Detailed Action
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 .
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and the fee set forth in 37 CFR 1.17(e) has been timely paid, the finality of the previous Office action has been withdrawn pursuant to 37 CFR 1.114.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 03/09/2026, has been entered.
Status of Claims
Claims 1, 8-11, 15, and 16 are amended. Claims 2, 7, and 14 are cancelled. Claims 30 and 31 are withdrawn. Claims 32-34 are newly added. Claims -----1, 3-6, 8-13, 15-29, and 32-34 are currently under examination.
Priority
The examiner acknowledges claim to domestic priority for the instant application. It is noted that the earliest application that provides adequate support or enablement in the manner provided by 35 U.S.C. 112(a) or pre-AIA 35 U.S.C. 112, are provisional applications 63/077133, filed 09/11/2020 and 63077140, filed 09/11/2020.
Information Disclosure Statement
Information Disclosure Statement (IDS) filed on 03/09/2026 has been considered.
Response to Remarks filed 03/09/2026
Applicant’s arguments regarding the 35 USC 101 rejection of claims -----1, 3-6, 8-13, 15-29, and 32-34 have been fully considered and are not persuasive.
Specifically, Applicant argues that the claimed methods recite a step of "performing mass spectrometry to obtain a plurality of peptide sequences of human immunoglobulin heavy chain variable domains and/or human immunoglobulin light chain variable domains that were obtained from a sample comprising a population of antibodies produced by a rodent immunized with the antigen." The claimed methods further recite a step of "interrogating a library of human immunoglobulin heavy chain variable domain sequences and/or human immunoglobulin light chain variable domain sequences with the plurality of peptide sequences," wherein "the interrogation comprises aligning the peptide sequences of the plurality to each other and to the human immunoglobulin heavy chain variable domains and/or human immunoglobulin light chain variable domains of the library." The steps of "performing mass spectrometry" to obtain peptide sequences and "interrogating" by aligning the peptide sequences to each other and to the variable domain sequences in the library are steps that could not be performed mentally (e.g., with a pen or paper). Performing mass spectrometry involves using physical instrumentation and processing of samples that cannot be performed in the human mind. See, e.g., Example 4.1 of the Specification as filed. Similarly, alignment of peptide sequences to a library of variable domain sequences may involve handling a large number (e.g., thousands to millions) of sequences. Such scales makes it virtually (if not actually) impossible to perform mentally.
Applicant’s arguments have been fully considered but are not deemed persuasive. The claims comprise a judicial exception, specifically, an abstract idea (mental process), at least because the claims include an interrogation step that comprises aligning peptide sequences and an identification step identifying a human immunoglobulin variable domain sequence or CDR sequence of one or more antibodies that are specific for the antigen, and these are steps that can be carried out by the human mind. Furthermore, the claims do not include additional elements that are sufficient to amount to significantly more than the judicial exception(s). A claim that focuses on judicial exception(s) can be shown to recite something “significantly more” than the judicial exception(s) by reciting a meaningful limitation beyond the judicial exceptions. However, in the instant case, the claims do not include additional elements that are sufficient to amount to significantly more than the judicial exception because the additional elements (when considered both individually and as an ordered combination) are limited to well-understood, routine and conventional methods of identifying antibodies in a biological sample from a subject (“Step 2B”). Methods of identifying antibodies in biological samples is well-understood, routine, and conventional (see page 57 of Li et al (Li et al, pg. 57, Abstract); and Detailed Description at [0089-0094] on page 25-28 of the instant specification that disclose the methods for identifying antibodies are “conventional”).
Therefore, the 35 USC 101 rejection of claims 1, 3-6, 8-13, and 15-29 are maintained.
Applicant’s arguments with respect to the rejection of the claims under 35 USC 103 have been fully considered but are not persuasive. Applicant argues that the claimed invention fills a gap in the field of antibody identification. Applicant further argues The present claims recite a method comprising the steps of "performing mass spectrometry to obtain a plurality of peptide sequences ...," and "interrogating a library of human immunoglobulin heavy chain variable domain sequences and/or human immunoglobulin light chain variable domain sequences with the plurality of peptide sequences," wherein the interrogation comprises, inter alia, "aligning the peptide sequences of the plurality to each other and to the human immunoglobulin heavy chain variable domains and/or human immunoglobulin light chain variable domains of the library." None of the Cited References teach or suggest these steps.
