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 .
Status of the Claims
Claims 1-3, 11-14, 21, and 25-26 are pending in the application.
Claims 3 and 13-14 are withdrawn.
Claims 1-2, 11-12, 21, and 25-26 are the subject of 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and the fee set forth in 37 CFR 1.17(e) has been timely paid, the finality of the previous Office action has been withdrawn pursuant to 37 CFR 1.114.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 25 November 2025 has been entered.
Claim Objections
Claim 1 is objected to as containing abbreviations which are not explicitly defined before their first use in the claims (see “(LM)” and “(HM)” which first appear in part c of claim 1, but which are not explicitly defined until later in the claim).
Claim Rejections - 35 USC § 112(b)
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.
Claims 1-2, 21, and 26 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 1 is vague regarding “the two different labels”. There is no prior introduction of “two different labels” in the claim, therefore there is insufficient antecedent basis for this limitation in the claims.
Dependent claims 2, 21, and 26 are rejected as indefinite because they depend from indefinite claim 1 and fail to remedy its deficiencies.
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.
Claims 1-2, 11-12, and 26 are rejected under 35 U.S.C. 103 as being unpatentable over Egan (US 2010/0323343 A1; previously cited) in view of Christiaens et al ("Anti-homogalacturonan antibodies: a way to explore the effect of processing on pectin in fruits and vegetables," Food Res. Int. 44 (1): 225-234; published online 29 October 2010.; IDS entered) and Boehringer (US 6,924,153 B1; previously cited).
Regarding claims 1-2 and 11-12, Egan teaches a system for detecting one or more analytes in a sample (Abstract), the system comprising:
A sheet comprising a Control Zone with at least two immobilized unlabeled capture reagents (Par. 11; the device includes a plurality of addressable lines comprising one or more test zones and one or more control regions, and a plurality of capture moiety partners disposed in each of the addressable lines; Par. 170: a labeled reagent is restrained in each of the one or more control zones, even when any or all analytes of interest are absent from the test sample. The control zones may comprise antibodies specific for the labeled reagents (i.e. detection antibodies); Par. 111);
A test zone with at least three immobilized unlabeled anti-analyte capture antibodies (Par. 111-112: the test device includes a test membrane comprising one or more test zones and one or more control zones; Par. 38: the test device comprises immobilized reagents that capture analyte complexes in the sample; Par. 41-42: capture probe may comprise an antibody which binds specifically to the target analyte; Fig. 18: 1802; Fig. 19; Par. 11, 65, 111, 166, 222-224, 326, 335);
At least two labeled anti-analyte detection antibodies, wherein a first detection antibody is labeled with a first label, and a second detection antibody is labeled with a second label (Par. 40-42: a detection probe comprises an antibody which specifically binds to the target analyte and a detectable label; Fig. 18: 1801, 1809; Fig. 19; Par. 11, 65, 111, 166, 222-224, 326, 335; Par. 65: the sample collection device (SCD) may contain multiple different detection antibodies which may comprise different labels);
Wherein the system comprises a container and the at least two labeled detection antibodies are in the container (Par. 38: a sample collection device (SCD) is utilized to collect a sample and/or process a sample with immunoreactive reagents that provide a detection means and a capture means. The sample containing one or more analytes is mixed in a SCD to form a mixture that can be stored or reacted with specific binding reagents in the SCD and subsequently expelled to a test device that provides immobilized reagents that capture analyte complexes in the sample. The specific binding reagents in the SCD comprise detectable labels).
Egan teaches that the system can be used to detect a wide variety of analytes, including polysaccharide analytes (Par. 38: detection can include measurement of one or more analytes; Abstract; Par. 276: analytes include but are not limited to toxins, organic compounds, proteins, peptides, microorganisms, bacteria, viruses, amino acids, nucleic acids, carbohydrates, and more).
Further regarding claims 11-12, Egan teaches:
Contacting the labeled anti-analyte detection antibodies in a container with a sample, wherein a portion of the sample forms an analyte/labeled detection antibody complex (Par. 37-39);
Allowing the analyte-labeled detection antibody complex to flow through the sheet to reach the immobilized unlabeled anti-analyte capture antibodies in at the test zone (Par. 37-39; Fig. 19); and
Allowing the sample to reach the immobilized unlabeled capture reagents at the control zone to form a color pattern (Fig. 19: control line 1985 downstream from the capture zone; Par. 170: the control zone may comprise a capture reagent such as an antibody which specifically binds the labeled reagent which then produces a detectable signal in the control zone; Par. 166: the label of the labeled detecton antibody may comprise a visually detectable label such as a color label).
