Prosecution Insights
Last updated: April 19, 2026
Application No. 17/705,924

Methods for Detecting Symmetrical Dimethylarginine

Non-Final OA §103§112
Filed
Mar 28, 2022
Examiner
EMCH, GREGORY S
Art Unit
1678
Tech Center
1600 — Biotechnology & Organic Chemistry
Assignee
IDEXX Laboratories, Inc.
OA Round
3 (Non-Final)
50%
Grant Probability
Moderate
3-4
OA Rounds
3y 7m
To Grant
93%
With Interview

Examiner Intelligence

Grants 50% of resolved cases
50%
Career Allow Rate
305 granted / 615 resolved
-10.4% vs TC avg
Strong +44% interview lift
Without
With
+43.6%
Interview Lift
resolved cases with interview
Typical timeline
3y 7m
Avg Prosecution
37 currently pending
Career history
652
Total Applications
across all art units

Statute-Specific Performance

§101
7.5%
-32.5% vs TC avg
§103
29.7%
-10.3% vs TC avg
§102
19.7%
-20.3% vs TC avg
§112
22.1%
-17.9% vs TC avg
Black line = Tech Center average estimate • Based on career data from 615 resolved cases

Office Action

§103 §112
Notice of Pre-AIA or AIA Status The present application is being examined under the pre-AIA first to invent provisions. DETAILED ACTION Responsive to communication entered 12/23/2025. 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and the fee set forth in 37 CFR 1.17(e) has been timely paid, the finality of the previous Office action has been withdrawn pursuant to 37 CFR 1.114.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 submissions filed on 12/23/2025 have been entered. Priority This application, filed on 03/28/2022, Pub. No. US 2022/0221446 A1, published 07/14/2022, is a continuation of U.S. Patent Application Serial No. 15/977,284, filed on 05/11/2018, Pub. No. US 2018/0335423 A1, published 11/22/2018, now abandoned, which is a continuation of U.S. Patent Application Serial No. 14/192,956, filed 02/28/2014, Publication No. US 2014/0242723 A1, issued as U.S. Patent No. 9,970,927, on May 15, 2018, which is a continuation of U.S. Patent Application Serial No. 13/918,531, filed June 14, 2013, Pub. No. US 2013/0280740 A1, issued as U.S. Patent No. 9,091,684, on July 28, 2015, which is a continuation of U.S. Ser. No. 12/512,479 filed 07/30/2009, Pub. No. US 2010/0035274 A1, issued as U.S. Patent No. 8,481,690, on July 9, 2013, which claims the benefit of U.S. Provisional Patent Application 61/086,870, filed on 08/07/2008. Status of Claims Claims 1, 2 and 5 are currently pending. Claims 1-5 have been originally pending and subject to election/restriction requirement mailed 10/24/2024. Claims 1, 4 and 5 have been amended, and Claim 3 has been cancelled, as set forth in Applicant’s amendment filed 08/11/2025. Claims 1 and 5 have been amended, and Claim 4 has been cancelled, as set forth in Applicant’s amendment filed 12/23/2025. Claims 1, 2 and 5 are examined. Withdrawn Objections/Rejections Any objection or rejection not reiterated herein has been withdrawn. The rejections of Claim 4 are moot in view of Applicant’s cancellation of Claim 4. The objection to Claim 1 is withdrawn in view of Applicant’s amendment of the claim. The rejection of Claims 1 and 2 under 35 U.S.C. 112(a) or 35 U.S.C. 112 (pre-AIA ), first paragraph (“new matter”), is withdrawn in view of Applicant’s amendment of the claims. Claim Rejections - 35 USC § 112 The following is a quotation of the appropriate paragraphs of 35 U.S.C. 112 that form the basis for the rejections under this section made in this Office action. The following is a quotation 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 35 U.S.C. 112 (pre-AIA ), first paragraph: 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. 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 and 5 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 claim(s) 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 pre-AIA the inventor(s), at the time the application was filed, had possession of the claimed invention (“genus-species”). The claims, as recited in independent amended Claim 1, are drawn to: PNG media_image1.png 228 1048 media_image1.png Greyscale It is the Examiner's position that the instant specification fails to provide adequate written description and clear guidance for devices comprising SDMA attached to a solid phase, wherein the SDMA is attached to a solid phase through a genus of modifications of a carboxylic acid group of the SDMA, which as claimed, and does not reasonable convey to one skilled in the relevant art that the inventor(s), at the time the application was filed, had possession of the entire scope of the claimed invention. The Examiner's position is based on the following facts and considerations. First, the disclosure as filed is limited to synthesis of the symmetrical dimethylarginine (SDMA) cystamide (3) and its conjugates with keyhole limpet hemocyanin (KLH), bovine serum albumin (BSA) or horse radish peroxidase (HRP) used as an immunogen for