For example, while the previous Non-Final Office Action asserted that Enzelberger discloses that "genome sequencing for antibody light chain and heavy chains can be done with Illumina Solexa, a next generation sequencing technique (Enzelberger et al, pg.1, paragraph 0003)," Enzelberger is entirely silent about performing mass spectrometry, let alone using such a technique to obtain peptide sequences. Non-Final Office Action, p. 12. Enzelberger further does not describe aligning any peptide sequences obtained by mass spectrometry to polypeptide sequences encoded by its determined nucleotide sequences. In other words, Enzelberger, at most, only provides half of the information, which alone is insufficient to identify which antibodies possess the desired characteristics. Not only does Enzelberger fail to disclose these steps, Enzelberger does not even contemplate the challenges that motivate Applicant's claimed approach. Enzelberger does not contemplate identifying antibodies present in circulation (e.g., in serum) with desired characteristics, nor does it bridge two categories of information-peptide-level information from antibodies circulating in vivo and nucleotide-level information reflecting the encoded B cells-to identify such antibodies.
Li likewise does not provide disclosure to fill the gaps in Enzelberger. To the extent that Li describes using mass spectrometry, it does so on a different sample, for an entirely different purpose-and ends up with a different set of information from the claimed methods. First, Li only characterizes two specific antibodies (mAb-X and mAb-Y), rather than performing mass spectrometry from a population of antibodies produced by a rodent with a germline genome as claimed. Li, 2.1. Second, Li uses mass spectrometry to evaluate glycosylation profiles, not to identify antibodies or peptides from antibodies that are present in circulation. Li, Introduction, 3.1, 3.2, Conclusion. Third, Li obtains information about antibody variants for biosimilar development, not information on which peptide sequences correspond to the variable domains encoded by nucleic acid sequences in B cells, as achieved by the claimed methods. Id. Indeed, Li does not use nucleotide sequences encoding variable domains or compare any of its mass spectrometry results (which the Office alleged includes peptide sequences) with any nucleotide sequences encoding variable domains, let alone using the combined information to identify antibodies with desired characteristics. None of Kucherlapati or Jakobovits remedy these deficiencies, as none of these references teach or suggest interrogating a library of variable domain sequences with peptide sequences obtained from mass spectrometry, as recited in the present claims.
The Cited References also do not contemplate the challenge that motivates Applicant's claimed approach-namely, the difficulty of linking antibodies (e.g., in circulation) having certain desired characteristics to the specific B cell source or nucleotide sequence encoding these antibodies-let alone Applicant's particular way of addressing that challenge. See also MPEP 2141.02(II) (stating "[A] patentable invention may lie in the discovery of the source of a problem...."). None of the Cited References teach or suggest an approach that bridges information about the variable region nucleotide sequences produced by B cells of the rodent and information about peptide sequences from the population of antibodies generated by the rodent. Therefore, a person of skill in the art would not have had any motivation to combine the references to arrive at the claimed approach, or any reasonable expectation of success in doing so.
Accordingly, as none of the Cited References, alone or in combination, teach or suggest the claimed methods, the present claims are patentable over the combination of the Cited References. Applicant respectfully requests reconsideration and withdrawal of this rejection.
However, as discussed in the 103, the combination of the prior art renders the claims obvious. It is initially noted that “[o]ne cannot show nonobviousness by attacking references individually where the rejections are based on combinations of references. In re Keller, 642 F.2d 413, 208 USPQ 871 (CCPA 1981); In re Merck & Co., Inc., 800 F.2d 1091, 231 USPQ 375 (Fed. Cir. 1986).”
Kucherlapati et al disclose the method of using an antigen to immunize a non-human animal capable of producing light chain and heavy chain variable regions (Kucherlapati et al, pg. 1, paragraph 0007). In the invention of referenced publication, the antibodies are human and specific for the antigen. The B-cells in the method of Kucherlapati et al secrete immunoglobulins that can be recovered from serum or primary B-cells (Kucherlapati et al, pg. 1, paragraph 0007). The referenced publication states that the XenoMouse can be used in a preferred embodiment for the above invention (Kucherlapati et al. pg. 2, 0028). Kucherlapati et al further disclose the method of aligning peptide sequences (Kucherlapati et al, pg. 13, paragraph 0148). Regarding Claim 1, the prior art teaches a method of immunizing a humanized rodent, obtaining peptide sequences encoding human light chain and heavy chain variable regions, and screening the library for an immunoglobulin with the desired affinity (Kucherlapati, claims 1-4). It is noted that aligning sequences is a routine method of screening (or interrogating) libraries.
