Notice of Pre-AIA or AIA Status
The present application, filed on or after March 16, 2013, is being examined under the first inventor to file provisions of the AIA .
DETAILED ACTION
Claims 1-6 and 12 are pending. Claims 7-11 are cancelled. Claims 1-5 are withdrawn. Claims 6 and 12 are under examination on their merits.
Response to Arguments
Applicant's arguments filed 2/5/2026 have been fully considered but they are not persuasive.
Applicant argues against the rejection of claims under 35 U.S.C. 101 on the grounds that claim 6 includes three types of additional elements that confer patent-eligibility: (1) a physical transformation of a biological sample, (2) concrete, technical biomarker measurements using immunoassay, and (3) a specific pattern-based diagnostic rule (multi-marker logic). Applicant concludes that the claim embodies an inventive concept that amounts to significantly more than the judicial exception because the process actively transforms a sample, measures multiple biomarkers using laboratory techniques, and then uses a multi-marker decision rule to provide diagnostic information (Arguments, pages 11-12).
In response, these arguments are unpersuasive because the output of performing the claim is purely information (diagnosis) and the laboratory techniques are well-understood, routine, and conventional techniques. Claim 6 recites obtaining a serum sample and then treating the serum sample with a primary antibody, treating the sample with a secondary antibody that specifically binds to the primary antibody, wherein the secondary antibody is conjugated to biotin via a constant region, and treating the sample with avidin conjugated to horseradish peroxidase. This technique is the avidin-biotin complex method and is well-understood, routine, and conventional: see Bratthauer (2010. The Avidin–Biotin Complex (ABC) Method and Other Avidin–Biotin Binding Methods. In: Oliver, C., Jamur, M. (eds) Immunocytochemical Methods and Protocols. Methods in Molecular Biology, vol 588. Humana Press; cited in the Non-Final Action mailed on 11/6/2026; Abstract and Figure 1). Furthermore, measuring multiple biomarkers to determine a disease state is also well-understood, routine, and conventional. For example, Schmidt et al. (Neuroscience letters 570 (2014): 81-85; cited in the Non-Final Action mailed on 11/6/2026) teaches that amyloid-beta 1–42, total protein Tau (T-tau) and hyperphosphorylated Tau (P-tau) are clinically used biomarkers for Alzheimer’s disease (page 81, Introduction, left column, paragraph 1). Schmidt teaches that tau and phospho-tau are elevated in the CSF of patients with Alzheimer’s disease, whereas amyloid beta 42 is depleted (page 81, Introduction, left column, paragraph 1). Therefore, the use of multiple biomarkers to diagnose a degenerative brain disease is not inventive and the claim does not amount to significantly more than the judicial exception of an abstract idea.
Drawings
The drawings are objected to because the x-axis contains overlapping labels behind stage 1 and stage 2/stage3 dementia in figures 2-13. 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 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.
(New Rejection Necessitated by Amendment) Claims 6 and 12 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 6 is indefinite for the limitation, “the avidin having horseradish peroxidase conjugated.” It is unclear whether the horseradish peroxidase is conjugated to avidin, conjugated to another unnamed component, or conjugated to both the avidin and another unnamed component. Applicant may consider amending to “wherein the avidin is conjugated to horseradish peroxidase.”
Claim 6 is further indefinite for “measuring in the serum sample, a level of…phospho-tau detected by AT180.” AT180 refers to the monoclonal antibody currently used to define an Alzheimer’s disease (AD)-related pathological form of the phosphorylated Tau protein. There are at least two different reasonable interpretations of this limitation in the claim, rendering the claim indefinite. In one interpretation, the measuring step requires detecting the phospho-tau with the AT180 monoclonal antibody. In a second interpretation, the measuring step is not limited to detecting phospho-tau by the AT180 monoclonal antibody but rather encompasses any measuring method that detects the form of phospho-tau that binds to the AT180 monoclonal antibody.
Claim 12 is rejected for depending from a rejected base claim and not rectifying the sources of indefiniteness discussed above.
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.
(New Rejection Necessitated by the Amendment) Claims 6 and 12 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 claims contains subject matter which was not described in the specification in such a way as to reasonably convey to one skilled in the relevant art that the inventor or a joint inventor, or for applications subject to pre-AIA 35 U.S.C. 112, the inventor, at the time the application was filed, had possession of the claimed invention.
