DETAILED ACTION
1. The present application, filed on or after March 16, 2013, is being examined under the first inventor to file provisions of the AIA .
2 Applicant's amendment, filed on 02/17/2026, is acknowledged.
3. Claims 1-3, 5, 8-13, 18-22 are pending.
4. Upon reconsideration, the Examiner extended the search to cover a composition further comprising a therapeutic agent and all the antibody species recited in claims 10-11.
4. Applicant’s election without traverse of Group I, claims 1-3, 5, 8-13, 18-22 directed to an antibody, or antigen-binding fragment thereof, specifically binding to Gremlin-1 (SEQ ID NO: 33), wherein the binding to Gremlin-1 reduces Gremin-1 activity with an EC50 50 nM, and the VH comprising the CDR1-3 of SEQ I DNO: 35-37 and VL comprising the CDR1-3 or SEQ ID NO: 38-40 and the VH and VL of SEQ ID NO: 17-18, filed on 02/17/2026, is acknowledged.
5. Claims 1-3, 5, 8-13 and 18-22 are under examination as they read on to an antibody, or antigen-binding fragment thereof, specifically binding to Gremlin-1 (SEQ ID NO: 33), wherein the binding to Gremlin-1 reduces Gremin-1 activity with an EC50 50 nM.
6. Applicant’s IDS, filed 05/03/2024 and 02/17/2026, is acknowledged.
7. Amended Claim 10 is objected to because SEQ ID NO: 39 (LAWYQQKPGNAPRLLIS) is the Framework 2 and not VL-CDR2, while the correct VL-CDR2 for clone 14-D10-2 is SEQ ID NO: 93 (GAT). Correction is required.
8. The following is a quotation of 35 U.S.C. 112(a) (Pre-AIA 35 U.S.C. 112, first paragraph):
(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.
9. Claims 1-3, 5, 8-9 and 18-22 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.
Claims-1-3, 8-9 and 18-22 encompass a broad genus of anti-Gremlin-1 antibodies that reduce Gremlin-1 activity with an EC50 50nM, inhibit Gremlin-1 to BMP2, BMP4 and/or BMP7.
However, there does not appear to be an adequate written description in the specification as-filed of the essential structural feature that provides the recited function of reducing Gremlin-1 activity with EC50 50nM and inhibiting Gremlin-1 to BMP2, BMP4 and/or BMP7. The Guidelines for the Examination of Patent Applications Under the 35 U.S.C. 112, ¶ 1 "Written Description" Requirement make clear that the written description requirement for a claimed genus may be satisfied through sufficient description of a representative number of species by actual reduction to practice, reduction to drawings, 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 genus.
The specification discloses that antibodies that bind to Gremlin-1 are known in the art. Such antibodies have been described as being suitable for use in the treatment of certain diseases such as cancer (WO 2019/243801) or bone fractures or defects (WO 2019/158658). [0004].
The specification discloses that biological responses induced by BMP signaling are regulated through specific antagonists, i.e. the DAN-family proteins Gremlin-1 and Gremlin-2. Gremlin-1 is a 184 amino acid glycoprotein that binds with high affinity BMP2, BMP4 and BMP7 and regulates BMP activity during development, controlling limb and kidney formation [0009].
Example 1 of the specification discloses the generation and production of anti-Gremlin-1 antibodies. [0555] C57BL/6 mice were immunized with 10 μg huGREM1 (HuGREM1, 120-42, PeproTech) conjugated with KLH (#77666, Thermofisher) and emulsified in Complete Freund's Adjuvant (CFA) on days 0, 15 and day 70 (subcutaneously) and on day 90 (intravenously). On day 97, splenocytes were obtained and fused with P3x63Ag8.653 myeloma cells.
[0557] Monoclonal α-GREM1 clones with an OD 492 nm>0.9 in a binding ELISA were selected for sequencing of their BCR. Antibodies chosen for BCR sequencing are: 3-A1-3, 7H12-1, 8-H2-2, 12-G9-12, 14-D10-2, 14-E6-3, 14-G2-4, 17-C2-3, and 20-D1-5.
Example 2 shows that anti-Gremlin-1 antibodies 14-D10-2 and 20-D1-5 bind to linearized epitopes of huGREM1.