Regarding claims 32-34, Enzelberger et al disclose the method can comprise cloning (Enzelberger et al, paragraphs 0053-0054).
Therefore, the 35 USC 103 rejection of claims 1, 3-6, 8-13, and 15-29 are maintained. The 35 USC 103 rejection of claim 2 and 7 is withdrawn due to cancellation of the claims. The 35 USC 103 rejections of claims 32-34 are added.
Previous Rejections Maintained- Nonfinal 04/18/2025 and Final 12/09/2025
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.
Claims 1, 3-6, 8-13, and 15-29 are rejected under 35 U.S.C. 101 because the claimed invention is directed to judicial exception(s) (i.e., a law of nature, a natural phenomenon, and/or an abstract idea) without significantly more. Abstract ideas include mathematical concepts (including mathematical relationships, formulas, equations, and calculations), mental processes (including concepts performed in the human mind), and certain methods of organizing human activity (including managing personal behavior, relationships, or interactions between people). The rationale for this determination is explained below:
Claims 1, 3-6, 8-13, and 15-29 are directed to abstract ideas because the claims recite abstract ideas (“Step 2A prong one”) and the judicial exception is not integrated into a practical application (“Step 2A prong two”). The “abstract ideas” include: the “obtaining” step of claims 1 and 2 and the “interrogating” step of claim 1, 15, 16 (all mental processes). The claim(s) does/do not include additional elements that are sufficient to amount to significantly more than the judicial exception(s). A claim that focuses on judicial exception(s) can be shown to recite something “significantly more” than the judicial exception(s) by reciting a meaningful limitation beyond the judicial exceptions. However, in the instant case, the claims do not include additional elements that are sufficient to amount to significantly more than the judicial exception because the additional elements (when considered both individually and as an ordered combination) are limited to well-understood, routine and conventional methods of identifying antibodies in a biological sample from a subject (“Step 2B”). Methods of identifying antibodies in biological samples is well-understood, routine, and conventional (see page 57 of Li et al (Li et al, pg. 57, Abstract); and Detailed Description at [0089-0094] on page 25-28 of the instant specification that disclose the methods for identifying antibodies are “conventional”). Well-understood, routine and conventional limitations are not meaningful limitations and are not enough to qualify the claimed method as reciting something “significantly more” than the judicial exception(s) (see Part I.B.1 of the interim Guidance).
MPEP 2106.05(d)(II) provides a non-limiting list of laboratory techniques recognized by courts as well-understood, routine, conventional activity. These techniques include:
i. Determining the level of a biomarker in blood by any means, Mayo, 566 U.S. at 79, 101 USPQ2d at 1968; Cleveland Clinic Foundation v. True Health Diagnostics, LLC, 859 F.3d 1352, 1362, 123 USPQ2d 1081, 1088 (Fed. Cir. 2017);
PNG
media_image1.png
18
19
media_image1.png
Greyscale
viii. Hybridizing a gene probe, Ambry Genetics, 774 F.3d at 764, 113 USPQ2d at 1247.
