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and the fee set forth in 37 CFR 1.17(e) has been timely paid, the finality of the previous Office action has been withdrawn pursuant to 37 CFR 1.114.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 12/30/2025 has been entered.
Claims Status
The amendments and remarks filed 12/30/2025 are acknowledged.
Claims 1-8, 10-15, 17-21, and 23-24 are pending.
Claims 9, 16, and 22 are canceled.
Claims 1-4, 14-15, and 17 are amended.
Claims 1-8 and 10-13 remain withdrawn from further consideration pursuant to 37 CFR 1.142(b) as being drawn to a nonelected invention and/or species, there being no allowable generic or linking claims.
Claims 14-15, 17-21, and 23-24 are under examination.
Information Disclosure Statement
The information disclosure statements (IDS) submitted on 12/10/2025, 01/12/2026, and 02/18/2026 are in compliance with the provisions of 37 CFR 1.97, except where noted. Accordingly, the information disclosure statement is being considered by the examiner.
The NPL document lined through on 02/18/2026 IDS has not been considered because the document is not in English.
Notably, the disclosure statement filed lists a Search Report. The listing of the references cited in a Search Report itself is not considered to be an information disclosure statement (IDS) complying with 37 CFR 1.98. 37 CFR 1.98(a)(2) requires a legible copy of: (1) each foreign patent; (2) each publication or that portion which caused it to be listed; (3) for each cited pending U.S. application, the application specification including claims, and any drawing of the application, or that portion of the application which caused it to be listed including any claims directed to that portion, unless the cited pending U.S. application is stored in the Image File Wrapper (IFW) system; and (4) all other information, or that portion which caused it to be listed. In addition, each IDS must include a list of all patents, publications, applications, or other information submitted for consideration by the Office (see 37 CFR 1.98(a)(1) and (b)), and MPEP § 609.04(a), subsection I. states, "the list ... must be submitted on a separate paper." Therefore, the references cited in the Search Report have not been considered. Applicant is advised that the date of submission of any item of information or any missing element(s) will be the date of submission for purposes of determining compliance with the requirements based on the time of filing the IDS, including all "statement" requirements of 37 CFR 1.97(e). See MPEP § 609.05(a).
Note: If copies of the individual references cited on the Search Report are also cited separately on the IDS (and these references have not been lined-through) they have been considered.
Maintained Rejections
Claim Rejections - 35 USC § 103
This rejection has been modified solely to address the amendments.
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.
The factual inquiries for establishing a background for determining obviousness under 35 U.S.C. 103 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 14-15, 17-21 and 23-24 are rejected under 35 U.S.C. 103 as being unpatentable over Fumiyoshi (WO 2011096528; 02/01/2024 PTO-892) in view of Henriques, 2014 (02/01/2024 PTO-892).
Regarding claims 14, 18-21, and 23, Fumiyoshi teaches an anti-CAPRIN-1 monoclonal antibody that has a heavy chain variable region (VH) region that has the amino acid sequence of SEQ ID NO: 43 and that has a light chain variable (VL) region that has an amino acid sequence of SEQ ID NO: 47, wherein the VH region includes a CDR1 with the amino acid sequence of SEQ ID NO: 40, a CDR2 with the amino acid sequence of SEQ ID NO: 41, and a CDR3 with the amino acid sequence of SEQ ID NO: 42, and wherein the VL region includes a CDR1 with the amino acid sequence of SEQ ID NO: 44, a CDR2 with the amino acid sequence of SEQ ID NO: 45, and a CDR3 with the amino acid sequence of SEQ ID NO: 46 [page 8, ninth-tenth paragraphs – page 9, first paragraph]. Further, the antibody against CAPRIN-1 having a heavy chain with SEQ ID NO: 43 and a light chain with SEQ ID NO: 47 is named monoclonal antibody #1 [page 21, second paragraph] and that it can be humanized [page 13, sixth-seventh paragraphs].
SEQ ID NOs: 40-42 of the VH region have 100% sequence identity to SEQ ID NOs: 36-38 of the instant application, respectively, and SEQ ID NOs: 44-46 have 100% sequence identity to SEQ ID NOs: 40-42 of the instant application respectively. Thus, this meets the limitation of claim 19, option (A). Further, SEQ ID NO: 43 of Fumiyoshi has 100% sequence identity to SEQ ID NO: 39 of the instant application and SEQ ID NO: 47 of Fumiyoshi has 100% sequence identity to SEQ ID NO: 43 of the instant application. Thus, this meets the limitation of claim 20, option (a).
Fumiyoshi further teaches that the anti-CAPRIN-1 antibody binds to CAPRIN-1 protein on cancer cells (i.e. a cancer expressing CAPRIN-1 protein) and exhibits an antitumor action, a pharmaceutical composition for the treatment and/or prevention of cancer, comprising the antibody as an active ingredient [page 15, first paragraph], and teaches the use of the antibody, which targets a cancer antigen protein (i.e. CAPRIN-1) which is expressed specifically on the surface of a cancer cell (i.e. cell membrane surface), and the antibody is immunologically reactive with a partial peptide of CAPRIN-1 [see Abstract]. Further, what the antibody binds to is an inherent property of the antibody. Since Fumiyoshi teaches an antibody with 100% sequence identity to that instantly claimed, then the antibody necessarily specifically binds to an extracellular region of the CAPRIN-1 protein since function flows from structure. See MPEP 2112.01(II). Applicant is reminded that chemical compounds and their properties are inseparable (In re Papesch, 315 F.2d 381, 137 USPQ 43 (CCPA1963)), as are their processes and yields (In re Von Schickh, 362 F.2d 821, 150 USPQ 300 (CCPA 1966)). A person of ordinary skill in the art would recognize that these are properties of the anti-CAPRIN-1 antibody.
