples or preferences is properly set forth in the specification rather than the claims. If stated in the claims, examples and preferences may lead to confusion over the intended scope of a claim."
Appropriate correction is required.
Claim 14 is objected to because of the following informalities:
“has cleaved” should be “has been cleaved”. The former suggests that Aß is the element doing the cleaving, which it is not.
Appropriate correction is required.
Improper Markush Group
Claim 22 is rejected on the basis that it contains an improper Markush grouping of alternatives. See In re Harnisch, 631 F.2d 716, 721-22 (CCPA 1980) and Ex parte Hozumi, 3 USPQ2d 1059, 1060 (Bd. Pat. App. & Int. 1984). A Markush grouping is proper if the alternatives defined by the Markush group (i.e., alternatives from which a selection is to be made in the context of a combination or process, or alternative chemical compounds as a whole) share a “single structural similarity” and a common use. A Markush grouping meets these requirements in two situations. First, a Markush grouping is proper if the alternatives are all members of the same recognized physical or chemical class or the same art-recognized class and are disclosed in the specification or known in the art to be functionally equivalent and have a common use. Second, where a Markush grouping describes alternative chemical compounds, whether by words or chemical formulas, and the alternatives do not belong to a recognized class as set forth above, the members of the Markush grouping may be considered to share a “single structural similarity” and common use where the alternatives share both a substantial structural feature and a common use that flows from the substantial structural feature. See MPEP § 2117.
The Markush grouping of various method intentions is improper because the alternatives defined by the Markush grouping do not share both a single structural similarity and a common use for the following reasons:
The alternatives do not share a common use. The alternatives are:
Comparing the effects of agents on catalysis of a disease marker to identify the agent with the greatest effect on catalysis
Screening agents for use in the treatment of neurodegeneration
Screening agents for use in the treatment of inflammatory activation
Screening agents for use in treatment of conditions associated with neurodegeneration
Determining an agent for personalized medicine by determining if the agent is effective in any capacity for human treatment wherein the effectiveness of the agent is determined by the result of step iv
These are all separate uses with different end goals. Each is a utility separate from the others on its own and does not meet the requirements for a single common use. For example, screening an agent for use when treating a condition associated with neurodegeneration (such mood swings, loss of appetite, or depression) would encompass certain agents that may or may not be also useful for treating inflammation and may or may not apply to personalized medicine. While there may be overlap, the end goal (the use) is clearly different.
To overcome this rejection, Applicant may set forth each alternative (or grouping of patentably indistinct alternatives) within an improper Markush grouping in a series of independent or dependent claims and/or present convincing arguments that the group members recited in the alternative within a single claim in fact share a single structural similarity as well as a common use.
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.
Claim 7 is 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 7 contains multiple qualifiers and alternatives such that it is unclear what is and is not being recited by the list. First, the use of “preferably” twice leads to confusion in the claim as to what this term modifies. It is unclear if “preferably wherein the FFAR4 agonist is DHA” is meant to be contained and where “and the combination” is no longer included in the preference; alternately, this preference extends through the end of the claim. It is also unclear if this second preference for the FFAR4 is meant to indicate that the first “preference” is actually a requirement, i.e., the agent must be a FFAR4 agonist, because the rest of the claim then (possibly) defines the options for this agonist.
The claim recites “an a7 nAChR agonist or PAM”. It is unclear if this is meant to end the list (terminating with “or”), in which case it is unclear how the rest of the elements are meant to be interpreted. If this is not terminating the list, then it is unclear why there is an “or” in the middle of the list. This causes a similar problem with the recitation of “a combination of a FFAR4 agonist and an a7 nAChR agonist or PAM,”, which could be interpreted as 1) a combination of a FFAR4 agonist and an a7 NAChR agonist or 2) PAM, because the previous use also separates two different elements. Alternately, this choice is a combination that requires a FFAR4 agonist, combined with either 1) a7 nAChR agonist or 2) PAM. The next line includes both an “or” and an “and” but also continues with “preferably”. The use of multiple “and”, “or”, and “preferably” creates confusion over the identity of the elements in the list and which are or are not actual claim limitations.