Egan does not explicitly teach that the capture and detection antibodies are anti-pectin antibodies such as LM19, LM20, and JIM7, and does not specifically teach the system comprising a template guide.
Regarding claims 1-2 and 11-12, Christiaens teaches a system for determining degree and distribution of pectin HG methyl-esterification (Abstract).
Christiaens teaches the system comprising anti-pectin antibodies which are used in an immunoassay to determine degree and distribution of pectin HG methyl-esterification (Abstract: anti-homogalacturonan antibodies JIM5, JIM7, LM7, LM18, LM19, LM20, and PAM1; Section 2.3 Immunodot assays).
It would have been obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to have modified the system of Egan to include anti-pectin capture and detection antibodies for the detection of pectin and for the characterization of the degree and distribution of pectin HG methyl-esterification, as taught by Christiaens. One of ordinary skill in the art would be motivated to modify the system for the detection of pectin because Christiaens teaches that pectin is of particular interest to food technologists due to the role it plays in the processing and texture of fruits and vegetables. One of ordinary skill in the art would have a reasonable expectation of success in making this modification because Egan discloses an immunoassay system which may comprise multiple species of capture and detection monoclonal antibodies for the detection of a target analyte which may be a carbohydrate or polysaccharide, and Christiaens teaches specific monoclonal antibodies which can be used for the detection and characterization of pectin in an immunoassay.
Christiaens further discloses that each species of antibody (i.e.JIM5, JIM7, LM18, LM19, LM20, and PAM1) has binding affinity to HG which is impacted by the degree and pattern of methyl-esterification of the pectin (Section 3.2.1). Specifically, Christiaens teaches:
Antibody
Binding Behavior
Citation
JIM5
Binding strength seems to increase with decreasing DE, but becomes weaker again when the DE falls below about 20%; both the degree and pattern of de-esterification influence the binding capacity of JIM5
Pg. 229, Col. 1, last Par.-Col. 2, first Par.
JIM7
The broad affinity of JIM7 towards pectin with very diverse degrees and pattern of methyl-esterification suggests the application of this antibody as a general anti-pectin probe
Pg. 229, Col. 2, Par. 2
LM18
Binding of LM18 to pectin increases with decreasing DE. LM18 has a preference for F-series (and C-series) pectins. A very low DBabs results in absence of binding of LM18, indicating that some block of non-methylesterified GalA residues are necessary for recognition
Pg. 230, Col. 1, Par. 1
LM19
Binds more strongly to pectin with a lower DE. The absence of LM19 binding to chemically (randomly) de-esterified pectin with a DE>50% shows that the pattern of methylesterification plays a role in LM19 binding. Binding strength generally increases with increasing DBabs
Pg. 230, Col. 1, Par. 2
LM20
Binding decreases with decreasing DE. Does not bind to F- and C-series pectin with very low DE. A low DBabs and a high DE generally result in stronger binding of LM20 than a high DBabs and a low DE. Instead of an increase in intensity, as was the case for LM18 and LM19, binding of LM20 will decrease upon de-esterification
Pg. 230, Col. 1, Par. 3
PAM1
The pattern of methyesterification has a larger influence on the binding capacity of PAM1 than the degree of methylesterification. The binding strength of PAM1 correlates with the increase in DBabs
Pg. 230, Col. 1, last Par.-Col. 2, first Par.
Thus, the immunodot assay results and analysis provided by Christiaens (Section 2.3; Section 3.2.1, Figs. 2-4) show that the different antibodies display different binding patterns and properties based on the degree and pattern of methyl-esterification of the pectin. Though Christiaens concedes that some or all of the antibodies lack an unequivocal trend in binding behavior based on degree and pattern of methylesterification (Pg. 230) the reference indicates that there are general trends in binding behavior of each antibody based on degree and pattern of methylesterification, and explicitly teaches that these observed trends in binding behavior can be used to assess the degree and pattern of methylesterification when the antibodies are used in combination (Pg. 233, Col. 1, last Par.: the possibility to combine the labeling patterns and binding specificities of the different anti-HG antibodies finally provides insight into the distribution of pectin methylesterification throughout the cell wall) (i.e. the results of the immunoassay may be evaluated to determine the pectin sample’s degree of methylesterification as LM or HM and the distribution of methylesterification as random, semi-random, or block-wise).