Fumiyoshi also teaches that breast cancer can be treated or prevented by administering to a subject the pharmaceutical composition [page 16, ninth paragraph] and that a higher therapeutic effect can be obtained by co-administering the antibody of the present invention and an antitumor agent [page 11, first paragraph]. Further, Fumiyoshi teaches that using anti-CAPRIN-antibody #1 confirmed the expression of CAPRIN-1 on breast cancer cell lines [page 27, fifth paragraph], and that antibody #1 had cytotoxic activity against the 10 breast cancer cell lines [page 28, third paragraph] and could damage breast cancer tumor cells expressing CAPRIN-1 by the cytotoxic activity [page 29, second paragraph]. Fumiyoshi also teaches administering antibody #1 to mice transplanted with a human breast cancer cell line and that antibody #1 exhibited antitumor effect in vivo by decreasing the tumor volume [page 30, second-third paragraphs].
However, Fumiyoshi does not teach administering imiquimod at the same time as or separately with the anti-CAPRIN-1 antibody.
Henriques teaches that a patient with invasive ductal carcinoma of the right breast (breast cancer) was administered imiquimod cream 5% to apply three times per week [page e22, right column, second paragraph]. Henriques further teaches that within one week of using the imiquimod cream, there was a decrease in the intensity and thickness of the lesion, and the surface area was stable (Fig 2) and the following week, there was a decrease in surface area and a further reduction in intensity and thickness (Fig 3), with no reported adverse effects [page e22, right column, second paragraph]. Henriques also teaches that three weeks after the start of imiquimod, the patient reported her pain intensity had lessened from a score of 8 of 10 to 6 of 10 [page e22, right column, second paragraph]. Henriques further teaches that the patient then stopped applying imiquimod for approximately 2 to 3 weeks, and the lesions quickly began to progress [page e23, left column, first paragraph]. Henriques also teaches that restarting imiquimod again led to regression (treatment of cancer), and during the next 4 months, the skin lesions and pain continued to improve with the use of topical imiquimod (Fig 4) [page e23, left column, first paragraph]. Henriques further teaches that imiquimod topical cream can be an effective treatment for cutaneous metastasis from breast cancer and possibly other cancers [page e23, left column, second paragraph – right column, first paragraph].
It would have been obvious to someone of ordinary skill in the art before the effective filing date of the claimed invention to have combined the anti-CAPRIN-1 antibody, as taught by Fumiyoshi, and the imiquimod, as taught by Henriques, for the treatment of breast cancer. One would have been motivated to combine these two treatments for the treatment of breast cancer because both references individually demonstrate effective treatment of breast cancer. Moreover, the instant situation is amenable to the type of analysis set forth in In re Kerkhoven, 205 USPQ 1069 (CCPA 1980) wherein the court held that it is prima facie obvious to combine two compositions each of which is taught by the prior art to be useful for the very same purpose. The idea of combining them flows logically from having been individually taught in the prior art. Applying the same logic to the instant claims, one of ordinary skill in the art would have been imbued with at least a reasonable expectation of success that by administering the anti-CAPRIN-1 antibody, as taught by Fumiyoshi, in combination with the imiquimod, as taught by Henriques, one would achieve a method for treating breast cancer.
Claim 15 is included in this rejection because Fumiyoshi teaches that the CAPIN-1 antibodies (i.e. antibody that specifically binds to the CAPRIN-1 protein) of the invention have antitumor activity against a polypeptide having an even sequence number among SEQ ID NOs: 2-30 [page 3, second paragraph], which CAPRIN proteins are represented by the even sequence number among SEQ ID NOs: 2 to 30 [page 15, sixth paragraph].
SEQ ID NO: 2 of Fumiyoshi has 100% sequence identity to SEQ ID NO: 2 of the instant application. SEQ ID NO: 4 of Fumiyoshi has 100% sequence identity to SEQ ID NO: 4 of the instant application.
Further, what the antibody specifically binds to is an inherent property of the antibody. Applicant is reminded that chemical compounds and their properties are inseparable (In re Papesch, 315 F.2d 381, 137 USPQ 43 (CCPA1963)), as are their processes and yields (In re Von Schickh, 362 F.2d 821, 150 USPQ 300 (CCPA 1966)). A person of ordinary skill in the art would recognize that these are properties of the anti-CAPRIN-1 antibody.
Claim 17 is included in this rejection because Fumiyoshi teaches that SEQ ID NO: 37 is a partial sequence of CAPRIN-1 that is recognized by the monoclonal antibody #1 of the invention.
SEQ ID NO: 37 of Fumiyoshi has 100% sequence identity to SEQ ID NO: 31 of the instant application.
Further, what the antibody specifically binds to is an inherent property of the antibody. Applicant is reminded that chemical compounds and their properties are inseparable (In re Papesch, 315 F.2d 381, 137 USPQ 43 (CCPA1963)), as are their processes and yields (In re Von Schickh, 362 F.2d 821, 150 USPQ 300 (CCPA 1966)). A person of ordinary skill in the art would recognize that these are properties of the anti-CAPRIN-1 antibody.
Claim 24 is included in this rejection because Henriques teaches that the patient was administered imiquimod 5% cream to apply [page e22, right column, second paragraph]. The instant specification defines percutaneously-administered agents (formulations) as agents called liniments and external medicines and that the external medicines include solid agents, solutions, sprays, ointments, creams, and gels [see paragraph 0117 of the specification]. Thus, the imiquimod 5% cream meets the limitation of a percutaneously administered formulation (agent).
Double Patenting
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.
Claims 14-15, 17-21 and 23-24 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-6, and 11-14 of U.S. Patent No. 12,274,745 (‘745) and further in view of Henriques, 2014 (02/01/2024 PTO-892).