Further, as above, the use of “preferably” is either a claim limitation, in which case it is unclear why this is referred to as a preference, or the term is not a claim limitation, in which case it is unclear why the phrase is in the claims at all. See MPEP § 2173.05(d) which states that “[d]escription of examples or preferences is properly set forth in the specification rather than the claims. If stated in the claims, examples and preferences may lead to confusion over the intended scope of a claim."
Therefore, claim 7 is indefinite.
Claims 2-9, 11-15, and 19-22 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.
The claims, e.g., claim 2, recite “a method of claim 1” or similar. In one interpretation, this is meant to be interpreted as “the method of claim 1”, relying on proper antecedent basis to refer to the whole of the method. Alternately, just maintaining the sample (claim 1 part i) is “a method” found in claim 1 and so the interpretation is that any process which is part of the claims previously recited is “a method”.
Therefore, claims 2-9, 11-15, and 19-22 are indefinite.
Claim Rejections - 35 USC § 103
The following is a quotation of 35 U.S.C. 103 which forms the basis for all obviousness rejections set forth in this Office action:
A patent for a claimed invention may not be obtained, notwithstanding that the claimed invention is not identically disclosed as set forth in section 102, if the differences between the claimed invention and the prior art are such that the claimed invention as a whole would have been obvious before the effective filing date of the claimed invention to a person having ordinary skill in the art to which the claimed invention pertains. Patentability shall not be negated by the manner in which the invention was made.
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 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.
Claim(s) 1-9, 11-15, 19 and 21-22 is/are rejected under 35 U.S.C. 103 as being unpatentable over Fladby (US 20140051084; form 892) in view of Cashman (US 20090263492; form 892) and Liebsch (form 892).
Regarding claim 1, Fladby teaches:
(i) maintaining a sample of MPS cells under conditions in which the MPS cells remain alive: “peripheral blood monocytes/macrophages from a healthy volunteer were isolated and incubated with addition of synthetic Aß42 in the growth medium overnight to facilitate uptake and phagocytosis of Aß42” (paragraph 92). A monocyte is an MPS cell (see instant claim 2). Using a “growth” formula and monitoring a biological process of the cell (phagocytosis) indicates the MPS cells remained alive. However, in the alternative, it would have been obvious to one of ordinary skill in the art at the time of filing to keep the MPS cells alive because the monitored activities such as phagocytosis require the cell to be alive in order to observe these activities. See MPEP 2141(II)(C): "A person of ordinary skill in the art is also a person of ordinary creativity, not an automaton." KSR, 550 U.S. at 421, 82 USPQ2d at 1397. "[I]n many cases a person of ordinary skill will be able to fit the teachings of multiple patents together like pieces of a puzzle." Id. at 420, 82 USPQ2d at 1397. Office personnel may also take into account "the inferences and creative steps that a person of ordinary skill in the art would employ." Id. at 418, 82 USPQ2d at 1396.
(ii) exposing the sample of MPS cells to a disease marker product to permit phagocytosis of the disease marker product by the MPS cells: “peripheral blood monocytes/macrophages from a healthy volunteer were isolated and incubated with addition of synthetic Aß42 in the growth medium overnight to facilitate uptake and phagocytosis of Aß42” (paragraph 92). Monocytes are MPS cells (see instant claim 2). Aß42 is a disease marker product (instant claim 1 “when the disease marker product is Aß1-42). Incubation with Aß42 meets the limitation of exposing the MPS cells to a disease marker. Facilitating uptake and phagocytosis of Aß42 meets the limitations of permitting phagocytosis of the disease marker product.
(iii) detecting the intracellular amount of the disease marker product and/or at least one fragment thereof in the sample of MPS cells: “Intracellular staining of macrophages/monocytes from patient and control using commercially available monoclonal antibodies against Aß1-42” (paragraph 119). “The concentration for the control is 0.40 ng/mL…The concentration for the patient is 0.22 ng/mL” (paragraph 126). “Both patient and control seems to have close to equal amount of intracellular Aß1-42” (paragraph 126). This establishes that Fladby measured the intracellular amount of Aß42 (disease marker product) in the MPS cells; the title of paragraph 119 is “flowcytometry of monocytes/macrophages from patient and control” establishing that this was performed in the monocytes.