Example 3 shows that clone 14-D10-2 demonstrated increased functional affinity (avidity) to huGREM1 compared to clone 20-D1-5 [0563].
Example 5 shows binding of anti-Gemlin-1 antibodies 14-D10-2 and 20-D1-5 to human and murine Gremlin-1. [0576] Rag1−/- mice treated with 200 μg of 20-D1-5 and 14-D10-2 before the cell transfer of cardiac myosin-specific autoreactive CD4+ T cells showed significantly reduced overall inflammation as determined by infiltration of CD45+ cells into the cardiac tissue (20-D1-5 p=0.008, 14-D10-2 p=0.004).
Example 8 shows nti-Gremlin-1 Antibodies 3-A1-3 and 14-D10-2 Neutralize Gremlin-2-Mediated BMP4 Inhibition.
It is noted that human Gremlin-1 is 184 amino acids in length. It is well known in the art that the epitope binding site of an antibody is usually defined by no more than six to eight amino acids. Neither the instant specification nor the art of record shows that the majority of antibodies that bind to any one of the multitude of epitopes present in a protein having the sequence of Gremlin-1 reduce Gremlin-1 activity with an EC50 50 nM and and capable of inhibiting inhibit Gremlin-1 bindign to BMP2, BMP4 and/BMP7, as is required for the operability of the claimed product. The required genus is not adequately described because neither the specification nor the art of record describes a representative number of species of antibody within the required genus.
Artisans are well aware that knowledge of a given antigen (for instance Gremlin-1) provides no information concerning the sequence/structure of antibodies that bind the given antigen. For example, Edwards et al (J Mol Biol. 2003 Nov 14;334(1): 103-18) teach that over 1,000 different antibodies to a single protein can be generated, all with different sequences spanning almost the entire heavy and light chain germline repertoire (42/49 functional heavy chain germlines and 33 of 70 V-lambda and V-kappa light chain germlines, and with extensive diversity in the FICDR3 region sequences (that are generated by VDJ germline segment recombination) as well, see entire document). Similarly, Lloyd et al (Protein Eng Des Sel. 2009 Mar;22(3):159-68) teach that a large majority of VH/VL germline gene segments are used in the antibody response to an antigen, even when the antibodies were selected by antigen binding, as their sequencing studies revealed that out of 841 unselected and 5,044 selected antibodies, all but one of the 49 functional VH gene segments was observed (see entire document). Goel et al (J Immunol. 2004 Dec 15; 173(12):7358-67) disclose the synthesis of three mAbs that bind to the same short (12-mer) peptide and found that the sequences of these antibodies which bound the same epitope exhibited diverse V gene usage indicating their independent germline origin (see entire document). As such, it does not seem possible to predict the sequence/structure of an antibody that binds a given antigen as there does not appear to be any common or core structure present within all antibodies that gives rise to the function of antigen binding. Further, given data such as that of Edwards et al. indicating the diversity of sequence bound in a population of antibodies that bind to a given antigen no number of species appears to reasonably representative of the breadth of the genus of antibodies that bind the given antigen. Indeed, Kanyavuz et al (Nat Rev Immunol. 2019 Jun; 19(6):355-368) teach that “Theoretically, under physiological conditions, the human immune system can generate BCRs with 1026 distinct sequences, an astronomical number that is far greater than the calculated number of all B cell clones that can be generated during the lifespan of a healthy human (estimated to be 4 x 1014).
Importantly, the USPTO has released a Memo on the Clarification of Written Description Guidance For Claims Drawn to Antibodies and Status of 2008 Training Materials, 02/22/2018.
See https://www.uspto.gov/sites/default/files/documents/amgen_22feb2018.pdf.
The Memo clarifies the applicability of USPTO guidance regarding the written description requirement of 35 U.S.C. § 112(a) concerning the written description requirement for claims drawn to antibodies, including the following.
“In view of the Amgen decision, adequate written description of a newly characterized antigen alone should not be considered adequate written description of a claimed antibody to that newly characterized antigen, even when preparation of such an antibody is routine and conventional”.