Regarding claims 14 and 15 of the instant application, claim 1 of ‘745 teaches a conjugate of an antibody or a fragment thereof linked to an immune activator, wherein the antibody or the fragment thereof has immunological reactivity with a CAPRIN-1 protein of any of even-numbered SEQ ID NOs among SEQ ID NO: 2 to 30, and wherein the immune activator is an imidazoquinoline compound which is a TLR7- or TLR8-binding ligand or agonist, and wherein the antibody or the fragment thereof is linked to the immune activator via a linker, claim 11 of ‘745 teaches a method for treating a cancer expressing a CAPRIN-1 protein on the cell membrane surface, comprising administering an effective amount of the conjugate according to claim 1 or a pharmaceutical composition comprising the conjugate as an active ingredient to a subject, claim 8 of ‘745 teaches a pharmaceutical composition comprising the conjugate according to claim 1 as an active ingredient and a pharmaceutically acceptable carrier, and claim 9 of ‘745 teaches the pharmaceutical composition according to claim 8, wherein the cancer is a cancer expressing a CAPRIN-1 protein on the cell membrane surface. Further, claim 6 of ‘745 teaches the conjugate according to claim 1, wherein the antibody or the fragment thereof is any of the following (A) to (M) and claim 7 of ‘745 teaches the conjugate according to claim 1, wherein the antibody or the fragment thereof is any of the following (a) to (al). Since ‘745 teaches an antibody that has immunological reactivity with CAPRIN-1 with 100% sequence identity to those instantly claimed (see rejections of instant claims 19 and 20 below), then the antibody necessarily specifically binds to an extracellular region of the CAPRIN-1 protein since function flows from structure. See MPEP 2112.01(II). Applicant is reminded that chemical compounds and their properties are inseparable (In re Papesch, 315 F.2d 381, 137 USPQ 43 (CCPA1963)), as are their processes and yields (In re Von Schickh, 362 F.2d 821, 150 USPQ 300 (CCPA 1966)). A person of ordinary skill in the art would recognize that these are properties of the anti-CAPRIN-1 antibody.
SEQ ID NO: 2 of the reference application has 100% sequence identity to SEQ ID NO: 2 of the instant application. Additionally, Imiquimod is an imidazoquinoline compound.
However, ‘745 does not teach administering imiquimod together or separately in combination with the anti-CAPRIN-1 antibody.
Henriques teaches that a patient with invasive ductal carcinoma of the right breast (breast cancer) was administered imiquimod cream 5% to apply three times per week [page e22, right column, second paragraph]. Henriques further teaches that within one week of using the imiquimod cream, there was a decrease in the intensity and thickness of the lesion, and the surface area was stable (Fig 2) and the following week, there was a decrease in surface area and a further reduction in intensity and thickness (Fig 3), with no reported adverse effects [page e22, right column, second paragraph].
The instant specification defines percutaneously-administered agents (formulations) as agents called liniments and external medicines and that the external medicines include solid agents, solutions, sprays, ointments, creams, and gels [see paragraph 0117 of the specification]. Thus, the imiquimod 5% cream meets the limitation of a percutaneously administered formulation (agent).
It would have been obvious to someone of ordinary skill in the art before the effective filing date of the claimed invention to have combined the anti-CAPRIN-1 antibody, as taught by ‘745, and the imiquimod, as taught by Henriques, for the treatment and/or prevention of breast cancer. One would have been motivated to combine these two treatments for the treatment of breast cancer because both references individually demonstrate effective treatment of breast cancer. Moreover, the instant situation is amenable to the type of analysis set forth in In re Kerkhoven, 205 USPQ 1069 (CCPA 1980) wherein the court held that it is prima facie obvious to combine two compositions each of which is taught by the prior art to be useful for the very same purpose. The idea of combining them flows logically from having been individually taught in the prior art. Applying the same logic to the instant claims, one of ordinary skill in the art would have been imbued with at least a reasonable expectation of success that by administering the anti-CAPRIN-1 antibody, as taught by ‘745, in combination with the imiquimod, as taught by Henriques, one would achieve a method for treating breast cancer.
Claim 17 is included in this rejection because claim 3 of ‘745 teaches the conjugate according to claim 1, wherein the antibody or the fragment thereof has immunological reactivity (i.e. specifically binds) with a partial polypeptide of the CAPRIN-1 protein, wherein the partial polypeptide consists of any of SEQ ID NO: 31 to 35 and 296 to 299, 308, and 309.
SEQ ID NO: 31 of the reference application has 100% sequence identity to SEQ ID NO: 31 of the instant application.
Claim 18 is included in this rejection because claim 5 of ‘745 teaches the conjugate according to claim 1, wherein the antibody is a monoclonal antibody or a polyclonal antibody.
Claim 19 is included in this rejection because the claim 6 of ‘745 teaches the conjugate according to claim 1, wherein the antibody or the fragment thereof is any of the following (A) to (M): and (A) is an antibody or fragment thereof, which comprises a heavy chain variable region comprising complementarity-determining regions of SEQ ID NO: 36, 37, and 38 (CDR1, CDR2, and CDR3, respectively) and a light chain variable region comprising complementarity-determining regions of SEQ ID NO: 40, 41, and 42 (CDR1, CDR2, and CDR3, respectively) and has immunological reactivity with the CAPRIN-1 protein.
SEQ ID NO: 36 of the reference application has 100% sequence identity to SEQ ID NO: 36 of the instant application, SEQ ID NO: 37 of the reference application has 100% sequence identity to SEQ ID NO: 37 of the instant application, SEQ ID NO: 38 of the reference application has 100% sequence identity to SEQ ID NO: 38 of the instant application, SEQ ID NO: 40 of the reference application has 100% sequence identity to SEQ ID NO: 40 of the instant application, SEQ ID NO: 41 of the reference application has 100% sequence identity to SEQ ID NO: 41 of the instant application, and SEQ ID NO: 42 of the reference application has 100% sequence identity to SEQ ID NO: 42 of the instant application.
Claim 20 is included in this rejection because claim 7 of ‘745 teaches the conjugate according to claim 1, wherein the antibody or the fragment thereof is any of the following (a) to (al) and (a) is an antibody or fragment thereof, comprising a heavy chain variable region comprising the amino acid sequence of SEQ ID NO: 39 and a light chain variable region comprising the amino acid sequence of SEQ ID NO: 43.