generating antibodies capable of selective recognition of SDMA over a symmetrical dimethylarginine (ADMA) or as a detectable compound in an SDMA immunoassay, respectively. This single compound clearly does not represent a sufficient number of species to reflect the structural variation within the claimed genus of modifications of a carboxylic acid group of the SDMA. Second, there is no evidence on record that any other compound, except for the SDMA cystamide (3), can be used in the claimed device for determining the presence of free symmetrical dimethylarginine (SDMA) in a patient sample. On the contrary, one of ordinary skill in the art would have known that structural modifications preserving ability of an SDMA analog to compete with SDMA for a receptor, such as an antibody, are unpredictable from the standpoint of receptor specificity. See, for example, Englebienne, “Immune and Receptor Assays in Theory and Practice,” CRC Press, 2000, p. 308 (IDS submitted 04/12/2022), teaching that the antibody specificity depends on composition of a linker conjugating an analog to a solid phase: PNG media_image2.png 156 747 media_image2.png Greyscale Emphasis added. Therefore, the scope of the instantly claimed broad genus of SDMA “attached to a solid phase through modification of a carboxylic acid group of the SDMA, wherein the modification converts the carboxylic acid group to an amide bond” is not satisfied through sufficient description of a representative number of species by actual reduction to practice at the time of the invention, or by disclosure of relevant, identifying characteristics, i.e., structure or other physical and/or chemical properties, by functional characteristics coupled with a known or disclosed correlation between function and structure, or by a combination of such identifying characteristics, sufficient to show the Applicant was in possession of the claimed genus. See MPEP § 2163. Accordingly, Claims 1, 2 and 5 do not meet the written description provision of 35 U.S.C. §112(a) or 35 U.S.C. §112 (pre-AIA ), first paragraph. Claim 5 is rejected under 35 U.S.C. 112(b) or 35 U.S.C. 112 (pre-AIA ), second paragraph, as being indefinite for failing to particularly point out and distinctly claim the subject matter which the inventor or a joint inventor (or for applications subject to pre-AIA 35 U.S.C. 112, the applicant), regards as the invention. The subject matter of Claim 5 is unclear because Claim 5 is drawn to the device of the cancelled Claim 4. Claim Rejections - 35 USC § 103 The following is a quotation of pre-AIA 35 U.S.C. 103(a) which forms the basis for all obviousness rejections set forth in this Office action: (a) A patent may not be obtained though the invention is not identically disclosed or described as set forth in section 102 of this title, if the differences between the subject matter sought to be patented and the prior art are such that the subject matter as a whole would have been obvious at the time the invention was made to a person having ordinary skill in the art to which said subject matter pertains. Patentability shall not be negatived by the manner in which the invention was made. The factual inquiries set forth in Graham v. John Deere Co., 383 U.S. 1, 148 USPQ 459 (1966), that are applied for establishing a background for determining obviousness under 35 U.S.C. 103(a) are summarized as follows: 1. Determining the scope and contents of the prior art. 2. Ascertaining the differences between the prior art and the claims at issue. 3. Resolving the level of ordinary skill in the pertinent art. 4. Considering objective evidence present in the application indicating obviousness or nonobviousness. Claims 1, 2 and 5 are rejected under pre-AIA 35 U.S.C. 103(a) as being unpatentable over Bode-Böger et al., “Symmetrical Dimethylarginine: A New Combined Parameter for Renal Function and Extent of Coronary Artery Disease,” J. Am. Soc. Nephrol., 2006, vol. 17, pp. 1128-1134 (IDS submitted 04/12/2022), in view of Buechler et al. WO 2006/078813, published 07/27/2006 (IDS submitted 04/12/2022). Bode-Böger et al., throughout the publication, and, for example, in Abstract, teach that SDMA reduces the endothelial NO synthesis, probably by limiting L-arginine supply to NOS, and might be a useful marker for detecting patients in very early stages of chronic kidney disease and for determining their risk for developing cardiovascular disease: PNG media_image3.png 452 1314 media_image3.png Greyscale Emphasis added. At page 1129, left column, third paragraph, Bode-Böger et al. teach determination of levels of L-arginine, SDMA, ADMA, and citrulline as ortho-phthalaldehyde derivatives by liquid chromatography–mass spectrometry (LC-MS) in plasma samples of 147 patients before elective coronary angiography. In Materials and Methods, Bode-Böger et al. teach employment of the