DETAILED ACTION
The present application, filed on or after March 16, 2013, is being examined under the first inventor to file provisions of the AIA .
Status of the Application
Receipt of the Response and Amendment after Non-Final Office Action filed 02/20/2026 and the Request for Continued Examination (RCE under 37 CFR 1.114) filed 03/16/2026 is acknowledged.
The status of the claims upon entry of the present amendment stands as follows:
Pending claims: 6-8, 16-24
Withdrawn claims: None
Previously cancelled claims: 1-5, 9-15
Newly cancelled claims: None
Amended claims: 6, 8
New claims: None
Claims currently under consideration: 6-8, 16-24
Currently rejected claims: 6-8, 16-24
Allowed claims: None
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and the fee set forth in 37 CFR 1.17(e) has been timely paid, the finality of the previous Office action has been withdrawn pursuant to 37 CFR 1.114.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 03/16/2026 has been entered.
Claim Rejections - 35 USC § 112
The text of those sections of Title 35, U.S. Code not included in this action can be found in a prior Office action.
Claims 6-8 and 16-24 are rejected under 35 U.S.C. 112(b) 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.
Claims 6 and 8 recite that the step of determining and/or quantifying the proteose peptone(s) is achieved by intact protein analysis and/or tryptic/GluC-digested peptide analysis. However, it is unclear as to how a protein can be intact and subjected to tryptic/GluC digestion for analysis (i.e., a protein cannot be intact and broken at the same time). Therefore, the claim is indefinite.
For the purpose of this examination, the claim will be interpreted as meaning that either intact protein analysis or tryptic/GluC-digested peptide analysis is performed.
Claims 7 and 16-24 are rejected by reason of dependency from claims 6 or 8.
Claim Rejections - 35 USC § 103
Claims 6-8, 16-21, and 24 are rejected under 35 U.S.C. 103 as being unpatentable over Etzel (US 2009/0068326; previously cited) in view of Elgar (Elgar et al., “Simultaneous separation and quantitation of the major bovine whey proteins including proteose peptone and caseinomacropeptide by reversed-phase high performance liquid chromatography on polystyrene-divinylbenzene”, 2000, Journal of Chromatograph A, 878, pages 183-196; previously cited) and Riggs (Riggs et al., “Automated signature peptide approach for proteomics”, 2001, Journal of Chromatography A, 924, pages 359-368) as evidenced by Yadav (Yadav et al., “Cheese whey: A potential resource to transform into bioprotein, functional/nutritional proteins and bioactive peptides”, 2015, Biotechnology Advances, vol. 33, pages 756-774; previously cited) and Vincent (Vincent et al., “Quantitation and Identification of Intact Major Milk Proteins for High-Throughput LC-ESI-Q-TOP MS Analysis”, 2016, PLoS ONE, 11(10); IDS citation).
Regarding claims 6 and 24, Etzel teaches a method for producing a whey protein fraction (corresponding to a whey protein isolate) wherein at least 90 wt.% of the total solids in the whey protein isolate are β-lactoglobulin and α-lactalbumin [0015]. Etzel teaches that the method comprises the step of: (i) providing a whey protein fraction from cheesemaking [0021]. Whey produced from cheesemaking comprises a mixture of different individual whey proteins including the β-casein derived proteose peptones PP8 fast, PP8 slow, and PP-5 (corresponding to component 8-fast, component 8-slow, and component 5, respectively) as evidenced by Yadav (page 764, column 1, paragraph under “4.2 Individual whey protein components”; page 765, column 1, paragraph under “4.2.7 Proteose-peptone component”); therefore, the provided whey protein fraction of Etzel contains at least one A1 β-casein derived proteose peptone selected from the list recited in present claim 6.