Recited active steps of the claims impose no meaningful limit on the scope of the claims, implicate a relevant pre-existing audience, and are recited at a high level of generality such that substantially all methods of identifying an antibody specific to an antigen of an immunized rodent would conventionally and routinely perform such steps. Here, the claims do not contain any significant additional elements or steps beyond the observation of judicial exception(s) present when performing routine and conventional methods. The active method steps are conventional and routine in the art for the reasons stated above and the claims do not amount to significantly more than the judicial exception(s). Further, just as methods comprising detecting paternal DNA sequences in particular samples by PCR was identified in Ariosa v. Sequenom as "well-known, routine, and conventional" (see first paragraph on page 13 of Ariosa Diagnostics, Inc. v. Sequenom, Inc. (Fed. Cir. 2015)) even though the prior art did not demonstrate detecting said paternal DNA sequences in said particular samples by PCR, the methods encompassed by the instant claims are well-known, routine, and conventional. The claims do not include additional elements that are sufficient to amount to significantly more than the judicial exception because the additional elements (common methods of detecting expression) are routinely performed in the art to obtain data regarding expression. In regards to “providing information” or “predicting”, it is further noted that merely presenting results of a process otherwise unpatentable under 35 U.S.C. 101 is insufficient to establish eligibility under the statute. See FairWarning IP, LLC v. Iatric Sys., Inc., No. 2015-1985, 2016 WL 5899185, at *3 (Fed. Cir. Oct. 11, 2016) (claim unpatentable under 35 U.S.C. 101 despite recitation of the step: “providing notification if [an] event has occurred”). Moreover, “[w]hile preemption may signal patent ineligible subject matter, the absence of complete preemption does not demonstrate patent eligibility…." Ariosa Diagnostics, Inc., v. Sequenom, Inc., 788 F.3d 1371, 1379 (Fed. Cir. 2015), cert. denied, No. 15-1182, 2016 WL 1117246 (U.S. June 27, 2016). Further, “Groundbreaking, innovative, or even brilliant discovery does not by itself satisfy the § 101 inquiry.” Ass’n for Molecular Pathology v. Myriad Genetics, Inc., 133 S. Ct. 2107, 2117 (2013). The claims do not recite something “significantly more” than the judicial exception(s); rather, the claims “simply inform” the natural phenomenon to one performing routine active method steps and do not amount to significantly more than the judicial exception(s).
As a result, the claims are not eligible subject matter under 35 U.S.C. 101.
Claim Rejections - 35 USC § 103
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.
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.
Claim(s) 1, 3-6, 8-13, and 15-29 are rejected under 35 U.S.C. 103 as being unpatentable over Kucherlapati et al (US20050054055, published 03/10/2005) in view of Enzelberger et al (US20100330577, published 12/30/2010), Jakobovits et al (CA2616914, published 05/29/2012) and (Li et al, Journal of Chromatography B, 1025 (2016) 57-67).
Regarding claims 1, 18, 25, 27, and 28, Kucherlapati et al disclose the method of using an antigen to immunize a non-human animal capable of producing light chain and heavy chain variable regions (Kucherlapati et al, pg. 1, paragraph 0007). In the invention of referenced publication, the antibodies are human and specific for the antigen. The B-cells in the method of Kucherlapati et al secrete immunoglobulins that can be recovered from serum or primary B-cells (Kucherlapati et al, pg. 1, paragraph 0007). The referenced publication states that the XenoMouse can be used in a preferred embodiment for the above invention (Kucherlapati et al. pg. 2, 0028). Kucherlapati et al further disclose the method of aligning peptide sequences (Kucherlapati et al, pg. 13, paragraph 0148). Regarding Claim 1, the prior art teaches a method of immunizing a humanized rodent, obtaining peptide sequences encoding human light chain and heavy chain variable regions, interrogating a library of human variable region sequences by aligning the obtained sequences to the sequences of the library, meeting the limitations disclosed in claim 1 of the instant application.
Regarding claims 3, 6, 27, and 28, claim 1 is discussed above. In the invention of the referenced publication, genes encoding the human antibodies can be prepared from B-cells obtained from blood or lymphoid tissues that include: spleen, tonsils, lymph nodes, and bone marrow and expressed in a recombinant host with or without modifications to produce the immunoglobulins (Kucherlapati et al, pg. 1, paragraph 0007).
It is noted that the XenoMouse is a rodent that comprises in its germline genome a heavy chain comprising human V, D, and J gene segments operably linked to a constant region and a light chain comprising human V and J gene segments operably linked to a constant region
It would be obvious to use the known method of developing human variable gene libraries and isolating human antibodies from lymphoid tissues that is taught in Kucherpalati in order to develop gene libraries and isolate human antibodies in the instant claims because one of ordinary skill in the art would be motivated with a reasonable expectation of success to develop gene libraries and isolate human antibodies by using the method of Kucherpalati which teaches a successful method of developing human variable gene libraries and isolating human antibodies .