Claim 6 recites treating a first portion of the serum sample with a first primary antibody that specifically binds to Aβ42, treating a second portion of the serum sample with a second primary antibody that specifically binds to the CRMP2, and treating a third portion of the serum sample with a third primary antibody that specifically binds to the phospho-tau, for each of the first portion, the second portion, and the third portion, treating the first, second, and third portions with a secondary antibody that specifically binds to the primary antibody.
The person of ordinary skill in the art would not have recognized that the inventors had possession of the claimed genus of primary antibodies that specifically bind to Aβ42 and the claimed genus of primary antibodies that specifically bind to CRMP2.
The specification discloses in [0046] that the antibodies used to measure the level of each biomarker were based on commercially available kits. Each biomarker is measured by a separate kit (i.e. a separate antibody). However, the structure of any of these antibodies is not disclosed. The specification does not provide any special definition, thus the term “antibody” is given its broadest reasonable interpretation as including fragments or derivatives of natural antibodies, such as monoclonal antibodies, Fab, scFv, or VHH.
An antibody molecule has three functional components: two Fragment-binding domains (Fabs) and the fragment crystallizable (Fc). Each of the Fabs have identical antigen-binding sites for binding to a specific target antigen (Chiu, Mark L., et al. "Antibody structure and function: the basis for engineering therapeutics." Antibodies 8.4 (2019): 55. (Year: 2019); cited in the Non-Final Action mailed on 11/6/2026; 1.1 Overall Features of the Immunoglobin, page 2, paragraph 1). In other words, although a traditional antibody has two “arms,” each arm binds to the same target antigen. The antigen-binding site, which is formed by pairing of the Fab, VH, and VL with the N-terminal region, is designated as the Fv. The Fv amino acid residues in contact with the antigen have specificity-determining residues and antibodies in complex with haptens, proteins, or peptides show distinctive specificity determining residue (SDR) patterns (Chiu et al., page 4, 1.2.2 The Fab Antigen-Binding site, paragraph 3, lines 1-3). The antigen-binding sites specific for peptides are groove-shaped depressions between VH and VL, while anti-protein antibodies tend to have larger binding sites compared to those of the anti-peptide binding class (Chiu et al., page 4, 1.2.2 The Fab Antigen-Binding site, paragraph 3).
Although the binding epitope for the AT180 monoclonal antibody is taught by the prior art of Amniai et al. (Biochemical and biophysical research communications 412.4 (2011): 743-746; Abstract), the state of the art does not disclose any binding epitope for Aβ42 or CRMP2 or the corresponding paratopes of the antibodies that bind to these antigens.
Therefore, the structure-function correlation between an antibody and the capability of binding to each of the claimed proteins (Aβ42 or CRMP2) is unknown. The person of ordinary skill in the art would have been unable to successfully visualize the species of the claimed genera.
The state of the art indicates that all of the heavy and light chain CDRs in their proper order and in the context of framework sequences that maintain their required conformation, are required in order to produce a protein having antigen-binding function and that proper association of heavy and light chain variable regions is required in order to form functional antigen binding sites. MacCallum et al. (Psychological methods 1.2 (1996): 130) teaches that although no single residue is in contact with the antigen in all structures, the CDR3 of the heavy and light chain dominate (MacCallum pg. 733, paragraph bridging columns). MacCallum teaches that contacts are more common at CDR residues which are located centrally within the combining site and non-contacting residues within the CDRs are important in defining "canonical" conformations (MacCallum Abstract).
De Pascalis et al. (the Journal of Immunology 169.6 (2002): 3076-3084) engineers a less immunogenic humanized monoclonal antibody by grafting CDRs onto the frameworks of the variable light and variable heavy regions of human monoclonal antibodies (Abstract). Although abbreviated CDR residues are used in the constructs, some residues in all 6 CDRs are used for the constructs (see De Pascalis page 3080, left column, paragraph 2).
Casset et al. (Biochemical and biophysical research communications 307.1 (2003): 198-205.) demonstrates the fact that not just one CDR is essential for antigen binding or maintaining the conformation of the antigen binding site: Casset constructs a peptide mimetic of an anti-CD4 monoclonal antibody binding site by rational design (Casset Abstract). Casset’s peptide mimetic is formed by 27 residues from 5 CDRs (Casset Abstract). Casset also teaches that although CDR H3 is at the center of most, if not all, antigen interactions, clearly other CDRs play an important role in the recognition process (Casset page 199, left column, paragraph 2) Casset uses all CDRs except L2 and additionally uses a framework residue located just before the H3 (Casset see page 202, left column, paragraph 1).