SEQ ID NO: 39 of the reference application has 100% sequence identity to SEQ ID NO: 39 of the instant application and SEQ ID NO: 43 of the reference application has 100% sequence identity to SEQ ID NO: 43 of the instant application.
Claim 21 is included in this rejection because claim 5 of ‘745 teaches the conjugate according to claim 1, wherein the antibody is a humanized antibody or a chimeric antibody.
Claim 23 is included in this rejection because claim 10 of ‘745 teaches the pharmaceutical composition according to claim 8, wherein the cancer is breast cancer, kidney cancer, pancreatic cancer, colorectal cancer, lung cancer, brain tumor, stomach cancer, uterine cancer, ovary cancer, prostate cancer, bladder cancer, esophagus cancer, leukemia, lymphoma, liver cancer, gallbladder cancer, sarcoma, mastocytoma, melanoma, adrenal cortex cancer, Ewing's tumor, Hodgkin's lymphoma, mesothelioma, multiple myeloma, testicle cancer, thyroid cancer, or head and neck cancer.
Claim 24 is included in this rejection because Henriques teaches that the patient was administered imiquimod 5% cream to apply [page e22, right column, second paragraph]. The instant specification defines percutaneously-administered agents (formulations) as agents called liniments and external medicines and that the external medicines include solid agents, solutions, sprays, ointments, creams, and gels [see paragraph 0117 of the specification]. Thus, the imiquimod 5% cream meets the limitation of a percutaneously administered formulation (agent).
Claims 14-15, and 17-21 and 23-24 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-6 and 10-13 of U.S. Patent No. 9,115,200 (‘200) in view of Fumiyoshi (WO 2011096528; 02/01/2024 PTO-892) and Henriques, 2014 (02/01/2024 PTO-892).
Regarding claims 14-15, 18-20, and 23 of the instant application, Claim 1 of ‘200 teaches a pharmaceutical composition for treating or inhibiting the recurrence of a cancer, comprising a monoclonal antibody or an antigen binding fragment thereof as an active ingredient that has immunological reactivity with a polypeptide consisting of the amino acid sequence SEQ ID NO: 69 or 70 contained in the amino acid sequence SEQ ID NO: 37 or a polypeptide consisting of an amino acid sequence having 80% or more sequence identity with the amino acid sequence of SEQ ID NO: 69 OR 70, and wherein the monoclonal antibody or antigen binding fragment thereof has immunological reactivity with one or more CAPRIN-1 sequences selected from the group of CAPRIN-1 sequences consisting of: SEQ ID NOS: 2, 4, 6, 8, 10, 12, 14, 16, 18, 20, 22, 24, 26, 28, and 30, claim 2 of ‘200 teaches the pharmaceutical composition according to claim 1, wherein the cancer is breast cancer, brain cancer, leukemia, lymphoma, lung cancer, renal cancer, uterine cervix cancer, bladder cancer, esophageal cancer, gastric cancer, or colorectal cancer, claim 4 of ‘200 teaches an isolated monoclonal antibody having immunological reactivity with a polypeptide, wherein the polypeptide consists of the amino acid sequence SEQ ID NO: 69 or 70 contained in the amino acid sequence SEQ ID NO: 37 or consists of an amino acid sequence having 80% or more sequence identity with the amino acid sequence of SEQ ID NO: 69 or 70, and wherein the isolated monoclonal antibody has immunological reactivity with one or more CAPRIN-1 sequences selected from the group of CAPRIN-1 sequences consisting of: SEQ ID NOS: 2, 4, 6, 8, 10, 12, 14, 16, 18, 20, 22, 24, 26, 28, and 30.
SEQ ID NO: 2 of ‘200 has 100% sequence identity to SEQ ID NO: 2 of the instant application.
Claim 5 of ‘200 teaches the isolated monoclonal antibody according to claim 4,
which has a cytotoxic activity (immunological reactivity) against a cancer cell expressing a CAPRIN-1 protein. Claim 6 of ‘200 teaches an isolated monoclonal antibody, which comprises a heavy chain variable region comprising SEQ ID NOS: 40, 41, and 42 and a light chain variable region comprising SEQ ID NOS: 44, 45, and 46, and has immunological reactivity with a CAPRIN-1 protein, claim 11 of ‘200 teaches a pharmaceutical combination for treating and/or inhibiting the recurrence of a cancer, comprising the pharmaceutical composition of claim 1, and a pharmaceutical composition containing an antitumor agent, claim 12 of ‘200 teaches a method for treating and/or inhibiting the recurrence of a cancer in a subject, comprising administering to the subject the monoclonal antibody of claim 4 or an antigen binding fragment thereof or the pharmaceutical composition of claim 1, and claim 13 of ‘200 teaches a method for treating and/or inhibiting the recurrence of a cancer in a subject, comprising administering to the subject the pharmaceutical combination of claim 11.
SEQ ID NO: 40 of ‘200 has 100% sequence identity to SEQ ID NO: 36 of the instant application, SEQ ID NO: 41 of ‘200 has 100% sequence identity to SEQ ID NO: 37 of the instant application, SEQ ID NO: 42 of ‘200 has 100% sequence identity to SEQ ID NO: 38 of the instant application, SEQ ID NO: 44 of ‘200 has 100% sequence identity to SEQ ID NO: 40 of the instant application, SEQ ID NO: 45 of ‘200 has 100% sequence identity to SEQ ID NO: 41 of the instant application, and SEQ ID NO: 46 of ‘200 has 100% sequence identity to SEQ ID NO: 42 of the instant application.
‘200 teaches an anti-CAPRIN-1 antibody that has the same CDRs as the antibody claimed in the instant application and therefore, the antibody of ‘200 necessarily specifically binds to an extracellular region of the CAPRIN-1 protein since function flows from structure. See MPEP 2112.01(II).