Martens-Lobenhoffer et al. method provides for determining the presence of free symmetrical dimethylarginine (SDMA) in a patient sample, such as serum, which the elected species (a): PNG media_image4.png 125 590 media_image4.png Greyscale PNG media_image5.png 152 594 media_image5.png Greyscale Bode-Böger et al. do not teach a device comprising SDMA attached to a solid phase, wherein the SDMA is attached to a solid phase through modification of a carboxylic acid group of the SDMA, as recited in the instant Claim 1. Buechler et al., throughout the publication, and, for example, in Abstract, teach the preparation of arginine analogs, which analogs are designed to provide a free thiol (SH) group, providing a linkage chemistry for convenient coupling, under mild conditions, to a suitable group on a target protein, polypeptide, or label, and at a site distal to the guanidino group. In paragraph [0004], Buechler et al. teach that in developing a binding assay for ADMA, the artisan must consider that samples may contain SDMA and/or arginine; thus, immunogenic and label conjugates should be designed to present arginine or its N-methyl derivatives in a manner that permits specific recognition and discrimination of molecules which differ only in the methylation state of the two equivalent nitrogens on the guanidino group. In paragraph [0004], Buechler et al. teach that the analogues are advantageously designed to present an arginine side chain that is free of chemical modifications required for conjugation of the analog to a conjugation target such as a protein, polypeptide, detectable label, solid phase, etc., and are particularly well suited for producing antibodies and labels for use in receptor binding assays for ADMA that can distinguish ADMA from SDMA and arginine itself. In paragraphs [0006] and [0007], Buechler et al. teach ADMA analogues of the formula: PNG media_image6.png 129 283 media_image6.png Greyscale wherein R1 is –H and R2 is a conjugating group having the structure: PNG media_image7.png 42 116 media_image7.png Greyscale Y is an optionally substituted C1-4 alkylene and Z is a moiety providing a thiol or a protected thiol at its terminus. Notably, the conjugating group R2, taught by Buechler et al., wherein Y = CH2 _ CH2 (= C2 alkylene) and Z is thiol (= -SH), reads on the conjugating group of the SDMA analog Compound A of Claim 5. In paragraphs [0018] - [0020], Buechler et al. teach that an ADMA analog comprising an unprotected thiol may be directly linked to an appropriate target protein, polypeptide, label, or other molecule to form a conjugate via any thiol-directed coupling group on the target molecule, and, in case of the preferred coupling groups on target molecules, which are maleimides, that leads to formartion of maleimide-based conjugates. In paragraph [0030], Buechler et al. teach assay methods that utilize an arginine analog(s) conjugated to a solid phase for binding to a labeled antibody. In paragraph [0087], Buechler et al. teach the elected species (a) serum as a sample. In paragraph [0084], Buechler et al. teach different types of devices, including the elected species (b) a test strip as a solid phase, incorporating by reference U.S. Pat. Nos. 5,939,272; 5,922,615; and 5,679,526; in paragraph [0085], Buechler et al. teach a plastic as a solid phase, and in paragraph [0086], Buechler et al. teach an assay device comprising a solid surface comprising one or more of the arginine analogs immobilized thereon, where the one or more arginine analogs correspond to one or more analytes of interest: PNG media_image8.png 502 1164 media_image8.png Greyscale PNG media_image9.png 270 836 media_image9.png Greyscale PNG media_image10.png 156 830 media_image10.png Greyscale PNG media_image11.png 389 1379 media_image11.png Greyscale Emphasis added. It would have been prima facie obvious, at the time the invention was made, for one of ordinary skill in the art to have made and used a modified SDMA comprising a conjugating group having the structure: PNG media_image7.png 42 116 media_image7.png Greyscale wherein Y = CH2 _ CH2 and Z is a thiol, in a device for determining the presence of free symmetrical dimethylarginine (SDMA) in a patient sample. One of ordinary skill in the art would have been motivated to have made and used a modified SDMA comprising a conjugating group having the structure: PNG media_image7.png 42 116 media_image7.png Greyscale wherein Y = CH2 _ CH2 and Z is a thiol in a device for determining the presence of free symmetrical dimethylarginine (SDMA) in a patient sample, because it would be desirable to have a convenient assay device for the quantitative determination of SDMA, which is a useful marker for detecting patients in very early stages of chronic kidney disease and for determining their risk for developing cardiovascular disease, as taught by Bode-Böger et