It would have been obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to have modified the system of Egan in view of Christiaens to further include the particular anti-pectin antibodies disclosed by Christiaens (e.g. JIM7, LM19, LM20) as the capture and detection antibodies in the system. One of ordinary skill in the art would be motivated to use these antibodies in combination to provide insight into the degree and pattern of methylesterification of pectin for the purpose of investigating the effects of processing conditions, as taught by Christiaens. One would be motivated to use the specific combination of antibodies recited in the instant claim (i.e. JIM7 and LM20 detection antibodies and JIM7, LM19, and LM20 capture antibodies), because Christiaens teaches that each antibody has unique binding properties which allow one to determine specifical properties of methyl-esterification, such that their use in combination allows for more complete characterization of both the degree and pattern of methylesterification. Alternatively, one could also be motivated to use all the antibodies disclosed by Christiaens in combination (i.e. JIM5, JIM7, LM18, LM19, LM20, and PAM1 as both capture and detection antibodies) for the purpose of gathering a larger amount of data on the degree and pattern of methylesterification. Wherein maximizing data gathered would be advantageous to drawing more accurate conclusions about the degree and pattern of methylesterification. Arrival at the claimed combination is additionally obvious because from the finite number of possibilities (i.e. species of antibodies) disclosed by Christiaens, one of ordinary skill in the art designing the multiplexed detection system of Egan in view of Christiaens would arrive at the specifically claimed combination (or a system comprising the specifically claimed combination) of capture and detection antibodies because it would be obvious to try. One of ordinary skill in the art would have a reasonable expectation of success in making this modification because Egan teaches an immunoassay which may detect multiple different target analytes or subtypes of target analytes using multiple species of capture and detection antibodies, while Christiaens teaches specific species of antibodies for use in such an immunoassay.
As an example, in a system of Egan in view of Christiaens which comprises JIM7, LM20 and LM19 capture antibodies and jIM7 and LM20 detection antibodies, a sample which yields strong binding of JIM7 and LM20 and low binding affinity for LM19 could be concluded to have a high degree of methylesterification (i.e. HM) and a low DBabs (i.e. random pattern of methylesterification), while a sample which yields strong binding of JIM7 and LM19 and low binding affinity of LM20 could be concluded to have a low degree of methylesterification (i.e. LM) and a high DBabs (i.e. block-wise pattern of methylesterification); wherein both conclusions could be made with a reasonable expectation of success based on the teachings and observations of Christiaens.
Such expectation of success would be further increased in a system which comprises additional species of capture and detection antibodies (e.g. JIM5, LM18, and PAM1), since the binding results yielded by these antibodies in addition to the binding results yielded by JIM7, LM19, and LM20 would give one more data from which to draw and confirm conclusions about the degree and pattern of methylesterification in the pectin sample.
Regarding the recitation in the preamble of claim 1 “for determining degree and distribution of pectin homogalacturonan (HG) methyl-esterification of a pectin sample”: the normal purpose of a claim preamble is to recite the purpose or intended use of the claimed invention. Such statements merely define the context in which the invention operates and usually will not limit the scope of the claim or distinguish it over the prior art (MPEP 2111.02). When the body of the claim fully and intrinsically sets forth the complete invention, including all of its limitation, and the preamble offers no distinct definition of any of the claimed invention’s limitation, but rather merely states, for example, the purpose or intended use of the invention, then the preamble is not of significance to claim construction because it cannot be said to constitute or explain a claim limitation (MPEP 2111.02(II)). Further, a recitation of intended use in a claim directed to a system does not distinguish over the prior art (even if it is recited in the body of the claim rather than in the preamble), because a claim directed to a system is defined by what the system is and not what it does (i.e. the claim is only limited by the components of the system and their structural features). As long as the prior art teaches the components and structural features of the claimed system, it is assumed to be able to perform the recited function and is understood to meet the instant claim, regardless of whether it is disclosed to be for the same intended use. See MPEP 2114 and 2115.
Similar rationale applies to the recitation in claim 1 “the system allowing a user to determine the pectin sample and degree of methyl esterification as low (LM) or high (HM), and its methyl esterification distribution as random, semi-random, or block-wise” which is a functional limitation of the claimed system and/or a recitation of intended use (i.e. this recitation does not define a physical component or structural feature of the claimed system). As described above, since a claim to a system is defined by its structural features, prior art which teaches all structural features of the claimed system is understood to be inherently capable of performing the claimed function, and is therefore understood to meet the instant claim, regardless of whether the function is explicitly taught in the reference (because there is no structural or physical distinction between the claimed system and the system taught by the prior art).
Regarding claims 1-2 and 11-12, Boehringer teaches a system comprising an immunoassay test strip for the detection of one or more analytes in a sample (Abstract; Fig. 1). Boehringer further teaches that instructions may be provided in a kit comprising the test strip, wherein the instructions provide a user with guidance for interpreting assay results and which comprise a chart or table which correlates the pattern of signal observed with the test results (Col. 20, Ln. 60-67).