However, ‘200 does not specifically teach that this antibody is used to treat cancer, specifically breast cancer, or combining imiquimod with the antibody.
Fumiyoshi teaches an anti-CAPRIN-1 monoclonal antibody that has a heavy chain variable region (VH) region that has the amino acid sequence of SEQ ID NO: 43 and that has a light chain variable (VL) region that has an amino acid sequence of SEQ ID NO: 47, wherein the VH region includes a CDR1 with the amino acid sequence of SEQ ID NO: 40, a CDR2 with the amino acid sequence of SEQ ID NO: 41, and a CDR3 with the amino acid sequence of SEQ ID NO: 42, and wherein the VL region includes a CDR1 with the amino acid sequence of SEQ ID NO: 44, a CDR2 with the amino acid sequence of SEQ ID NO: 45, and a CDR3 with the amino acid sequence of SEQ ID NO: 46 [page 8, ninth-tenth paragraphs – page 9, first paragraph]. Further, the antibody against CAPRIN-1 having a heavy chain with SEQ ID NO: 43 and a light chain with SEQ ID NO: 47 is named monoclonal antibody #1 [page 21, second paragraph] and that it can be humanized [page 13, sixth-seventh paragraphs].
SEQ ID NOs: 40-42 of the VH region have 100% sequence identity to SEQ ID NOs: 36-38 of the instant application, respectively, and SEQ ID NOs: 44-46 have 100% sequence identity to SEQ ID NOs: 40-42 of the instant application respectively. Thus, this meets the limitation of claim 19, option (A). Further, SEQ ID NO: 43 of Fumiyoshi has 100% sequence identity to SEQ ID NO: 39 of the instant application and SEQ ID NO: 47 of Fumiyoshi has 100% sequence identity to SEQ ID NO: 43 of the instant application. Thus, this meets the limitation of claim 20, option (a).
Fumiyoshi further teaches that the anti-CAPRIN-1 antibody binds to CAPRIN-1 protein on cancer cells and exhibits an antitumor action, a pharmaceutical composition for the treatment and/or prevention of cancer, comprising the antibody as an active ingredient [page 15, first paragraph], and teaches the use of an antibody, which targets a cancer antigen protein (CAPRIN-1) which is expressed specifically on the surface of a cancer cell (i.e. cell membrane surface), and the antibody is immunologically reactive with a partial peptide of CAPRIN-1 [see Abstract]. Fumiyoshi also teaches that breast cancer can be treated or prevented by administering to a subject the pharmaceutical composition [page 16, ninth paragraph] and that a higher therapeutic effect can be obtained by co-administering the antibody of the present invention and an antitumor agent [page 11, first paragraph]. Further, Fumiyoshi teaches that using anti-CAPRIN- antibody #1 confirmed the expression of CAPRIN-1 on breast cancer cell lines [page 27, fifth paragraph], and that antibody #1 had cytotoxic activity against the 10 breast cancer cell lines [page 28, third paragraph] and could damage breast cancer tumor cells expressing CAPRIN-1 by the cytotoxic activity [page 29, second paragraph]. Fumiyoshi also teaches administering antibody #1 to mice transplanted with a human breast cancer cell line and that antibody #1 exhibited antitumor effect in vivo by decreasing the tumor volume [page 30, second-third paragraphs].
Henriques teaches that a patient with invasive ductal carcinoma of the right breast (breast cancer) was administered imiquimod cream 5% to apply three times per week [page e22, right column, second paragraph]. Henriques further teaches that within one week of using the imiquimod cream, there was a decrease in the intensity and thickness of the lesion, and the surface area was stable (Fig 2) and the following week, there was a decrease in surface area and a further reduction in intensity and thickness (Fig 3), with no reported adverse effects [page e22, right column, second paragraph]. Henriques also teaches that three weeks after the start of imiquimod, the patient reported her pain intensity had lessened from a score of 8 of 10 to 6 of 10 [page e22, right column, second paragraph]. Henriques further teaches that the patient then stopped applying imiquimod for approximately 2 to 3 weeks, and the lesions quickly began to progress [page e23, left column, first paragraph]. Henriques also teaches that restarting imiquimod again led to regression (treatment of cancer), and during the next 4 months, the skin lesions and pain continued to improve with the use of topical imiquimod (Fig 4) [page e23, left column, first paragraph]. Henriques further teaches that imiquimod topical cream can be an effective treatment for cutaneous metastasis from breast cancer and possibly other cancers [page e23, left column, second paragraph – right column, first paragraph].
The antibody of ‘200 is the same antibody taught in Fumiyoshi, therefore, it would have been obvious to someone of ordinary skill in the art before the effective filing date of the claimed invention to have combined the anti-CAPRIN-1 antibody, as taught by ‘200 and Fumiyoshi, and the imiquimod, as taught by Henriques, for the treatment and/or prevention of breast cancer. One would have been motivated to combine these two treatments for the treatment of breast cancer because Fumiyoshi and Henriques each individually demonstrate effective treatment of breast cancer. Moreover, the instant situation is amenable to the type of analysis set forth in In re Kerkhoven, 205 USPQ 1069 (CCPA 1980) wherein the court held that it is prima facie obvious to combine two compositions each of which is taught by the prior art to be useful for the very same purpose. The idea of combining them flows logically from having been individually taught in the prior art. Applying the same logic to the instant claims, one of ordinary skill in the art would have been imbued with at least a reasonable expectation of success that by administering the anti-CAPRIN-1 antibody, as taught by ‘200 and Fumiyoshi, in combination with the imiquimod, as taught by Henriques, one would achieve a method for treating breast cancer.