In contrast to applicant’s reliance of describe the epitope of the Gremlin-1 or epitope of SEQ ID NO: 33, 96-97 in providing a fully characterized antigen / specific epitope as well as claiming structural elements of the antigen, one or more functions recited in the claims and binding affinity, there is insufficient written description of the required kind of structure-identifying information about the corresponding makeup of the claimed anti-Gremlin-1 / SEQ ID NO: 33 antibodies to demonstrate possession. Also, see Amgen Inc. v. Sanofi, 124 USPQ2d 1354 (Fed. Cir. 2017).
There is no evidence that knowledge of the chemical structure of an antigen gives the required kind of structure identifying information about the corresponding antibodies Applicants attempt to describe the invention by describing something that is not the invention: viz., the antigens to which the antibodies may bind. There nothing in the disclosure that describes the antibodies as required by the test set forth in Ariad.
However, the anti-Gremlin-1 / SEQ ID NO: 33/96/97 antibodies are required to practice the invention. The specification fails to provide any specific structural or physical information so as to define a genus of antibodies having the desired therapeutic properties. Applicant is merely relying on the identification of Gremlin-1 / SEQ ID NO: 33 as the antigen and the well-known structure of antibodies in general. However, the claims do not recite a general antibody, but an antibody having a specific desired activity. However, Federal Circuit clarification of the law of written description as it applies to antibodies. Amgen v. Sanofi, 872 F.3d 1367 (Fed. Cir. 2017).
The claims are directed to a genus of anti-Gremlin-1 / SEQ ID NO: 33/96/97 antibodies. However, Federal Circuit clarification of the law of written description as it applies to antibodies. The U.S. Court of Appeals for the Federal Circuit (Federal Circuit) decided Amgen v. Sanofi, 872 F.3d 1367 (Fed. Cir. 2017), which concerned adequate written description for claims drawn to antibodies. The Federal Circuit explained in Amgen that when an antibody is claimed, 35 U.S.C. § 112(a) requires adequate written description of the antibody itself. Amgen, 872 F.3d at 1378-79. The Amgen court expressly stated that the so-called "newly characterized antigen" test, which had been based on an example in USPTO-issued training materials and was noted in dicta in several earlier Federal Circuit decisions, should not be used in determining whether there is adequate written description under 35 U.S.C. § 112(a) for a claim drawn to an antibody. Citing its decision in Ariad Pharmaceuticals, Inc. v. Eli Lilly & Co., the court also stressed that the "newly characterized antigen" test could not stand because it contradicted the quid pro quo of the patent system whereby one must describe an invention in order to obtain a patent. Amgen, 872 F.3d at 1378-79, quoting Ariad Pharmaceuticals, Inc. v. Eli Lilly & Co., 598 F.3d 1336, 1345 (Fed. Cir. 2010). In view of the Amgen decision, adequate written description of a newly characterized antigen alone should not be considered adequate written description of a claimed antibody to that newly characterized antigen, even when preparation of such an antibody is routine and conventional.
Moreover, there is insufficient written description of the required kind of structure-identifying information about the corresponding makeup of the claimed anti- Gremlin-1 / SEQ ID NO: 33/96/97 antibodies to demonstrate possession. Also, see Amgen Inc. v. Sanofi, Aventisub LLC, No. 2017-1480 (Fed. Cir. 2017). The Court reiterated that adequate written description must “contain enough information about the actual makeup of the claimed products . . . .” The Court simultaneously suggested that the “newly characterized antigen” test “flouts” section 112 because it “allows patentees to claim antibodies by describing something that is not the invention, i.e. the antigen.” The Court concluded that for written description of an antibody to be adequate when presented with “functional” terminology, there must be an established correlation in the art between structure and function.
Possession is not be shown by merely describing how to obtain possession of members of the claimed genus or how to identify their common structural features. See University of Rochester, 358 F.3d at 927, 69 USPQ2d at 1895. Sufficient description to show possession of such a genus may be achieved by means of a recitation of anti-Gremlin-1 / SEQ ID NO: 33/96/97 antibodies falling within the scope of the genus or of a recitation of structural features common to members of the genus, which features constitute a substantial portion of the genus. See Eli Lilly, 119F.3d at 1568, 43 USPQ2d at 1406.
Vas-Cath Inc. v. Mahurkar, 19 USPQ2d 1111, makes clear that “applicant must convey with reasonable clarity to those skilled in the art that, as of the filing date sought, he or she was in possession of the invention. The invention is, for purposes of the written description inquiry, whatever is now claimed.” (See page 1117.) The specification does not “clearly allow persons of ordinary skill in the art to recognize that [he or she] invented what is claimed.” (See Vas-Cath at page 1116.). Consequently, Applicant was not in possession of the instant claimed invention. See University of California v. Eli Lilly and Co. 43 USPQ2d 1398.