It would have been obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to have further modified the system of Egan in view of Christiaens to include a template guide with which to compare the color pattern observed on the sheet to determine the assay results (i.e. to determine detection of pectin and to determine the pectin sample’s HG methyl-esterification) as taught by Boehringer. One would be motivated to provide the template guide to assist the user in interpreting the assay results. One of ordinary skill in the art would have a reasonable expectation of success in making this modification because both Egan and Boehringer are directed to systems comprising an immunoassay test strip.
Claim 1 further recites limitations regarding the particular content of the Template Guide which is used to interpret results yielded from the claimed system. These particular contents of the Template Guide (i.e. printed matter) do not serve to further limit the claimed system or distinguish it over the prior art. See MPEP 2111.05: Once it is determined that the limitation is directed to printed matter, the examiner must determine if the matter is functionally or structurally related to the associated physical substrate. Regarding evidence for or against such a functional relationship, 2111.05 further provides: A functional relationship can be found where the printed matter performs some function with respect to the product to which it is associated. Where the printed matter and product do not depend upon each other, no functional relationship exists. For example, in a kit containing a set of chemicals and a printed set of instructions for using the chemicals, the instructions are not related to that particular set of chemicals.
Similarly, MPEP 2112.01(III) further provides: where the only difference between a prior art product and a claimed product is printed matter that is not functionally related to the product, the content of the printed matter will not distinguish the claimed product from the prior art. See In re Ngai, 367 F.3d 1336, 1339, 70 USPQ2d 1862, 1864 (Fed. Cir. 2004) (Claim at issue was a kit requiring instructions and a buffer agent. The Federal Circuit held that the claim was anticipated by a prior art reference that taught a kit that included instructions and a buffer agent, even though the content of the instructions differed, explaining "[i]f we were to adopt [applicant’s] position, anyone could continue patenting a product indefinitely provided that they add a new instruction sheet to the product."). See also In re Gulack, 703 F.2d 1381, 1385-86, 217 USPQ 401, 404 (Fed. Cir. 1983) ( "Where the printed matter is not functionally related to the substrate, the printed matter will not distinguish the invention from the prior art in terms of patentability….[T]he critical question is whether there exists any new and unobvious functional relationship between the printed matter and the substrate."
As it applies to the instant case, the printed matter (i.e. the particular contents of the Template Guide) do not have a functional relationship to the claimed system, because they merely provide instructions for the intended use of the claimed system, and do not further limit the function and structure of the system itself. This is similar to the examples discussed above wherein courts have determined that the particular contents of instructions included with a kit do not share a functional relationship with the contents of the kit itself, and do not serve to further limit the product over the prior art. As such, prior art which teaches all physical components of the claimed system and which teaches the inclusion of a Template Guide within that system is sufficient to meet the instant claim, regardless of whether the particular contents of the Template Guide differ from what is claimed.
Regarding claim 26, Egan teaches that the immunoassay system/method may comprise multiple control zones configured for the immobilization of multiple different labeled reagents (e.g. labeled detection antibodies), wherein the reagent in the control zone which immobilizes the detection antibody may itself be an antibody that is specific for the detection antibody (Par. 170: : one or more control zones are useful to verify that the sample flow is as expected. Each of the control zones typically comprise a spatially distinct region that often includes an immobilized member of a specific binding pair which reacts with a labeled reagent. Each control zone may contain an antibody that is specific for the immobilization of each labeled reagent (e.g. detection antibody)). Wherein the use of multiple control zones specific for multiple types of detection antibodies is desirable for confirming the proper function of each different detection antibody.
Christiaens teaches that JIM7 is an IgA antibody and that LM20 is an IgM antibody (Table 1).
Though Egan does not explicitly teach the use of anti-IgM and anti-IgA secondary antibodies as the unlabeled capture reagents of the control zone, it would have been obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to have modified the system of Egan in view of Christiaens to comprise anti-IgM and anti-IgA in each of two different control zones for the purpose of immobilizing the detection antibodies in an embodiment of the system which comprises labeled JIM7 IgA detection antibodies and labeled LM20 IgM detection antibodies (as discussed above) to confirm the function of each species of detection antibody. One of ordinary skill in the art would have a reasonable expectation of success in making this modification because Egan teaches that each control zone may comprise a reagent capable of specifically binding to a labeled detection reagent.
Claims 21 and 25 are rejected under 35 U.S.C. 103 as being unpatentable over Egan (US 2010/0323343 A1; previously cited) in view of Christiaens et al ("Anti-homogalacturonan antibodies: a way to explore the effect of processing on pectin in fruits and vegetables," Food Res. Int. 44 (1): 225-234; published online 29 October 2010.; IDS entered) and Boehringer (US 6,924,153 B1; previously cited), as applied to claims 1 and 11 above, and further in view of Herrera et al (WO 2021/222597 A2; previously cited).