al. One of ordinary skill in the art would have had a reasonable expectation of success in making and using a modified SDMA, comprising a conjugating group having the structure: PNG media_image7.png 42 116 media_image7.png Greyscale wherein Y = CH2 _ CH2 and Z is a thiol, in a device for determining the presence of free symmetrical dimethylarginine (SDMA) in a patient sample, because the use of this type of arginine analogues, which is advantageously designed to present an arginine side chain that is free of chemical modifications required for conjugation of the analog to a detectable label, was known in the devices for detecting free asymmetrical dimethylarginine (ADMA) in a patient sample, as taught by Buechler et al. With regard to the elected species (b) a test strip as a solid phase, the Examiner further notes Applicant’s admission in paragraph [0071] of the application as filed, that the use of reagent-impregnated test strips in specific binding assays is well-known in the art: PNG media_image12.png 300 928 media_image12.png Greyscale PNG media_image13.png 404 922 media_image13.png Greyscale Emphasis added. With regard to the elected species (c) an SDMA analog B, although Buechler et al. do not specifically teach a linker comprising alkylthio group, this type a linker, as evidenced by Valdez, US 2007/0218486, published 09/20/2007 (PTO-892 mailed 03/11/2025), is well-known in the art of preparing hapten conjugates for detecting of small molecule analytes: See, for example, Claim 1: PNG media_image14.png 396 592 media_image14.png Greyscale PNG media_image15.png 176 570 media_image15.png Greyscale PNG media_image16.png 120 572 media_image16.png Greyscale Emphasis added. Claim Objections Claim 1 is objected to because of the following informalities: reciting (-CO(NH-) instead of (-C(O)NH-). Appropriate correction is required. Response to Arguments Applicant's arguments filed 12/23/2025 have been considered but they are not persuasive. Claim Rejections - 35 USC § 112, (pre-AIA ), first paragraph At pages 5-6 of the Remarks, Applicant argues that: PNG media_image17.png 224 1046 media_image17.png Greyscale PNG media_image18.png 370 1068 media_image18.png Greyscale PNG media_image19.png 220 1060 media_image19.png Greyscale Emphasis added. The Examiner respectfully disagrees for the following reasons. First, Applicant misconstrues the Office Action wherein converting a carboxylic acid group of SDMA to an amide bond (-C(O)NH-) was addressed in the context of the broad genus of any possible modifications of the carboxylic acid group of the SDMA. Second, the number of possible variants for attaching symmetrical dimethylarginine (SDMA) to a solid phase through converting the carboxylic acid group of SDMA to an amide bond (-C(O)NH-) is vast, essentially "unlimited" from a practical standpoint, as it depends on the functional groups available on SDMA and the solid phase material, and the virtually infinite combinations of linker molecules that can bridge them. Third, “using the solid phase in immunoassay” argued by Applicant requires ability of the SDMA attached to the solid phase to compete with free SDMA for an antibody. As indicated above, here, there is no evidence on record that any other compound, except for the SDMA cystamide (3), can be used in the claimed device for determining the presence of free symmetrical dimethylarginine (SDMA) in a patient sample. Moreover, as evidenced by Englebienne, “Immune and Receptor Assays in Theory and Practice,” CRC Press, 2000, p. 308 (IDS submitted 04/12/2022), one of ordinary skill in the art would have known that structural modifications are unpredictable because the antibody specificity depends on composition of a linker conjugating SDMA to a solid phase. Claim Rejections - 35 USC § 103(a) At pages 6-9 of the Remarks, Applicant argues that: PNG media_image20.png 80 1034 media_image20.png Greyscale PNG media_image21.png 80 932 media_image21.png Greyscale PNG media_image22.png 156 928 media_image22.png Greyscale PNG media_image23.png 670 1068 media_image23.png Greyscale PNG media_image24.png 220 1070 media_image24.png Greyscale PNG media_image25.png 216 1078 media_image25.png Greyscale PNG media_image26.png 76 912 media_image26.png Greyscale PNG media_image27.png 120 926 media_image27.png Greyscale Emphasis added. The Examiner respectfully disagrees for the following reasons. First, it is noted that “the second Declaration of Dr. Rainer Böger“ filed by Applicant as Exhibit B in the 12/23/2025 Response is identical to the Declaration under 37 CFR § 1.132 of Dr. Rainer Böger dated 12/17/2021 filed by Applicant both as Exhibit A and Exhibit C in the 08/11/2025 Response. Second, contrary to Applicant’s allegation, Bode-Böger et al., do teach that measurement of SDMA can be a marker for detecting patients in very early stages of chronic kidney disease