Etzel teaches that the provided whey protein fraction is subjected to gel filtration (corresponding to ion exchange using gel beads [0035] and optionally, subsequent gel filtration [0102]) in order to produce the whey protein fraction wherein at least 90 wt.% of the total solids in the whey protein fraction are β-lactoglobulin and α-lactalbumin [0015]. Since the filtered whey protein fraction contains at least 90 wt.% β-lactoglobulin and α-lactalbumin based on the total solids in the filtered whey protein fraction, the A1 β-casein derived proteose peptone content in the filtered whey protein fraction is at most 10 wt.% based on the total protein in the whey protein fraction. As such, Etzel teaches step (ii) of reducing the A1 β-casein derived proteose peptone content in the whey protein fraction of step (i) to a concentration which falls within the claimed concentration based on total protein in the whey protein fraction, thereby forming a reduced whey protein fraction. Since Etzel teaches steps (i) and (ii) of the method of present claim 6, it also teaches that the method produces a whey protein fraction having a reduced A1 β-casein derived proteose peptone as recited in present claim 6.
Furthermore, since the A1 β-casein derived proteose peptone content in the filtered whey protein fraction of Etzel is at most 10 wt.% based on the total protein in the whey protein fraction, the concentration of the at least one A1 β-casein derived proteose peptone selected from the group consisting of PP8 fast, PP8 slow, and PP-5 in the whey protein fraction after the reducing step is at most 10 wt.%. This concentration range of “at most 10 wt.%” encompasses the concentration recited in present claim 24. It would have been obvious to one of ordinary skill in the art to select any portions of the disclosed ranges including the instantly claimed ranges from the ranges disclosed in the prior art references, particularly in view of the fact that; "The normal desire of scientists or artisans to improve upon what is already generally known provides the motivation to determine where in a disclosed set percentage ranges is the optimum combination of percentages" In re Peterson 65 USPQ2d 1379 (CAFC 2003). Also In re Malagari, 182 USPQ 549,533 (CCPA 1974) and MPEP 2144.05.I.
Etzel also teaches that the method further comprises quantifying the degree of purity of the whey protein fraction using any method known to those skilled in the art [0104]. Therefore, Etzel teaches step (a) of claim 6 of providing a dairy-based product to be analyzed. Etzel does not teach steps (b)-(c) of the method as recited in present claim 6.
However, Elgar teaches that the most common method for analyzing whey proteins is liquid chromatography (LC), particularly high-performance liquid chromatography (HPLC) such as reversed-phase (RP) HPLC (page 184, column 1, 2nd paragraph). Elgar teaches that RP-HPLC can be coupled with electrospray ionization mass spectrometry (ESI-MS) for a more complete separation of major whey proteins such as proteose peptones with good recovery and, suitable for quantitation (abstract; page 184, column 1, 3rd paragraph). Determination and quantification of components by LC and MS is performed by detecting compounds of defined m/z values (corresponding to detecting bCN in the milk samples using the defined m/z values of bCN standards); and deconvoluting one or more mass spectrometry spectra to calculate monoisotopic masses as evidenced by Vincent (page 12, 2nd paragraph; page 16, Fig. 4, Panels F and H; pages 23-24, section labeled “1.2. Mass spectrometry”). Therefore, Elgar discloses subjecting a whey protein fraction to LC-MS analysis; and determining and/or quantifying the at least one A1 β-casein derived proteose peptone by detecting compounds of defined m/z values and deconvoluting one or more mass spectrometry to calculate monoisotopic masses as recited in steps (b) and (c) of present claim 6.
It would have been obvious for a person of ordinary skill in the art to have modified the method of Etzel to include subjecting a whey protein fraction to LC-MS analysis; and determining and/or quantifying the at least one A1 β-casein derived proteose peptone by detecting compounds of defined m/z values and deconvoluting one or more mass spectrometry to calculate monoisotopic masses as taught by Elgar. Since Etzel teaches that the method further comprises quantifying the degree of purity of the whey protein fraction using any method known to those skilled in the art [0104], a skilled practitioner would be motivated to consult Elgar in order to determine a suitable known method of determining and quantifying the proteins in the whey protein fraction of Etzel. In consulting Elgar, the skilled practitioner would readily recognize that RP-HPLC is a known method of quantifying milk proteins including proteose peptones comprising PP8 fast, PP8 slow, and PP-5 and that this known method may be coupled with ESI-MS in order to optimize the quantification process. Therefore, the combination of Etzel and Elgar renders subjecting a whey protein fraction to LC-MS analysis; and determining and/or quantifying the at least one A1 β-casein derived proteose peptone by detecting compounds of defined m/z values and deconvoluting one or more mass spectrometry to calculate monoisotopic masses as recited in steps (b) and (c) of present claim 6 obvious.