Regarding claim 16, the invention of Kucherlapati et al discloses that the immunized animal can be used to generate a library for screening for variable regions for further manipulation to generate antibodies or analogs with desirable characteristics using standard recombination techniques (Kucherlapati et al, pg. 1, paragraph 0007). Although Kucherlapati does not specifically disclose the process of ranking in generating antibodies or analogs with desirable characteristics, ranking is simply a common practice in the art when choosing antibodies for desirable characteristics and would therefore be obvious to perform in the instant application.
Regarding claim 25, it is further noted that ADAM6 is not mutated in the model of Kucherlapati et al. and therefore, would be expected to function.
Kucherlapati et al does not disclose that a rat can be used as the non-human animal.
Regarding, claim 17, Enzelberger et al discloses that a rat may be immunized for the purposes of creating antibodies (Enzelberger et al, pg. 3-4, paragraph 0041). It would be obvious to combine the two teachings as one skilled in the art would be motivated to use a rat as simply taking one B-cell having mammal and replacing it with another would lead to predictable results and would have a reasonable expectation for success.
Kucherlapati et al and Enzelberger et al do not teach the sequencing of cDNA to obtain variable domain sequences of the library.
Regarding claim 4, the method of instant claim 1 is discussed above. Furthermore, Jakobovits discloses sequencing the cDNA of a XenoMouse for assessment of rearranged heavy chain and light chain variable regions (Jakobovits et al, pg. 30, paragraph 3).It would be obvious to use the known method of sequencing the cDNA of a XenoMouse that is taught in Jakobovits et al in order to develop gene libraries and isolate human antibodies in the instant claims because one of ordinary skill in the art would be motivated with a reasonable expectation of success to develop gene libraries and isolate human antibodies by using the combined teachings of Kucherpalati et al, Enzelberger et al, and Jakobovits to arrive at the method of claim 1, wherein the human immunoglobulin heavy chain variable domain sequences and/or human immunoglobulin light chain variable domain sequences of the library were obtained from sequencing of cDNA of the rodent that comprise rearranged heavy chain VDJ sequences and/or rearranged light chain VJ sequences because sequencing of cDNA.
Regarding claim 5, the method of claim 4 is discussed above. Furthermore, Enzelberger et al disclose that genome sequencing for antibody light chain and heavy chains can be done with Illumina Solexa, a next generation sequencing technique (Enzelberger et al, pg.1, paragraph 0003).
Regarding claims 4 and 5, it would be obvious to one skilled in the art to use a known method of sequencing heavy chains and light chains to sequence the same in the instant application to arrive at predictable results because it would be routine in the art to use next generation sequencing to sequence antibody light chains and heavy chains.
Kucherlapati, Enzelberger, and Jakobovits et al do not teach the method of sequencing with LC-MS after denaturing or proteolyzing the antibody specific to the antigen.
Regarding claims 7-9, the instant method of claim 1 is discussed above. Additionally, Li et al (Li et al, Journal of Chromatography B, 1025 (2016) 57-67) discloses the method of denaturing antigen specific antibodies to analyze by LC-MS, a method of mass spectrometry (Li et al, pg. 58, paragraph 2.2.3).
It would be obvious to one skilled in the art to use a method for determining light chain and heavy chain variable regions with LC-MS to determine light chain and heavy chain variable regions with LC-MS in the instant invention because you would arrive at predictable results because LC-MS is the most commonly used technique for the characterization of antibody variants (Li et al, pg. 57, Abstract).
Regarding claims 10-13, the instant method of claim 1 is discussed above. Li et al further discloses that the antibodies can undergo proteolysis prior to LC-MS (Li et al, pg. 58, paragraph 2.2.4) in order to facilitate enrichment of the antibodies for specific characteristics (Li et al, pg. 66, paragraph 2). It would be obvious to one skilled in the art to conduct proteolysis to enrich for smaller fragments as the smaller size fragments allows easier and more straightforward studies by LC-MS than intact IgGs (Li et al, pg. 59, paragraph 3.2). The limitation of claims 12 and 13 are fully addressed by claims 11 because in the specification antigen-specific means that it binds to an antigen and is unable to bind to other antigens. Therefore, there is no ability to enrich for antibodies that bind the antigen (claim 12) or deplete antibodies that bind a different antigen (claim 13).