Applicant is invited to point to clear support or specific examples of the claimed invention in the specification as-filed.
10. The following is a quotation of the appropriate paragraphs of 35 U.S.C. 102 that form the basis for the rejections under this section made in this Office action:
A person shall be entitled to a patent unless –
(a)(1) the claimed invention was patented, described in a printed publication, or in public use, on sale or otherwise available to the public before the effective filing date of the claimed invention.
(a)(2) the claimed invention was described in a patent issued under section 151, or in an application for patent published or deemed published under section 122(b), in which the patent or application, as the case may be, names another inventor and was effectively filed before the effective filing date of the claimed invention.
11. Claims 1-3, 5, 8-9 and 18-22 are rejected under 35 U.S.C. 102(a)(1)/(2) as being anticipated by US 10947304 B2.
The `304 patent teaches and claims a monoclonal anti-Gremlin-1 antibody comprising a HCDR1/HCDR2/HCDR3/LCDR1/LCDR2/LCDR3 sequence combination of SEQ ID NOs: 4/5/6/7/8/9 or SEQ ID NOs: 3/5/6/7/8/9. wherein said antibody is a Fab, modified Fab, Fab′, modified Fab′, F(ab′)2, Fv, single domain antibody or an scFv, wherein said antibody comprises SEQ ID NOs: 10 and 11, wherein said antibody comprises SEQ ID NOs: 12 and 13.
A pharmaceutical composition comprising the monoclonal antibody and a pharmaceutically acceptable adjuvant and/or carrier (see issued claims 1-12). The `304 patent teaches that Gremlin 1 was able to inhibit the BMP 4/7 signaling in the Hek-Id1 reporter gene assay (col., 27, lines 1-2). Example 4 teaches the production of anti-Gremlin-1 antibodies. Anti-Gremlin-1 antibodies were derived by immunization and library panning. 25 human and mouse cross-reactive antibodies from the library were panned using recombinant human Gremlin. 10 antibodies were selected for scale up and purified as scFvs for testing in the screening assays. Binding affinity of anti-Gremlin-1 antibody Ab7326 taken as the average KD value for 5 determinations, was found to be below 100 pM.
The `304 patent teaches:
SEQ ID NO: 14 shows the mouse Ab 7326 full length IgG1 heavy chain (variant 1).
SEQ ID NO: 15 shows the mouse Ab 7326 full length IgG1 light chain (variant 1).
SEQ ID NO: 16 shows the human Ab 7326 full length IgG1 heavy chain (variant 2).
SEQ ID NO: 17 shows the human Ab 7326 full length IgG1 light chain (variant 2) (see col. 5, lines 20+).
Claim 3 is included because the `304 patent provides an antibody which binds to an epitope on Gremlin-1 comprising at least one residue selected from Trp93, Phe117, Tyr119, Phe125, Tyr126 and Phe138, wherein the residue numbering is according to SEQ ID NO: 1 (col. 7, lines 16+). SEQ ID NO: 96 is EEGCNSRTIINRFCYGQ and SEQ ID NO: 97 is EEGCRSRTILNRFCYGQ which correspond to F117 and Y119 in Gremlin-1.
Since the office does not have a laboratory to test the reference antibodies, it is applicant’s burden to show that the reference antibody does not reduce Gremlin-1 activity with an EC50 50 nM. See In re Best, 195 USPQ 430, 433 (CCPA 1977); In re Marosi, 218 USPQ 289, 292-293 (Fed. Cir. 1983); and In re Fitzgerald et al., 205 USPQ 594 (CCPA 1980).
The reference teachings anticipate the claimed invention.