The combination of Etzel and Elgar does not teach that the analysis of the whey protein fraction comprises intact protein analysis or tryptic/GluC-digested peptide analysis.
However, Riggs teaches that the most common strategy in liquid chromatography is to tryptic digest all the proteins in a sample prior to subjecting the digested protein to chromatography (page 359, column 2, 2nd paragraph). Riggs discloses the tryptic digestion of milk prior to RPLC (abstract).
It would have been obvious for a person of ordinary skill in the art to have modified the method of modified Etzel to comprise tryptic digestion of a whey protein fraction prior to subjecting the whey protein fraction to liquid chromatography as taught by Riggs. Since Etzel teaches that the method further comprises quantifying the degree of purity of the whey protein fraction using any method known to those skilled in the art [0104]; and Elgar teaches that the most common method for analyzing whey proteins is LC (page 184, column 1, 2nd paragraph); and Riggs teaches that the tryptic digestion of protein prior to LC is the most common strategy used in chromatography (page 359, column 2, 2nd paragraph), a skilled practitioner would readily recognize that the whey protein fraction of Etzel may be subjected to tryptic digestion prior to LC. Therefore, the claimed peptide analysis comprising a step of tryptic digest of the whey protein fraction prior to peptide analysis is rendered obvious.
Regarding claim 7, Etzel teaches the invention as described above in claim 6, including reducing the content of the at least one A1 β-casein derived proteose peptone comprises gel filtration of the whey protein fraction (corresponding to ion exchange using gel beads [0035] and optionally, subsequent gel filtration [0102]) of the whey protein fraction.
Regarding claim 8, Etzel teaches a method for producing a nutritional composition (corresponding to foodstuffs, protein supplement, pharmaceutical formulation, or therapeutic application) containing a whey protein fraction (corresponding to a whey protein isolate), wherein at least 90 wt.% of the total solids in the whey protein fraction are β-lactoglobulin and α-lactalbumin [0014]-[0015]. Etzel teaches that the whey protein fraction is whey from cheesemaking that has undergone gel filtration (corresponding to ion exchange using gel beads and optionally, subsequent gel filtration) [0021], [0035], [0102]. Whey produced from cheesemaking comprises a mixture of different individual whey proteins including the β-casein derived proteose peptones PP8 fast, PP8 slow, and PP-5 (corresponding to component 8-fast, component 8-slow, and component 5, respectively) as evidenced by Yadav (page 764, column 1, paragraph under “4.2 Individual whey protein components”; page 765, column 1, paragraph under “4.2.7 Proteose-peptone component”); therefore, the provided whey protein fraction of Etzel contains at least one A1 β-casein derived proteose peptone selected from the claimed list. Etzel teaches that the whey from cheesemaking is subjected to gel filtration [0035], [0102] in order to produce the whey protein fraction wherein at least 90 wt.% of the total solids in the whey protein fraction are β-lactoglobulin and α-lactalbumin [0015]. Since the whey protein fraction contains at least 90 wt.% β-lactoglobulin and α-lactalbumin based on the total solids in the whey protein fraction, the A1 β-casein derived proteose peptone content in the whey protein fraction is at most 10 wt.% based on the total protein in the whey protein fraction. Therefore, Etzel teaches that the whey protein fraction is a reduced whey protein fraction having a reduced A1 β-casein derived proteose peptone content and teaches step (i) of providing a whey protein fraction and step (ii) of selecting the whey protein fraction having at most 10 wt.% of A1 β-casein derived proteose peptone based on the total protein in the whey protein fraction, forming a selected whey protein fraction as presently claimed. Etzel then teaches that the method comprises step (iv) of preparing a nutritional composition with the selected whey protein fraction [0014] as presently claimed. Since Etzel teaches the claimed method, Etzel teaches a method for producing a nutritional composition having a reduced -casein derived proteose peptone content as presently claimed. does not teach steps (b)-(c) of the method.
Etzel also teaches that the method further comprises quantifying the degree of purity of the whey protein fraction using any method known to those skilled in the art [0104]. Therefore, Etzel teaches step (ii) of claim 8 of determining and quantifying A1 β-casein derived proteose peptone (as a consequence of determining and quantifying the amount of whey in the whey protein fraction); and step (a) of claim 8 of providing a dairy-based product to be analyzed.