Fladby compares AD monocytes with non-AD monocytes but does not include a test agent. Since no test agent was included, Fladby also does not teach comparing the intracellular amount of Aß42 in the presence of the agent versus in the absence of the agent. The measurements above meet the limitations of measuring the Aß42 in the absence of an agent. Fladby teaches “this method can be used to measure specific degradation products in biological samples” (paragraph 126).
In summary, Fladby teaches the relevance of amyloid phagocytosis to Alzheimer’s disease (e.g., paragraph 7) and describes a method of using living monocytes to monitor Aß phagocytosis and intracellular Aß amounts. Fladby teaches the method may also be used to measure degradation products.
Cashman is also concerned with Aß42 phagocytosis in monocytes and the relevance to Alzheimer’s disease. Cashman teaches deficient Aß phagocytosis by macrophages and that certain compounds can treat AD by correcting this deficiency in AD subjects (paragraphs 3-4) as well as the role of monocytes in this process (paragraph 5). Cashman teaches a screening method comprising incubating a cell with a test compound and detecting the amount of Aß42 or other amyloid phagocytosed by the cell as an indication of the compound’s activity (claim 13). The cell is a monocyte (claim 14). As above, the observation of phagocytosis suggests the cells are alive, rendering such a step obvious because living cells are needed to study the physiological processes of those cells. Detecting the amount of Aß42 phagocytosed by the cell also requires that the cells were exposed to Aß42 in the first place.
In summary, Cashman also teaches the relevance of amyloid phagocytosis to Alzheimer’s disease and also describes a method of using living monocytes to monitor Aß phagocytosis and intracellular Aß amounts. Cashman teaches measuring the amount of phagocytosis in the presence of the test compound. However, Cashman compares the amount of intracellular Aß in the presence of the test compound compared to other test compounds (paragraph 201). In one case, this is “in the absence of the agent” as using a different agent indicates the first agent is not present. However, it would have further been obvious to one of ordinary skill in the art to compare the amount in the presence of the agent with the amount in the absence of any agent. Both Fladby and Cashman discuss the importance of monitoring monocyte phagocytosis of Aß42 and the relevance of such to AD. Fladby teaches the expected amount of phagocytosis in diseased cells, which would have been recognized as a baseline for the diseased cells. Cashman teaches screening compounds for their effect on phagocytosis in these diseased cells. It would have been obvious that measuring the effect of a compound requires comparison to some baseline value in order to determine if the phagocytosis is increased, decreased, or does not change. Since Fladby provides such a method, this comparison would have been obvious. This would have provided the relevant information regarding the effect of the agent on monocyte phagocytosis.
The combination above does not “detect a region of [a] fragment comprising at least 4 amino acids” which includes residue 34 of Aß42 identified as SEQ ID NO: 1, i.e., a leucine residue. While the art recognizes that the method may be used to detect such fragments (see Fladby discussion above), the art above lacks a teaching that such fragments are relevant to the disease state or to phagocytosis.
Liebsch teaches Aß34 is elevated in dementia, that Aß34 levels correlate with overall clearance rates, and that Aß34 is a marker of amyloid clearance (abstract). Liebsch teaches that intracellular Aß is “especially susceptible to BACE1 mediated degradation at the Aß34 cleavage site” (p.12 C1) and that Aß34 levels are correlated to AD progression (p.7 C1). Liebsch detects specifically the C-terminus of Aß34, which includes the leucine residue at position 34 and at least 4 consecutive amino acids. A “neo-epitope” indicates the Aß was cleaved after position 34, creating the new epitope (fragment of Aß42 that includes residue 34). Whether the antibody of Liebsch binds at least 4 amino acids is an inherent property of the antibody. The art clearly indicates the antibody binds residue 34 and epitopes are typically at least four amino acids long (as evidenced by Buus, abstract and p.1798 C2; form 892). The Office is not equipped to make and test prior art products and the evidence supports the conclusion that the antibody of Liebsch meets the limitations of an antibody that detects at least 4 amino acids where one of those amino acids is residues 34 of Aß42 (leucine).