12. Claims 1-2, 5, 8-9 and 18-22 are rejected under 35 U.S.C. 102(a)(1) as being anticipated by US 20160024195 A1.
The `195 publication teaches an isolated human monoclonal antibody or antigen-binding fragment thereof that binds specifically to human gremlin-1 (GREM1), wherein the antibody or antigen-binding fragment thereof blocks GREM1 binding to one of bone morphogenetic protein—2 (BMP2), BMP4, BMP7 or heparin. An isolated human antibody or antigen-binding fragment thereof that binds specifically to GREM1, wherein the antibody or antigen-binding fragment thereof exhibits one or more properties selected from the group consisting of: (a) binds GREM1 at 37° C. with a binding dissociation equilibrium constant (KD) of less than about 275 nM as measured by surface plasmon resonance; (b) binds to GREM1 at 37° C. with a dissociative half-life (t½) of greater than about 3 minutes as measured by surface plasmon resonance; (c) binds GREM1 at 25° C. with a KD of less than about 280 nM as measured by surface plasmon resonance; (d) binds to GREM1 at 25° C. with a t % of greater than about 2 minutes as measured by surface plasmon resonance; (e) blocks GREM1 binding to BMP4 with an IC50 of less than about 1.9 nM as measured in a competition ELISA assay at 25° C.; (f) blocks GREM1-mediated inhibition of BMP signaling and promotes cell differentiation; and (g) blocks GREM1 binding to heparin. Composition comprising an isolated human antibody or antigen-binding fragment thereof that binds to GREM1, and a pharmaceutically acceptable carrier or diluent. The `195 publication teaches the use of the anti-GREM1 antibody is administered to the patient in combination with a second therapeutic agent, wherein the second therapeutic agent is selected from the group consisting of another antibody to GREM1, a VEGF antagonist, a cytotoxic agent, a chemotherapeutic agent, radiation, surgery, an anti-inflammatory drug, a corticosteroid, a nutritional supplement, and any other palliative therapy, wherein the VEGF antagonist is an anti-VEGF antibody or a VEGF-inhibiting fusion protein, wherein the VEGF antagonist is aflibercept. The `195 publication teaches that the anti-GREM1 antibodies can be derived from IgG1, IgG4 [0121].
Since the office does not have a laboratory to test the reference antibodies, it is applicant’s burden to show that the reference antibody does not reduce Gremlin-1 activity with an EC50 50 nM. See In re Best, 195 USPQ 430, 433 (CCPA 1977); In re Marosi, 218 USPQ 289, 292-293 (Fed. Cir. 1983); and In re Fitzgerald et al., 205 USPQ 594 (CCPA 1980).
The reference teachings anticipate the claimed invention.
13. The nonstatutory double patenting rejection is based on a judicially created doctrine grounded in public policy (a policy reflected in the statute) so as to prevent the unjustified or improper timewise extension of the “right to exclude” granted by a patent and to prevent possible harassment by multiple assignees. A nonstatutory double patenting rejection is appropriate where the conflicting claims are not identical, but at least one examined application claim is not patentably distinct from the reference claim(s) because the examined application claim is either anticipated by, or would have been obvious over, the reference claim(s). See, e.g., In re Berg, 140 F.3d 1428, 46 USPQ2d 1226 (Fed. Cir. 1998); In re Goodman, 11 F.3d 1046, 29 USPQ2d 2010 (Fed. Cir. 1993); In re Longi, 759 F.2d 887, 225 USPQ 645 (Fed. Cir. 1985); In re Van Ornum, 686 F.2d 937, 214 USPQ 761 (CCPA 1982); In re Vogel, 422 F.2d 438, 164 USPQ 619 (CCPA 1970); In re Thorington, 418 F.2d 528, 163 USPQ 644 (CCPA 1969).
A timely filed terminal disclaimer in compliance with 37 CFR 1.321(c) or 1.321(d) may be used to overcome an actual or provisional rejection based on nonstatutory double patenting provided the reference application or patent either is shown to be commonly owned with the examined application, or claims an invention made as a result of activities undertaken within the scope of a joint research agreement. See MPEP § 717.02 for applications subject to examination under the first inventor to file provisions of the AIA as explained in MPEP § 2159. See MPEP § 2146 et seq. for applications not subject to examination under the first inventor to file provisions of the AIA . A terminal disclaimer must be signed in compliance with 37 CFR 1.321(b).