Etzel does not teach steps (b)-(c) of the method as recited in present claim 8.
However, Elgar teaches that the most common method for analyzing whey proteins is liquid chromatography (LC), particularly high-performance liquid chromatography (HPLC) such as reversed-phase (RP) HPLC (page 184, column 1, 2nd paragraph). Elgar teaches that RP-HPLC can be coupled with electrospray ionization mass spectrometry (ESI-MS) for a more complete separation of major whey proteins such as proteose peptones with good recovery and, suitable for quantitation (abstract; page 184, column 1, 3rd paragraph). Determination and quantification of components by LC and MS is performed by detecting compounds of defined m/z values (corresponding to detecting bCN in the milk samples using the defined m/z values of bCN standards); and deconvoluting one or more mass spectrometry spectra to calculate monoisotopic masses as evidenced by Vincent (page 12, 2nd paragraph; page 16, Fig. 4, Panels F and H; pages 23-24, section labeled “1.2. Mass spectrometry”). Therefore, Elgar discloses subjecting a whey protein fraction to LC-MS analysis; and determining and/or quantifying the at least one A1 β-casein derived proteose peptone by detecting compounds of defined m/z values and deconvoluting one or more mass spectrometry to calculate monoisotopic masses as recited in steps (b) and (c) of present claim 8.
It would have been obvious for a person of ordinary skill in the art to have modified the method of Etzel to include subjecting a whey protein fraction to LC-MS analysis; and determining and/or quantifying the at least one A1 β-casein derived proteose peptone by detecting compounds of defined m/z values and deconvoluting one or more mass spectrometry to calculate monoisotopic masses as taught by Elgar. Since Etzel teaches that the method further comprises quantifying the degree of purity of the whey protein fraction using any method known to those skilled in the art [0104], a skilled practitioner would be motivated to consult Elgar in order to determine a suitable known method of determining and quantifying the proteins in the whey protein fraction of Etzel. In consulting Elgar, the skilled practitioner would readily recognize that RP-HPLC is a known method of quantifying milk proteins including proteose peptones comprising PP8 fast, PP8 slow, and PP-5 and that this known method may be coupled with ESI-MS in order to optimize the quantification process. Therefore, the combination of Etzel and Elgar renders subjecting a whey protein fraction to LC-MS analysis; and determining and/or quantifying the at least one A1 β-casein derived proteose peptone by detecting compounds of defined m/z values and deconvoluting one or more mass spectrometry to calculate monoisotopic masses as recited in steps (b) and (c) of present claim 8 obvious.
The combination of Etzel and Elgar does not teach that the analysis of the whey protein fraction comprises intact protein analysis or tryptic/GluC-digested peptide analysis.
However, Riggs teaches that the most common strategy in liquid chromatography is to tryptic digest all the proteins in a sample prior to subjecting the digested protein to chromatography (page 359, column 2, 2nd paragraph). Riggs discloses the tryptic digestion of milk prior to RPLC (abstract).
It would have been obvious for a person of ordinary skill in the art to have modified the method of modified Etzel to comprise tryptic digestion of a whey protein fraction prior to subjecting the whey protein fraction to liquid chromatography as taught by Riggs. Since Etzel teaches that the method further comprises quantifying the degree of purity of the whey protein fraction using any method known to those skilled in the art [0104]; and Elgar teaches that the most common method for analyzing whey proteins is LC (page 184, column 1, 2nd paragraph); and Riggs teaches that the tryptic digestion of protein prior to LC is the most common strategy used in chromatography (page 359, column 2, 2nd paragraph), a skilled practitioner would readily recognize that the whey protein fraction of Etzel may be subjected to tryptic digestion prior to LC. Therefore, the claimed peptide analysis comprising a step of tryptic digest of the whey protein fraction prior to peptide analysis is rendered obvious.
Regarding claim 16, Etzel teaches the invention as described above in claim 8, including reducing the content of the A1 β-casein derived proteose peptone comprises gel filtration of the whey protein fraction (corresponding to ion exchange using gel beads [0035] and optionally, subsequent gel filtration [0102]) of the whey protein fraction.