Vajdos et al. (Journal of molecular biology 320.2 (2002): 415-428) teaches that antigen binding is primarily mediated by the CDRs and that the more highly conserved framework segments that connect the CDRs are mainly involved in supporting the CDR loop conformations (page 416, left column, bottom paragraph). However, in some cases framework residues also contact the antigen (page 416, left column, bottom paragraph).
Even minor changes in the amino acid sequences of the heavy and light variable regions, particularly in the CDRs, may dramatically affect antigen-binding function. Rudikoff et al. (Proceedings of the National Academy of Sciences 79.6 (1982): 1979-1983. 1982) teaches that the alteration of a single amino acid in the CDR of a phosphocholine-binding myeloma protein resulted in the loss of antigen-binding function (Abstract).
The above references demonstrate that an antibody must comprise all 6 CDRs in order to maintain the antigen binding specificity and affinity which is characteristic of the immunoglobulin.
The instant claims fail to meet the requirements for disclosure because the antibody is described solely by the antigen to which it binds (Aβ42 or CRMP-2). The specification does not disclose all 6 CDRs for any antibody; therefore, it does not teach the structure associated with the claimed function for the antibody.
Although the AT180 monoclonal antibody that binds to phospho-tau is taught by the prior art, there a limited number of species of antibodies taught by the prior art that bind to Aβ42 or CRMP-2. For example, Williamson et al. (Journal of Alzheimer’s Disease 27.3 (2011): 615-625) generates phosphospecific CRMP2 antibodies by injecting sheep with phosphopeptides conjugated to bovine serum album (page 617, Materials and Methods, left column, Materials paragraph 1). However, Williamson does not teach the structure of the antibodies.
Given the lack of disclosure provided within the specification and the state of the art just before the effective filing date of the claimed invention, the person of ordinary skill in the art would not have recognized that the inventor had possession of the claimed genus of primary antibodies capable of binding to amyloid beta 42 or primary antibodies capable of binding to CRMP2. The specification does not disclose the structure (6 CDRs) for any of the claimed antibodies.
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.
(New Rejection Necessitated by the Amendment) Claims 6 and 12 are rejected under 35 U.S.C. 112(a) or 35 U.S.C. 112 (pre-AIA ), first paragraph, because the specification, while being enabling for a method of diagnosing mild cognitive impairment or dementia, does not reasonably provide enablement for any other degenerative brain disease. The specification does not enable any person skilled in the art to which it pertains, or with which it is most nearly connected, to make and use the invention commensurate in scope with these claims.
Per MPEP 2164.01(a), the following eight factors should be considered when determining whether the person of ordinary skill in the art would face undue experimentation to make and/or use the invention: (1) The nature of the invention; (2) the state of the prior art; (3) the relative skill of those in the art; (4) the predictability or unpredictability of the art; (5) the breadth of the claims; (6) the amount of direction or guidance presented; (7) the presence or absence of working examples; and (8) the quantity of experimentation necessary. While it is not essential that every factor be examined in detail, those factors deemed most relevant should be considered.
Nature of the invention. Claim 6 recites a method of diagnosing a degenerative brain disease in a subject comprising obtaining a blood sample from the subject, processing the blood sample by allowing the blood sample to clot for about 2 hours using a serum separator tube and centrifuging the blood sample at about 1000 × g for about 15 minutes to obtain a serum sample, measuring, in the serum sample, a level of amyloid beta 42, a level of collapsin response mediator protein-2, and a level of phospho-tau detected by AT180, comparing the level of AB42, the level of CRMP2, and the level of phospho-tau detected by AT180 with corresponding levels of AB42, CRMP2, and phospho-tau detected by AT180 in a control group of individuals without the degenerative brain disease; and diagnosing the degenerative brain disease in the subject when the level of Aβ42 is lower than the corresponding level of Aβ42 in the control group and the level of CRMP2 and the level of phospho-tau detected by AT180 are higher than corresponding levels of CRMP2 and phospho-tau detected by AT180 in the control group.
Breadth of the claims. Claim 6 is generic to any degenerative brain disease. Claim 12 limits the degenerative brain disease to any one or more selected from the group consisting of Alzheimer's disease, frontotemporal dementia, Parkinson's disease, amyotrophic lateral sclerosis, progressive supranuclear palsy, corticobasal
degeneration, Pick's disease, mild cognitive impairment (MCI), and dementia.
State of the prior art and unpredictability. Although Aβ42 and phospho-tau have been detected in the serum of patients with Alzheimer’s disease and mild cognitive impairment (Nam et al., International journal of molecular sciences 21.14 (2020): 5007; page 15, 4.8. Measurements of t-tau and p-tau Protein Levels). the prior art does not teach detecting CRMP-2 in the serum of patient’s with neurodegenerative diseases. The person of ordinary skill in the art would have been unable to predict which neurodegenerative diseases result in increased levels of CRMP-2 in the serum.