Regarding claim 15, the method of claim 7 is discussed above. Furthermore, Jakobovits et al discloses interrogation of peptide sequences comprising matching CDR3 regions (Jakobovits et al, pg. 37, paragraphs 2-3). It would be obvious to one skilled in the art to use the methods of the referenced publication to compare CDR3 regions because it is known in the art that you can use CDR3 regions to compare the diversity of antibodies (Jakobovits et al, pg. 37, paragraphs 2-3).
Regarding claims 19-24, the instant method of claim 1 is discussed above. Furthermore, Jakobovits et al discloses a version of the XenoMouse, called the L6 mouse, that has human variable regions and mouse constant regions (Jakobovits et al, pg. 24, paragraphs 2-3). It would be obvious to one skilled in the art to replace one operable human constant region with an operable rodent constant region to arrive at the predictable results of an operable chimeric antibody that possesses improved immunogenicity.
Furthermore, regarding claims 21-24, Kucherlapati et al disclose that one would only need one human heavy chain and one human light chain to generate genes encoding immunoglobulins (Kucherlapati et al, pg. 2, paragraph 0027). It would be obvious to one skilled in the art to choose specific variable regions for known characteristics resulting in i) a universal light or heavy chain or ii) the restriction of heavy chain and light chain genes as a matter of mere experimentation which could result in a single variant of a heavy chain or a light chain in order to improve function.
"[W]here the general conditions of a claim are disclosed in the prior art, it is not inventive to discover the optimum of workable ranges by routine experimentation." Application of Aller, 220 F.2d 454, 456, 105 USPQ 233, 235-236 (C.C.P.A. 1955). "No invention is involved in discovering optimum ranges of a process by routine experimentation." Id. at 458, 105 USPQ at 236-237. The "discovery of an optimum value of a result effective variable in a known process is ordinarily within the skill of the art." Application of Boesch, 617 F.2d 272, 276, 205 USPQ 215, 218-219 (C.C.P.A. 1980).
Regarding claims 21-24, the claimed number of gene segments for heavy chains and light chains merely represent an obvious antibody variant with single V, D, J gene segments that would be arrived at by routine optimization of the values of the cited prior art. The gene segments are result effective variables in the range taught by Kucherlapati et al and so will be arrived at by routine experimentation. Additionally, one skilled in the art is motivated to perform the routine experimentation to optimize the heavy chains and light chains of antibodies for characteristics such as affinity, so it would be obvious to limit antibodies to known heavy or light chains with these characteristics (Kucherlapati et al, pg. 1, paragraph 007).
Regarding claim 26, the instant method of claim 1 is above. Furthermore, Enzelberger discloses the use of TdT for eukaryotic expression vectors. TdT is used for standard practice in the art and that renders this claim obvious.
Regarding claim 29, the instant method of claim 27 is described above. Furthermore, Kucherlapati et al disclose that the resulting antibody can be coupled to a variety of additional substances including fully human variable regions, creating bispecific antibodies (Kucherlapati et al, pg. 3, paragraph 0032). It would be obvious to one skilled in the art to use a known method for creating a bispecific antibody if the desire is to target various antigens simultaneously.
For the reasons above, all claims are deemed obvious and therefore, rejected.
Conclusion
No claim is allowed.
Any inquiry concerning this communication or earlier communications from the examiner should be directed to JOSEPHINE K DARPOLOR whose telephone number is (571)272-0115. The examiner can normally be reached 7:30ET-4:30ET.
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, Samira Jean-Louis can be reached at (571)270-3503. The fax phone number for the organization where this application or proceeding is assigned is 571-273-8300.
Information regarding the status of published or unpublished applications may be obtained from Patent Center. Unpublished application information in Patent Center is available to registered users. To file and manage patent submissions in Patent Center, visit: https://patentcenter.uspto.gov. Visit https://www.uspto.gov/patents/apply/patent-center for more information about Patent Center and https://www.uspto.gov/patents/docx for information about filing in DOCX format. For additional questions, contact the Electronic Business Center (EBC) at 866-217-9197 (toll-free). If you would like assistance from a USPTO Customer Service Representative, call 800-786-9199 (IN USA OR CANADA) or 571-272-1000.
/J.K.D./Examiner, Art Unit 1642
/NELSON B MOSELEY II/Primary Examiner, Art Unit 1642
Prosecution Insights