Regarding claim 17, Etzel teaches the invention as described above in claim 8, including the selected whey fraction contains at least 95 wt.% whey protein comprising β-lactoglobulin and α-lactalbumin [0015]. Since the selected whey protein fraction contains at least 95 wt.% whey protein comprising β-lactoglobulin and α-lactalbumin based on the total solids in the selected whey protein fraction, the content of the A1 β-casein derived proteose peptone in the fraction is at most 5 wt.% based on the total protein in the whey protein fraction, which falls within the claimed A1 β-casein derived proteose peptone content, thereby forming a reduced whey protein fraction as presently claimed.
Regarding claim 18, Etzel teaches the invention as described above in claim 8, including the selected whey fraction contains at least 99 wt.% whey protein comprising β-lactoglobulin and α-lactalbumin [0015]. Since the selected whey protein fraction contains at least 99 wt.% whey protein comprising β-lactoglobulin and α-lactalbumin based on the total solids in the selected whey protein fraction, the A1 β-casein derived proteose peptone content in the fraction is at most 1 wt.% based on the total protein in the whey protein fraction, which falls within the claimed A1 β-casein derived proteose peptone content, thereby forming a reduced whey protein fraction as presently claimed.
Regarding claim 19, Etzel teaches the invention as described above in claim 8, including the nutritional composition is an infant formula [0143].
Regarding claim 20, Etzel teaches the invention as described above in claim 6, including the selected whey fraction contains at least 95 wt.% whey protein comprising β-lactoglobulin and α-lactalbumin [0015]. Since the selected whey protein fraction contains at least 95 wt.% whey protein comprising β-lactoglobulin and α-lactalbumin based on the total solids in the selected whey protein fraction, the content of the A1 β-casein derived proteose peptone in the fraction is at most 5 wt.% based on the total protein in the whey protein fraction, which falls within the claimed A1 β-casein derived proteose peptone content, thereby forming a reduced whey protein fraction as presently claimed.
Regarding claim 21, Etzel teaches the invention as described above in claim 6, including the selected whey fraction contains at least 99 wt.% whey protein comprising β-lactoglobulin and α-lactalbumin [0015]. Since the selected whey protein fraction contains at least 99 wt.% whey protein comprising β-lactoglobulin and α-lactalbumin based on the total solids in the selected whey protein fraction, the A1 β-casein derived proteose peptone content in the fraction is at most 1 wt.% based on the total protein in the whey protein fraction, which falls within the claimed A1 β-casein derived proteose peptone content, thereby forming a reduced whey protein fraction as presently claimed.
Claims 22-23 are rejected under 35 U.S.C. 103 as being unpatentable over Etzel (US 2009/0068326; previously cited) in view of Elgar (Elgar et al., “Simultaneous separation and quantitation of the major bovine whey proteins including proteose peptone and caseinomacropeptide by reversed-phase high performance liquid chromatography on polystyrene-divinylbenzene”, 2000, Journal of Chromatograph A, 878, pages 183-196; previously cited) and Riggs (Riggs et al., “Automated signature peptide approach for proteomics”, 2001, Journal of Chromatography A, 924, pages 359-368) as evidenced by Yadav (Yadav et al., “Cheese whey: A potential resource to transform into bioprotein, functional/nutritional proteins and bioactive peptides”, 2015, Biotechnology Advances, vol. 33, pages 756-774; previously cited) and Vincent (Vincent et al., “Quantitation and Identification of Intact Major Milk Proteins for High-Throughput LC-ESI-Q-TOP MS Analysis”, 2016, PLoS ONE, 11(10); IDS citation) as applied to claim 6 above, and further in view of Scigelova (Scigelova et al., “Orbitrap Mass Analyzer – Overview and Applications in Proteomics”, 2006, Practical Proteomics Journal, https://analyticalsciencejournals.onlinelibrary.wiley.com/doi/10.1002/pmic.200600528, pages 16-21; previously cited).
Regarding claims 22 and 23, modified Etzel teaches the invention as described above in claim 6, including the method comprises ESI-MS (Elgar, page 184, column 1, 3rd paragraph). Elgar discloses that the mass spectrometer may be a triple quadropole spectrometer (page 186, column 2, paragraph under section 2.11).