Galasko et al. (Alzheimer's research & therapy 5.2 (2013): 10) teaches that one of the challenges in discovering blood biomarkers to diagnose AD is that the mechanisms of neurodegeneration occur in the brain and a significant dilution of proteins occurs as they traffic from the brain to the CSF and then to the bloodstream, resulting in a considerable analytical detection challenge (page 4, right column, bottom paragraph, Conclusions).
Lawal et al. (Computers in Biology and Medicine 98 (2018): 168-177) teaches that CRMP-2 is a CNS-embedded protein that has been implicated in the pathogenesis of AD as a result of its phosphorylation (page 168, right column, middle paragraph and bottom paragraph). Lawal teaches that it is desirable for CRMP-2 inhibitors to cross the blood-brain barrier (Title and Abstract). Thus, the person of ordinary skill in the art would have understood from the teachings of Galasko and Lawal that CRMP-2 is localized to the brain and that the ability to detect CRMP-2 in the blood would depend on the concentration in the disease state and the ability of CRMP-2 to traffic to the blood from the brain.
Levels of biomarkers in cerebrospinal fluid (CSF) do not always positively correlate with levels in serum. For example, serum levels of Aβ42 are negatively correlated with CSF Aβ42 whereas phospho-tau is higher in serum (Abstract of Teunissen et al., Disease 62.4 (2018): 1857-1863.).
Furthermore, the prior art teaches that neurodegenerative diseases differ from each other. For example, Williamson et al. (Journal of Alzheimer’s Disease 27.3 (2011): 615-625) teaches that CRMP2 hyperphosphorylation is characteristic of Alzheimer’s disease and is not a feature common to other neurodegenerative diseases (Title). Olsson et al. (The Lancet Neurology 15.7 (2016): 673-684) teaches that both CSF Aβ42 and CSF phospho-tau can separate patients with Alzheimer’s disease from controls, whereas plasma total tau is the only blood biomarker that discriminates patients with Alzheimer’s disease from controls (page 683, left column, bottom paragraph).
In summary, there is a high degree of unpredictability in the art with respect to blood biomarkers of neurodegenerative diseases, especially with regard to CRMP-2.
Guidance in the specification and working examples. The specification discloses that blood samples were provided from normal volunteers, patients with mild cognitive impairment, patients with stage 1 dementia, patients with stage 2 dementia, and patients with stage 3 dementia ([55]). Fig. 3 illustrates Aβ42 serum levels in control, stage 1 dementia, and stage 2/3 dementia. Fig. 9 illustrates CRMP-2 serum levels in control, stage 1, and stage 2/3 dementia patients. Fig. 12 illustrates the levels of phospho-tau detected by AT180 in control, stage 1 dementia, and stage 2/3 dementia. The specification does not disclose the levels of Aβ42, phospho-tau detected by AT180, or CRMP-2 in any other degenerative brain diseases.
Amount of experimentation necessary. Given the lack of predictability in the state of the art with respect to serum biomarkers in degenerative brain diseases and the limited amount of guidance in the specification, the person of ordinary skill in the art would have faced undue experimentation to practice the full scope of the invention. In particular, the person of ordinary skill in the art would have had to test at least each of the degenerative diseases recited in claim 12 since the person of ordinary skill in the art would have had no way of predicting which degenerative diseases resulted in elevated serum levels of CRMP-2, except for mild cognitive impairment and dementia.
Taking these factors into account, undue experimentation would be required by one of ordinary skill in the art to practice the full scope of the claimed invention. Thus, the claims are not fully enabled by the disclosure.
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.
(New Rejection Necessitated by the Amendment) Claims 6 and 12 are rejected under 35 U.S.C. 101 because the claimed invention is directed to the judicial exception of an abstract idea without significantly more.
The rationale for this determination is explained below.
A flowchart has been established to determine subject matter eligibility under 35 U.S.C. 101. See MPEP 2106 part (III) and 2106.04 part (II)(A). The flowchart comprises answering: Step 1) Is the claim to a process, machine, manufacture or composition of matter? Step 2A Prong One) Does the claim recite an abstract idea, law of nature or natural phenomenon? Step 2A Prong Two) Does the claim recite additional elements that integrate the judicial exception into a practical application? Step 2B) Does the claim recite additional elements that amount to significantly more than the judicial exception? The claims are analyzed for eligibility in accordance with their broadest reasonable interpretation.