It would have been obvious to modify the method above to detect fragments of Aß42 including Aß34. Fladby and Cashman teach the relevance of Aß42 phagocytosis (internalization) to AD disease and Liebsch teaches Aß34 is also a useful measure of AD progression. Moreover, Fladby and Cashman teach monocytes internalize Aß and measure intracellular Aß, while Liebsch teaches intracellular Aß is prone to degradation to Aß34. This would have made obvious to one of ordinary skill in the art that the method of measuring the amount of Aß42 could be modified to detect Aß34 (Liebsch)
Finally, as this meets all of the active steps of the method, the combination must also arrive at the determination of the effect of the agent on catalysis by MPS cells of the disease marker product/fragment by the result of the comparison step iv. This “wherein” clause indicates what the results of the comparison step indicate but does not require any specific step itself. However, it is also noted that Liebsch teaches that Aß34 is degraded intracellularly, suggesting this as a marker for catalysis of an agent.
Regarding claim 2, both macrophages and monocytes are taught above and would have been obvious for the reasons above.
Regarding claim 3, Cashman teaches differentiating PBMCs into macrophages (paragraph 188); it is noted that peripheral blood mononuclear cells contain monocytes. Cashman teaches contacting the differentiated macrophages with the test agent (paragraph 197). Cashman teaches the relevance of both monocytes and macrophages to the method (e.g., paragraph 197, 199, 201; claim 14) as does Fladby (e.g., paragraph 60, 92, 118; claim 12, 18). It would have been obvious to include the step of differentiating monocytes into macrophages because the art teaches macrophages/monocytes as part of the method and Cashman teaches this differentiation step.
Regarding claim 4, Fladby teaches obtaining the cells from humans (paragraph 8) as does Cashman (paragraph 19) making this an obvious source for the cells.
Regarding claim 5, Fladby teaches the sample is blood (paragraph 8) as does Cashman (paragraph 19) making this an obvious sample to obtain.
Regarding claim 6, the instant specification indicates that culturing is a step which allows the cells to grow (p. 24 L 4-5). It would have been obvious to keep the cells alive as discussed above. Fladby teaches incubating the cells in growth medium (paragraph 92), which meets the limitations of culturing the cells. One of ordinary skill in the art provided with these teachings would have found it obvious to culture the cells for the reasons above.
Regarding claim 7, Cashman contacts the macrophages/monocytes with curcuminoids and notes that this increases Aß uptake (paragraph 4). This meets the limitations of a stimulator or inhibitor of the MPS autophagic or endolysosomal systems.
Regarding claim 8, it was known that Aß—including Aß42—is degraded into Aß34 as discussed above. This necessarily creates two fragments: the N-terminal fragment ending at residue 34 and the C-terminal fragment that is 35-40 or 35-42. It would have been obvious that this C-terminal fragment could also be detected, which meets the limitations of an Aß42 fragment that comprises residue 41 or an Aß40 fragment.
Regarding claim 9, as discussed above and throughout the documents of record, Aß is a disease marker associated with Alzheimer’s disease.
Regarding claim 11, as discussed above, the detected fragment terminates at residue 34 and an epitope is a minimum of four amino acids. The prior art product appears to meet the claim limitations.
Regarding claim 12, the Aß neoepitope at residue 34 is the C-terminal of instant SEQ ID NO: 6 and measuring this would have been obvious as above.
Regarding claim 13, it would have been obvious to detect Aß42 as well as the fragment including Aß34 as discussed above. “It is prima facie obvious to combine two compositions each of which is taught by the prior art to be useful for the same purpose, in order to form a third composition to be used for the very same purpose.... [T]he idea of combining them flows logically from their having been individually taught in the prior art.” In re Kerkhoven, 626 F.2d 846, 850, 205 USPQ 1069, 1072 (CCPA 1980). See MPEP § 2144.06(I). Similarly, both Aß42 and the Aß34 fragment are taught as useful to detect using the method and so it would have been obvious to detect both, meeting the limitation of “detecting more than one of the…C-terminal of SEQ ID NO: 6 [the Aß fragment terminating at residue 34] and the regions of Aß1-42”.
Regarding claim 14, the Aß was cleaved between residues 34 and 35 creating the neo-epitope at residue 34 as discussed above.
Regarding claim 15, the use of antibodies to detect the fragments of Aß42 is discussed above.