Regarding claims 21 and 25, Egan teaches that each species of labeled detection antibody may be labeled with a different substance (Par. 65: the sample collection device (SCD) may contain multiple different detection antibodies which may comprise different labels for the detection of different analytes). Egan further teaches that the labels used for detection antibodies may comprise colloidal gold (Par. 278: “Label” refers to any substance which is capable of producing a signal that is detectable by visual or instrumental means. Suitable labels include colloidal gold), but does not specifically teach that the labels comprise spherical gold nanoparticles or gold nanourchins.
Regarding claims 21 and 25, Herrera teaches an immunoassay comprising a capture reagent immobilized on a solid support, and a detection reagent labeled with a visualizing reagent, wherein the detection reagent may be an antibody which is labeled with a visualizing reagent which may be a spherical gold nanoparticular or a gold nanourchin (Abstract; Par. 20, 25, 160).
It would have been obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to have modified the invention of Egan in view of Christiaens to further include the JIM7 and LM20 detection antibodies labeled with different substances, wherein the different substances are spherical gold nanoparticles and gold nanourchins, as taught by Herrera. One of ordinary skill in the art would be motivated to make this modification because Egan teaches that different species of detection antibodies can be labeled with different labeling substances, and teaches that such labeling substances may comprise gold labels, which would include gold nanoparticles and gold nanourchins. Specific use of the gold nanoparticles and gold nanourchins disclosed by Herrera would be advantageous because the nanoparticles and nanourchins are labels with different size an color, such that one could discern one detection antibody from the other in the immunoassay results by observing or detecting different colors of the detection antibody labels. One of ordinary skill in the art would have reasonable expectation of success in making this modification because both Egan and Herrera are directed to immunoassays comprising detection antibodies labeled with gold visualizing reagents.
Response to Arguments
Applicant’s arguments filed 25 November 2025 have been fully considered.
The previous 112(b) rejections over the terms “low” and “high” in claims 1 and 11 are overcome by the amendment to claim 1 which specifically defines the terms, and the rejection is withdrawn.
Regarding the previous 112(b) rejections over the terms “random”, “semi-random”, and “block-wise”, applicant argues that these are terms commonly used in the pectin field of study to described the distribution of methyl ester groups and unesterified galacturonic acid residues in a pectin sample. As such, applicant submits that a person of ordinary skill in the relevant art would understand the meaning and scope of these terms. This argument is persuasive and the 112(b) rejection is withdrawn.
All other previous 112(b) rejections are overcome by amendments to the claims, and all previous 112(b) rejections are withdrawn.
New grounds of 112(b) rejection are presented above.
Regarding the 103 rejection, applicant argues that the cited prior art does not teach the amended limitations of the template guide of claim 1. This argument is not persuasive, as discussed in the rejection above, because the particular contents of the Template Guide do not serve to distinguish the claimed system over the prior art.
Applicant argues that prior to the instant application, one of ordinary skill would not have known which antibodies disclosed by Christiaens to use in the modified system of Egan or in which portions of the Egan system to add them, which combination of antibodies disclosed by Christiaens to use as labeled detection antibodies, what substances to use to label the detection antibodies, or what pattern on the system would indicate a pectin sample’s degree or distribution of methyl-esterification, as taught by the claimed template guide. This argument is not persuasive. As discussed in the 103 rejection above, Christiaens identifies particular trends in the binding behavior of each disclosed antibody, wherein trends in binding behavior are reflective of differences in the pattern and distribution of methyl-esterification. Christiaens further explicitly posits that these antibodies may be used in combination (e.g. in a system such as the one taught by Egan) such that the trends in binding behavior of each antibody may be observed in combination and used to determine the degree and distribution of methyl esterification. The rejection above explicitly discusses exemplary embodiments wherein one of ordinary skill in the art could use the teachings of Christiaens in the modified system of Egan in view of Christiaens to draw conclusions about degree and pattern of methyl esterification with a reasonable expectation of success.
The previous 103 rejection is withdrawn in favor of the new grounds of 103 rejection above which addresses the amendments to the claims.
Conclusion
Any inquiry concerning this communication or earlier communications from the examiner should be directed to ELLIS LUSI whose telephone number is (571)270-0694. The examiner can normally be reached M-Th 8am-6pm ET.
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/ELLIS FOLLETT LUSI/Examiner, Art Unit 1677
/CHRISTOPHER L CHIN/Primary Examiner, Art Unit 1677