Further, regarding the limitation of “comprising administering an antibody or a fragment thereof having an immunological reactivity with a cytoplasmic-activation and proliferation associated protein 1 (CAPRIN-1) protein present on a surface of a cancer cell,” Fumiyoshi teaches that the antibodies of the invention identify a cancer antigen protein which is expressed specifically on the surface (extracellular) of a cancer cell [see Abstract]. The antibody’s immunological reactivity is an inherent property of the antibody. Applicant is reminded that chemical compounds and their properties are inseparable (In re Papesch, 315 F.2d 381, 137 USPQ 43 (CCPA1963)), as are their processes and yields (In re Von Schickh, 362 F.2d 821, 150 USPQ 300 (CCPA 1966)). A person of ordinary skill in the art would recognize that these are properties of the anti-CAPRIN-1 antibody.
Claim 17 is included in this rejection because Fumiyoshi teaches that SEQ ID NO: 37 is a partial sequence of CAPRIN-1 that is recognized by the monoclonal antibody #1 of the invention.
SEQ ID NO: 37 of Fumiyoshi has 100% sequence identity to SEQ ID NO: 31 of the instant application.
Further, the antibody’s immunological reactivity is an inherent property of the antibody. Applicant is reminded that chemical compounds and their properties are inseparable (In re Papesch, 315 F.2d 381, 137 USPQ 43 (CCPA1963)), as are their processes and yields (In re Von Schickh, 362 F.2d 821, 150 USPQ 300 (CCPA 1966)). A person of ordinary skill in the art would recognize that these are properties of the anti-CAPRIN-1 antibody.
Claim 21 is included in this rejection because claim 3 of ‘200 teaches the pharmaceutical composition according to claim 1, wherein the antibody is a human antibody, humanized antibody, chimeric antibody, single chain antibody, or bispecific antibody, and claim 10 of ‘200 teaches the isolated monoclonal antibody according to claim 4, which is a human antibody, humanized antibody, chimeric antibody, single chain antibody, or bispecific antibody.
Claim 24 is included in this rejection because Henriques teaches that the patient was administered imiquimod 5% cream to apply [page e22, right column, second paragraph]. The instant specification defines percutaneously-administered agents (formulations) as agents called liniments and external medicines and that the external medicines include solid agents, solutions, sprays, ointments, creams, and gels [see paragraph 0117 of the specification]. Thus, the imiquimod 5% cream meets the limitation of a percutaneously administered formulation (agent).
Claims 14-15, 17-21 and 23-24 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-3, 6-7, and 9 of U.S. Patent No. 9,180,187 (‘187) in view of Fumiyoshi (WO 2011096528; 02/01/2024 PTO-892) and Henriques, 2014 (02/01/2024 PTO-892).
Regarding claims 14-15, 18-20, and 23 of the instant specification, claim 1 of ‘187 teaches a method for treating and/or preventing recurrence of a CAPRIN-1 expressing cancer, comprising: administering a medicament to a subject suspected of having a cancer, wherein the medicament comprises a combination of an antibody or a fragment thereof having immunological reactivity with a CAPRIN-1 protein, and one or two or more types of antitumor agents, wherein the antibody or fragment and the antitumor agent or antitumor agents are combined together or separately, wherein the antibody or fragment and the antitumor agent are not conjugated together, wherein the cancer expresses the CAPRIN-1 protein on the cell surface of the cancer and the antibody or fragment binds specifically to the extracellular region of a CAPRIN-1 protein existing on the surface of a cancer cell (i.e. cell membrane surface), claim 2 of ‘187 teaches the method according to claim 1, wherein the antibody or a fragment thereof having immunological reactivity with a CAPRIN-1 protein is an antibody or a fragment thereof which binds specifically to a polypeptide consisting of the amino acid sequence of SEQ ID NO: 37 in the extracellular region of the CAPRIN-1 protein existing on the surface of a cancer cell, claim 3 of ‘187 teaches the method according to claim 1, wherein the CAPRIN-1 protein is from a human, claim 6 of ‘187 teaches the method according to claim 1, wherein the antibody is selected from the group consisting of single chain antibodies (scFv), Fab, F(ab1)2, and Fv, claim 9 of ‘187 teaches a method for treating and/or preventing recurrence of a CAPRIN-1 expressing cancer, comprising administering a medicament to a subject suspected of having a cancer, wherein the medicament comprises a combination of an antibody or a fragment thereof having immunological reactivity with a CAPRIN-1 protein, and one or two or more types of antitumor agents, wherein the antibody or fragment and the antitumor agent or antitumor agents are combined together or separately, wherein the antibody or fragment and the antitumor agent are not conjugated together, wherein the cancer expresses the CAPRIN-1 protein on the cell surface of the cancer, and wherein the antibody or a fragment thereof having immunological reactivity with a CAPRIN-1 protein is an antibody or a fragment thereof which binds specifically to a polypeptide consisting of the amino acid sequence of SEQ ID NO: 37 in the extracellular region of the CAPRIN-1 protein existing on the surface of a cancer cell.
SEQ ID NO: 37 of ‘187 has 100% sequence identity to partial sequences of the even numbered SEQ ID NOs: 2 to 30.
However, ‘187 does not specifically teach that this antibody is used to treat cancer, specifically breast cancer, or combining imiquimod with the antibody.
Fumiyoshi teaches an anti-CAPRIN-1 monoclonal antibody that has a heavy chain variable region (VH) region that has the amino acid sequence of SEQ ID NO: 43 and that has a light chain variable (VL) region that has an amino acid sequence of SEQ ID NO: 47, wherein the VH region includes a CDR1 with the amino acid sequence of SEQ ID NO: 40, a CDR2 with the amino acid sequence of SEQ ID NO: 41, and a CDR3 with the amino acid sequence of SEQ ID NO: 42, and wherein the VL region includes a CDR1 with the amino acid sequence of SEQ ID NO: 44, a CDR2 with the amino acid sequence of SEQ ID NO: 45, and a CDR3 with the amino acid sequence of SEQ ID NO: 46 [page 8, ninth-tenth paragraphs – page 9, first paragraph]. Further, the antibody against CAPRIN-1 having a heavy chain with SEQ ID NO: 43 and a light chain with SEQ ID NO: 47 is named monoclonal antibody #1 [page 21, second paragraph] and that it can be humanized [page 13, sixth-seventh paragraphs].