Regarding claim 19, detection of both the N-terminal (X-34) and C-terminal (35-X) fragments of amyloid would have been obvious as above.
Regarding claim 21, including a control group of cells which have not been exposed to the test agent would have been obvious as discussed above.
Regarding claim 22, the phrase “is for” and “for use” is interpreted as an intended use. There is no requirement by the claims that the method is actually used for such a purpose nor any active step that achieves these purposes that have not been addressed in the discussed of claim 1. These “for use” phrases are not considered to be limiting to the claim scope as the steps of the claim fully define the method and these “for use” phrases do not contain any steps themselves. Further, Cashman discusses the method and that curcuminoids could be used to treat AD (e.g., paragraph 4, 8). Both Fladby and Cashman describe the deficiencies of macrophages/monocytes as it relates to Alzheimer’s disease and it would have been obvious that observing agents that correct these deficiencies, such as in Cashman, could be “for” screening agents for use in neurodegeneration (AD) treatment. Note that the “wherein” clause at line 10 is clearly part of the “for determining whether an agent is an effective treatment for a human subject” and so is not required by the other alternatives of the claim.
Therefore, claims 1-9, 11-15, 19 and 21-22 would have been obvious.
Claim(s) 20 is/are rejected under 35 U.S.C. 103 as being unpatentable over Fladby (US 20140051084) in view of Cashman (US 20090263492) and Liebsch as applied to claims 1-9, 11-15, 19 and 21-22 above, and further in view of Bogin (US20170196906; form 892) and Monroe (US20180244770; form 892).
The discussion of the documents as they apply to claims 1-9, 11-15, 19 and 21-22 is set forth above and incorporated herein. The combination teaches the agent is a stimulator or inhibitor of the MPS autophagic or endolysosomal systems as discussed (e.g., claim 7). The combination does not teach adding an inflammatory activator in addition to the agent in step ii.
However, Cashman suggests evaluating the effects of anti-inflammatory therapies (paragraph 8). Cashman teaches TLR antagonists are anti-inflammatory (paragraph 10) and that TLR increases Aß uptake by microglia (paragraph 11). Both Cashman and Fladby teach amyloid is phagocytosed by macrophages (above).
Monroe teaches one method of performing an amyloid phagocytosis assay includes exposing macrophages to LPS (paragraph 664). While Monroe exposes the cells to LPS prior to addition of Aß, the LPS is not removed and so the cells are still exposed to LPS in step ii. LPS is the “preferred” inflammatory activator of instant claim 20 and so meets the limitations of an inflammatory activator.
Bogin also teaches isolating monocytes from PBMC as in Fladby/Cashman. Bogin teaches dendritic cells—cells which are differentiated from monocytes—exposed to both LPS and Aß (paragraph 26).
It would have been obvious to a person of ordinary skill in the art to include the pro-inflammatory LPS with the agent in step ii. The combination suggests monitoring the effects of anti-inflammatory agents and so a person of ordinary skill would recognize that methods such as Monroe and Bogin would create a pro-inflammatory environment in which to study these anti-inflammatory effects. Further, this combination teaches that including LPS in phagocytosis assays including phagocytosis of Aß was an established technique.
Therefore, claims 1-9, 11-15, and 19-22 would have been obvious.
Conclusion
Art of note includes WO 2020212627 (IDS 1/12/24 A10), which is cited on the international search report for the parent PCT and is relevant for the reasons therein. However, this document shares an assignee and inventors with the instant application. As an art rejection is of record, it would be duplicative to include a rejection over this piece of art. It is noted that there is a prima facie exception under §102(b)(2) but no prima facie exception under §102(b)(1).
Henjum (892) is made of record as it pertains to microglial processing of Aß, specifically of the Aß mid-domain.
Any inquiry concerning this communication or earlier communications from the examiner should be directed to ADAM M WEIDNER whose telephone number is (571)272-3045. The examiner can normally be reached M-T 9-18; W-R 9-15.
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If attempts to reach the examiner by telephone are unsuccessful, the examiner’s supervisor, Jeffrey Stucker can be reached at 571-272-0911. The fax phone number for the organization where this application or proceeding is assigned is 571-273-8300.
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/Adam Weidner/ Primary Examiner, Art Unit 1675
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