and for determining their risk for developing cardiovascular disease: PNG media_image3.png 452 1314 media_image3.png Greyscale Emphasis added. Third, the alleged “major breakthrough in the area” is not commensurate in scope with the claims because the number of possible variants for attaching symmetrical dimethylarginine (SDMA) to a solid phase through converting the carboxylic acid group of SDMA to an amide bond (-C(O)NH-) is vast, essentially "unlimited" from a practical standpoint, as it depends on the functional groups available on SDMA and the solid phase material, and the virtually infinite combinations of linker molecules that can bridge them. However, using the solid phase in immunoassay requires ability of the SDMA attached to the solid phase to compete with free SDMA for an antibody. Here, there is no evidence on record that any other compound, except for the SDMA cystamide (3), can be used in the claimed device for determining the presence of free symmetrical dimethylarginine (SDMA) in a patient sample. Fourth, the general strategies for the production of compound selective antibodies against small molecules, are well-known in the art since at least 1995. See, for example, Goodrow et al., “Strategies for Immunoassay Hapten Design,” in Immunoanalysis of Agrochemicals; Nelson, J., et al.; ACS Symposium Series, 1995, vol. 586, Chapter 9, pp. 119–139 (IDS submitted 04/12/2022): “Immunoassay performance is a function of the affinity and selectivity of the antibody. The immunizing hapten should represent a near perfect mimic of the target molecule in structure, electronic and hydrophobic properties. These haptens are tethered with an antigenically inert handle distal to the determinant group(s) and do not mask or alter any functional group. Optimal hapten design criteria are based on extending an existing carbon chain, or replacing a C-H moiety of the target molecule with a CH2 chain terminated by a functional group for conjugation to proteins. Careful selection of immunizing hapten can lead to the production of compound or class selective antibodies. A multiple hapten approach, based on handle location, length, and composition, results in assays with sub-ppb levels of detection and improved selectivity. Examination of cross-reactivity data of the haptens led to the identification of the best coating/enzyme-labeled haptens for improved heterologous assays.” Abstract; Emphasis added. Fifth, one of ordinary skill in the art would have been motivated to have made and used a modified SDMA comprising a conjugating group having the structure: PNG media_image7.png 42 116 media_image7.png Greyscale wherein Y = CH2 _ CH2 and Z is a thiol in a device for determining the presence of free symmetrical dimethylarginine (SDMA) in a patient sample, because it would be desirable to have a convenient assay device for the quantitative determination of SDMA, which is a useful marker for detecting patients in very early stages of chronic kidney disease and for determining their risk for developing cardiovascular disease, as taught by Bode-Böger et al. Accordingly, the rejections of the claims are maintained. Conclusion No claims are allowed. Any inquiry concerning this communication or earlier communications from the examiner should be directed to GALINA M YAKOVLEVA whose telephone number is (571)270-3282. The examiner can normally be reached on M-F 8:30 AM-5:00 PM. 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, GREGORY S EMCH can be reached on (571)272-8149. The fax phone number for the organization where this application or proceeding is assigned is 571-273-8300. Information regarding the status of an application may be obtained from the Patent Application Information Retrieval (PAIR) system. Status information for published applications may be obtained from either Private PAIR or Public PAIR. Status information for unpublished applications is available through Private PAIR only. For more information about the PAIR system, see http://pair-direct.uspto.gov. Should you have questions on access to the Private PAIR system, contact the Electronic Business Center (EBC) at 866-217-9197 (toll-free). If you would like assistance from a USPTO Customer Service Representative or access to the automated information system, call 800-786-9199 (IN USA OR CANADA) or 571-272-1000. /GALINA M. YAKOVLEVA/Primary Examiner, Art Unit 1678
Read full office action

Prosecution Timeline

Mar 28, 2022
Application Filed
Mar 06, 2025
Non-Final Rejection — §103, §112
May 27, 2025
Applicant Interview (Telephonic)
May 27, 2025
Examiner Interview Summary
Aug 11, 2025
Response Filed
Sep 20, 2025
Final Rejection — §103, §112
Dec 23, 2025
Request for Continued Examination
Dec 29, 2025
Response after Non-Final Action
Jan 10, 2026
Non-Final Rejection — §103, §112 (current)

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