Claim 6 is drawn to a process, which is one of the four statutory categories of invention (Step 1: Yes). The method preamble of claim 6 is “A method of diagnosing a degenerative brain disease in a subject,” which is an abstract idea, and claim 6 also recites two active steps that are mental processes (abstract ideas): “comparing the levels of Aβ42, the level of CRMP2, and the level of phospho-tau detected by AT180 with corresponding levels of Aβ42, CRMP2, and phospho-tau detected by AT180 in a control group of individuals without the degenerative brain disease,” and “diagnosing the degenerative brain disease in the subject when the level of Aβ42 is lower than the corresponding level of Aβ42 in the control group and the level of CRMP2 and the level of phospho-tau detected by AT180 are higher than the corresponding level of CRMP2 and phospho-tau detected by AT180 in the control group.” Therefore, claim 6 recites the judicial exception of an abstract idea (Step 2A Prong One: Yes).
Claims 6 and 12 do not integrate the judicial exception of an abstract idea/mental process into a practical application (Step 2A Prong Two: No). No practical application is recited in any of the claims (for example, a specific treatment administered to the individual diagnosed with the degenerative brain disease).
The additional elements recited in claims 6 and 12 are insignificant, extra-solution activity as well as well-understood, routine, and conventional (Step 2B: No).
Claims 6 and 12 recite measuring markers for diagnosing degenerative brain disease, which is well-understood, routine, and conventional. See MPEP 2106.05(d)(II): The courts have recognized the following laboratory techniques as well-understood, routine, conventional activity in the life science arts when they are claimed in a merely generic manner (e.g., at a high level of generality) or as insignificant extra-solution activity: i. Determining the level of a biomarker in blood by any means. Here, the claimed invention is determining the level of biomarkers via antibody-based detection and the biological sample is serum derived from blood. Furthermore, the methods for measuring the levels of the markers comprise treating the serum sample with a primary antibody, treating the sample with a secondary antibody that specifically binds to the primary antibody, wherein the secondary antibody is conjugated to biotin via a constant region, and treating the sample with avidin conjugated to horseradish peroxidase. This technique is the avidin-biotin complex method and is well-understood, routine, and conventional: see Bratthauer (2010. The Avidin–Biotin Complex (ABC) Method and Other Avidin–Biotin Binding Methods. In: Oliver, C., Jamur, M. (eds) Immunocytochemical Methods and Protocols. Methods in Molecular Biology, vol 588. Humana Press; cited in the Non-Final Action mailed on 11/6/2026; Abstract and Figure 1). Tetramethylbenzidine or TMB is also a well-known chromogenic substrate of horseradish peroxidase and commonly coupled with absorbance measurements in ELISA assays (Abstract of Thermo Fisher; 2011 website). Claim 6 also recites obtaining a serum sample, which is well-understood, routine and conventional activity.
Therefore, none of the claims are eligible under 35 U.S.C. 101.
Conclusion
Applicant's amendment necessitated the new ground(s) of rejection presented in this Office action. Accordingly, THIS ACTION IS MADE FINAL. See MPEP § 706.07(a). Applicant is reminded of the extension of time policy as set forth in 37 CFR 1.136(a).
A shortened statutory period for reply to this final action is set to expire THREE MONTHS from the mailing date of this action. In the event a first reply is filed within TWO MONTHS of the mailing date of this final action and the advisory action is not mailed until after the end of the THREE-MONTH shortened statutory period, then the shortened statutory period will expire on the date the advisory action is mailed, and any nonprovisional extension fee (37 CFR 1.17(a)) pursuant to 37 CFR 1.136(a) will be calculated from the mailing date of the advisory action. In no event, however, will the statutory period for reply expire later than SIX MONTHS from the mailing date of this final action.
Any inquiry concerning this communication or earlier communications from the examiner should be directed to CANDICE LEE SWIFT whose telephone number is (571)272-0177. The examiner can normally be reached M-F 8:00 AM-4:30 PM (Eastern).
Examiner interviews are available via telephone, in-person, and video conferencing using a USPTO supplied web-based collaboration tool. To schedule an interview, applicant is encouraged to use the USPTO Automated Interview Request (AIR) at http://www.uspto.gov/interviewpractice.
If attempts to reach the examiner by telephone are unsuccessful, the examiner’s supervisor, Louise 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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/LOUISE W HUMPHREY/Supervisory Patent Examiner, Art Unit 1657
/CANDICE LEE SWIFT/Examiner, Art Unit 1657
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