SEQ ID NOs: 40-42 of the VH region have 100% sequence identity to SEQ ID NOs: 36-38 of the instant application, respectively, and SEQ ID NOs: 44-46 have 100% sequence identity to SEQ ID NOs: 40-42 of the instant application respectively. Thus, this meets the limitation of claim 19, option (A). Further, SEQ ID NO: 43 of Fumiyoshi has 100% sequence identity to SEQ ID NO: 39 of the instant application and SEQ ID NO: 47 of Fumiyoshi has 100% sequence identity to SEQ ID NO: 43 of the instant application. Thus, this meets the limitation of claim 20, option (a).
Fumiyoshi further teaches that the anti-CAPRIN-1 antibody binds to CAPRIN-1 protein on cancer cells and exhibits an antitumor action, a pharmaceutical composition for the treatment and/or prevention of cancer, comprising the antibody as an active ingredient [page 15, first paragraph], and teaches the use of an antibody, which targets a cancer antigen protein (CAPRIN-1) which is expressed specifically on the surface of a cancer cell, and the antibody is immunologically reactive with a partial peptide of CAPRIN-1 [see Abstract]. Fumiyoshi also teaches that breast cancer can be treated or prevented by administering to a subject the pharmaceutical composition [page 16, ninth paragraph] and that a higher therapeutic effect can be obtained by co-administering the antibody of the present invention and an antitumor agent [page 11, first paragraph]. Further, Fumiyoshi teaches that using anti-CAPRIN- antibody #1 confirmed the expression of CAPRIN-1 on breast cancer cell lines [page 27, fifth paragraph], and that antibody #1 had cytotoxic activity against the 10 breast cancer cell lines [page 28, third paragraph] and could damage breast cancer tumor cells expressing CAPRIN-1 by the cytotoxic activity [page 29, second paragraph]. Fumiyoshi also teaches administering antibody #1 to mice transplanted with a human breast cancer cell line and that antibody #1 exhibited antitumor effect in vivo by decreasing the tumor volume [page 30, second-third paragraphs].
Henriques teaches that a patient with invasive ductal carcinoma of the right breast (breast cancer) was administered imiquimod cream 5% to apply three times per week [page e22, right column, second paragraph]. Henriques further teaches that within one week of using the imiquimod cream, there was a decrease in the intensity and thickness of the lesion, and the surface area was stable (Fig 2) and the following week, there was a decrease in surface area and a further reduction in intensity and thickness (Fig 3), with no reported adverse effects [page e22, right column, second paragraph]. Henriques also teaches that three weeks after the start of imiquimod, the patient reported her pain intensity had lessened from a score of 8 of 10 to 6 of 10 [page e22, right column, second paragraph]. Henriques further teaches that the patient then stopped applying imiquimod for approximately 2 to 3 weeks, and the lesions quickly began to progress [page e23, left column, first paragraph]. Henriques also teaches that restarting imiquimod again led to regression (treatment of cancer), and during the next 4 months, the skin lesions and pain continued to improve with the use of topical imiquimod (Fig 4) [page e23, left column, first paragraph]. Henriques further teaches that imiquimod topical cream can be an effective treatment for cutaneous metastasis from breast cancer and possibly other cancers [page e23, left column, second paragraph – right column, first paragraph].
It would have been obvious to someone of ordinary skill in the art before the effective filing date of the claimed invention to have combined the anti-CAPRIN-1 antibody, as taught by ‘187 and Fumiyoshi, and the imiquimod, as taught by Henriques, for the treatment and/or prevention of breast cancer. One would have been specifically motivated to choose the antibody of Fumiyoshi for the method of treating cancer of ‘187 because Fumiyoshi teaches that the antibody was an effective treatment for breast cancer. Further, one would have been motivated to combine these two treatments for the treatment of breast cancer because Fumiyoshi and Henriques each individually demonstrate effective treatment of breast cancer. Moreover, the instant situation is amenable to the type of analysis set forth in In re Kerkhoven, 205 USPQ 1069 (CCPA 1980) wherein the court held that it is prima facie obvious to combine two compositions each of which is taught by the prior art to be useful for the very same purpose. The idea of combining them flows logically from having been individually taught in the prior art. Applying the same logic to the instant claims, one of ordinary skill in the art would have been imbued with at least a reasonable expectation of success that by administering the anti-CAPRIN-1 antibody, as taught by ‘187 and Fumiyoshi, in combination with the imiquimod, as taught by Henriques, one would achieve a method for treating breast cancer.
Claim 17 is included in this rejection because Fumiyoshi teaches that SEQ ID NO: 37 is a partial sequence of CAPRIN-1 that is recognized by the monoclonal antibody #1 of the invention.
SEQ ID NO: 37 of Fumiyoshi has 100% sequence identity to SEQ ID NO: 31 of the instant application.
Further, the antibody’s immunological reactivity is an inherent property of the antibody. Applicant is reminded that chemical compounds and their properties are inseparable (In re Papesch, 315 F.2d 381, 137 USPQ 43 (CCPA1963)), as are their processes and yields (In re Von Schickh, 362 F.2d 821, 150 USPQ 300 (CCPA 1966)). A person of ordinary skill in the art would recognize that these are properties of the anti-CAPRIN-1 antibody.
Claim 21 is included in this rejection because claim 7 of ‘187 teaches the method according to claim 1, wherein the antibody is a human antibody, humanized antibody, chimeric antibody, single chain antibody, or bispecific antibody.
Claim 24 is included in this rejection because Henriques teaches that the patient was administered imiquimod 5% cream to apply [page e22, right column, second paragraph]. The instant specification defines percutaneously-administered agents (formulations) as agents called liniments and external medicines and that the external medicines include solid agents, solutions, sprays, ointments, creams, and gels [see paragraph 0117 of the specification]. Thus, the imiquimod 5% cream meets the limitation of a percutaneously administered formulation (agent).