The filing of a terminal disclaimer by itself is not a complete reply to a nonstatutory double patenting (NSDP) rejection. A complete reply requires that the terminal disclaimer be accompanied by a reply requesting reconsideration of the prior Office action. Even where the NSDP rejection is provisional the reply must be complete. See MPEP § 804, subsection I.B.1. For a reply to a non-final Office action, see 37 CFR 1.111(a). For a reply to final Office action, see 37 CFR 1.113(c). A request for reconsideration while not provided for in 37 CFR 1.113(c) may be filed after final for consideration. See MPEP §§ 706.07(e) and 714.13.
The USPTO Internet website contains terminal disclaimer forms which may be used. Please visit www.uspto.gov/patent/patents-forms. The actual filing date of the application in which the form is filed determines what form (e.g., PTO/SB/25, PTO/SB/26, PTO/AIA /25, or PTO/AIA /26) should be used. A web-based eTerminal Disclaimer may be filled out completely online using web-screens. An eTerminal Disclaimer that meets all requirements is auto-processed and approved immediately upon submission. For more information about eTerminal Disclaimers, refer to www.uspto.gov/patents/apply/applying-online/eterminal-disclaimer.
14. Claims 1-3, 5, 8-13 and 18-22 are provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-14, 18-19, and 22-26 of copending Application No. 18857007 (reference application). Although the claims at issue are not identical, they are not patentably distinct from each other because the claims of `007 application is directed an antibody, or an antigen-binding fragment thereof, pan-specifically binding to Gremlin-1 and Gremlin-2, antibody 14-D10-2 that binds to epitope 105-121aa (i.e., claimed SEQ ID NO: 96).
Alignment of claimed SEQ ID NOS: 35-37 with referenced SEQ ID NO: 11, 31
Qy 1 GYSFTGYY-----------------FFPYNGFS--------------------------- 16
|||||||| ||||||||
Db 26 GYSFTGYYMHWVKQSHGNILDWIGYFFPYNGFSNCNQKFKGKATLTVDKSSSTAYMELRS 85
Qy 17 -----------ARGGLGRGYFDV 28
||||||||||||
Db 86 LTSEDSAVYYCARGGLGRGYFDV 108
Alignment of claimed SEQ ID NOS: 38-40 with referenced SEQ ID NO: 33
Qy 1 DHINNWLAWYQQKPGNAPRLLIS------------------------------------- 23
|||||||||||||||||||||||
Db 27 DHINNWLAWYQQKPGNAPRLLISGATSLETGVPSRFSGSGSGKDYTLSITSLQTEDVATY 86
Qy 24 --QQYWSSPRT 32
|||||||||
Db 87 YCQQYWSSPRT 97
Alignment of claimed SEQ ID NOS: 38-93-40 with referenced SEQ ID NO: 16-18, 33,
Qy 1 DHINNW-----------------GAT---------------------------------- 9
|||||| |||
Db 27 DHINNWLAWYQQKPGKAPRLLISGATSLETGVPSRFSGSGSGTDYTLTISSLQPEDVATY 86
Qy 10 --QQYWSSPRT 18
|||||||||
Db 87 YCQQYWSSPRT 97
The specification of the `007 application teaches the antibody composition comprising at least one further therapeutic agent, wherein the further therapeutic agent is an anti-inflammatory agent, an immunomodulator, an antibiotic, an angiotensin-converting-enzyme inhibitor, a P-blocker and a diuretic, infliximab, adalimumab, certolizumab pegol, golimumab, etanercept, curcumin, IL- 1 RA, rilonacept, canakinumab, allopurinol, colchicine, prednisone, pentoxifylline (see pages 6-7). The claims of the `007 application anticipate the instant claims.
This is a provisional nonstatutory double patenting rejection because the patentably indistinct claims have not in fact been patented.
16. No claim is allowable.
17. Claims 10-13 would be allowable if rewritten to overcome the rejection under NS-ODP and objection, set forth in this Office action and to include all of the limitations of the base claim and any intervening claims.
18. Any inquiry concerning this communication or earlier communications from the examiner should be directed to MAHER M HADDAD whose telephone number is (571)272-0845. The examiner can normally be reached on Monday-Friday from7:00AM to 4:30PM. If attempts to reach the examiner by telephone are unsuccessful, the examiner’s supervisor, Misook Yu, can be reached at telephone number 571-272-0839. The fax phone number for the organization where this application or proceeding is assigned is 571-273-8300.
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March 9, 2026 /MAHER M HADDAD/ Primary Examiner, Art Unit 1644