The prior art does not disclose that the mass spectrometry is a high resolution mass spectrometry performed at a resolution above 100,000 as recited in present claims 22 and 23.
However, Scigelova teaches ESI followed by MS wherein the spectrometer used is an orbitrap analyzer (page 18, Fig. 6). Scigelova teaches that, since the commercial introduction of the orbitrap analyzer, the orbitrap analyzer has become the instrument of choice by those skilled in the art due to its accuracy and high resolution (abstract; page 16, 1st-2nd paragraphs under “Introduction”). Scigelova teaches that the maximum resolution of the orbitrap analyzer is just over 100,000 (page 17, paragraph under “Resolving Power”), which overlaps the resolution recited in present claim 23, and thus qualifies as high resolution mass spectrometry as recited in present claim 22.
It would have been obvious for a person of ordinary skill in the art to have modified the method of modified Etzel to include using the orbitrap analyzer for mass spectrometry as taught by Scigelova. Elgar discloses that the method comprises ESI-MS; discloses a desire for high resolution in its method; and discloses using a triple quadropole spectrometer (page 184, column 1, 2nd - 3rd paragraphs; page 186, column 2, paragraph under section 2.11). Scigelova discloses ESI followed by MS wherein the spectrometer used is an orbitrap analyzer (page 18, Fig. 6). Therefore, Elgar discloses a comparable base device (i.e., a mass spectrometer for ESI-MS) upon which the claimed invention can be seen as an improvement (i.e., the claimed invention seeks to use a mass spectrometer having a high resolution). Since orbitrap analyzers are known in the art to have high accuracy and high resolution when compared to some other mass spectrometers, a skilled practitioner would have been motivated to apply this known spectrometer to the method comprising ESI-MS of the prior art. The practitioner would have had a reasonable expectation of success since the use of known techniques to improve similar methods in the same way renders the claimed invention obvious. MPEP 2143.I.D.
Response to Arguments
Claim Rejections – 35 U.S.C. §103 of claims 6-8, 16-21, and 24 over Etzel and Elgar as evidenced by Yadav and Vincent; claims 22-23 over Etzel, Elgar, and Scigelova as evidenced by Yadav and Vincent: Applicant’s arguments and amendments have been fully considered and are considered to overcome the rejections as written in the Final Office Action filed 12/22/2025. Therefore, those rejections are withdrawn, However, upon further consideration, the claims are now rejected as being rendered obvious by the combination of Etzel, Elgar, and Riggs as evidenced by Yadav and Vincent.
Applicant amended claims 6 and 8 to recite that determination and/or quantification of the proteose peptone(s) comprises intact protein analysis or tryptic- or GluC-digested peptide analysis. Applicant argued that the cited prior art does not teach such a feature or motivate a skilled practitioner to perform such a step (Applicant’s Remarks, page 6, 6th paragraph – page 9, 3rd paragraph).
However, in the new grounds of rejection, the features of claims 6 and 8 are rendered obvious by the combination of Etzel, Elgar, and Riggs as evidenced by Yadav and Vincent. As described above in the rejections of claims 6 and 8, Riggs teaches that the most common strategy in liquid chromatography is to tryptic digest all the proteins in a sample prior to subjecting the digested protein to chromatography (page 359, column 2, 2nd paragraph). Riggs also discloses the tryptic digestion of milk prior to RPLC (abstract). Since Etzel teaches that the method further comprises quantifying the degree of purity of the whey protein fraction using any method known to those skilled in the art [0104]; and Elgar teaches that the most common method for analyzing whey proteins is LC (page 184, column 1, 2nd paragraph); and Riggs teaches that the tryptic digestion of protein prior to LC is the most common strategy used in chromatography and discloses the tryptic digestion of milk prior to RPLC (abstract; page 359, column 2, 2nd paragraph), a skilled practitioner would readily recognize that the whey protein fraction of Etzel may be subjected to tryptic digestion prior to LC. Therefore, the claimed peptide analysis comprising a step of tryptic digest of the whey protein fraction prior to peptide analysis is rendered obvious.
Since the prior art is shown to render the present claims obvious, the rejections of the claims stand as written herein.
Conclusion
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/KELLY P KERSHAW/Examiner, Art Unit 1791