Response to Arguments
The rejections of claims 14-15, 17-21 and 23-24 under 35 U.S.C. 103 over Fumiyoshi in view of Henriques are maintained. On page 19 of the remarks, Applicant cites U.S. Case Law, specifically Graham v. John Deere Co., arguing that the Graham factors weigh in Applicant’s favor, arguing that a proper rational has not been used to reject the claims. This is not found persuasive because the Examiner has set forth a clear reason as to why it would have been obvious, with a reasonable expectation of success, to have combined the teachings of Fumiyoshi and Henriques, relying on the applicable case law of In re Kerkhoven, to arrive at the claimed invention. Applicant further argues that the claims have been amended to make the scope of the claims consistent with the scope in which the significant therapeutic effects are observed. This is not found persuasive because Applicant has not amended the claims to be consistent with the scope in which the alleged significant therapeutic effects are observed. Applicant has only amended the claims to recite that the cancer expresses CAPRIN-1 protein on the cell membrane surface and that the antibody or fragment thereof specifically binds to an extracellular region of the CAPRIN-1 protein. To reiterate what was stated in the Office Actions mailed 09/04/2024 and 04/01/2025 regarding the alleged significant therapeutic effects of the instantly claimed method, the results of Example 3 are potentially persuasive suggesting that the humanized antibody #1 combined with imiquimod are unexpectedly better than the humanized antibody #1 combined with other cancer treatments, but that these results are not commensurate in scope with the instant claims because the instant claims are directed to the broad genus of any antibody or fragment thereof that has immunological reactivity with CAPRIN-1 protein (i.e. binds to an extracellular region of the CAPRIN-1 protein), not to the specific humanized antibody #1 that is used in Example 3.
On page 20 of the remarks, Applicant notes the reference of Campione. To reiterate what was stated in the Office Action mailed 06/28/2024, the citation of the Campione reference is not representative of any alleged unexpected results of the claimed invention. Campione is directed to the combination of rituximab, an anti-CD20 antibody, and imiquimod, whereas the instant application is directed to the combination of an anti-CAPRIN-1 antibody and imiquimod. Applicant further argues that humanized antibody #1 showed a significant synergy effect with imiquimod (see Example 2), and polyclonal antibody #1 also showed a significant antitumor effect when combined with imiquimod (see Example 3). Applicant additionally argues that it is general technical knowledge that a polyclonal antibody is a population of numerous types of monoclonal antibodies, and that from these examples, the skilled artisan would understand that the effect of the present invention is shown not only in the case the humanized antibody #1 is used, but also in the case any antibody capable of binding to CAPRIN-1 protein is used. To reiterate what was stated in the Office Action mailed 10/30/2025, this is not found persuasive because the results of Examples 2 and 3 cannot be relied upon to demonstrate unexpected results for any CAPRIN-1 antibody or fragment thereof in combination with imiquimod because while the broadly defined antibodies or fragments thereof may all bind to CAPRIN-1, different CAPRIN-1 antibodies, monoclonal or polyclonal, will bind to different parts of the protein, have different binding affinities, and thus, have different interactions. Therefore, one of skill in the art would not expect all CAPRIN-1 antibodies to function in the same ways. The results of Examples 2 and 3 of the instant application that Applicant relies upon to demonstrate the alleged unexpected results is not commensurate in scope with the instant claims. See MPEP 716.02(d). Applicant reiterates the argument that while a high antitumor effect was observed when polyclonal antibody #1, which is "an antibody which specifically binds to an extracellular region of a CAPRIN-1 protein," was used in combination with imiquimod, it is highly likely that a similar level of effect will be achieved when a monoclonal antibody, which is also "an antibody which specifically binds to an extracellular region of a CAPRIN-1 protein," is used in combination with imiquimod. This argument has been addressed above and the response to the argument is incorporated herein and will not be reiterated.
The double patenting rejections of claims 14-15, 17-21 and 23-24 over U.S. Patent No. 12,274,745 in view of Henriques, U.S. Patent No. 9,115,200 in view of Fumiyoshi and Henriques, and U.S. Patent No. 9,180,187 in view of Fumiyoshi and Henriques are maintained. On page 21 of the remarks, Applicant does not present any arguments to these rejections and requests that these rejections be held in abeyance. A request to hold a rejection in abeyance is not a proper response to a rejection. Rather, a request to hold a matter in abeyance may only be made in response to an OBJECTION or REQUIREMENTS AS TO FORM (see 37 CFR 1.111(b) and MPEP §714.02). Thus, the double patenting rejections of record have been maintained as no response to these rejections has been filled by applicant at this time.
Conclusion
No claims are allowed.
All claims are identical to or patentably indistinct from, or have unity of invention with claims in the application prior to the entry of the submission under 37 CFR 1.114 (that is, restriction (including a lack of unity of invention) would not be proper) and all claims could have been finally rejected on the grounds and art of record in the next Office action if they had been entered in the application prior to entry under 37 CFR 1.114. Accordingly, THIS ACTION IS MADE FINAL even though it is a first action after the filing of a request for continued examination and the submission under 37 CFR 1.114. See MPEP § 706.07(b). Applicant is reminded of the extension of time policy as set forth in 37 CFR 1.136(a).
A shortened statutory period for reply to this final action is set to expire THREE MONTHS from the mailing date of this action. In the event a first reply is filed within TWO MONTHS of the mailing date of this final action and the advisory action is not mailed until after the end of the THREE-MONTH shortened statutory period, then the shortened statutory period will expire on the date the advisory action is mailed, and any nonprovisional extension fee (37 CFR 1.17(a)) pursuant to 37 CFR 1.136(a) will be calculated from the mailing date of the advisory action. In no event, however, will the statutory period for reply expire later than SIX MONTHS from the mailing date of this final action.
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/B.E.D./Examiner, Art Unit 1675
/JEFFREY STUCKER/Supervisory Patent Examiner, Art Unit 1675
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