DETAILED ACTION
Notice of Pre-AIA or AIA Status
The present application, filed on or after March 16, 2013, is being examined under the first inventor to file provisions of the AIA .
Priority
This application is a 371 of PCT/KR2021/010001, filed on 07/30/2021, claiming priority to foreign application KR 10-2020-0095988, filed on 07/31/2020.
Claims Status
Acknowledgement is made of the receipt and entry of the amendment to the claims filed on October 14, 2025. Claims 1-5, 7-8 are canceled. Claims 6 and 9-11 are pending and under examination.
Action Summary
Claims 7 and 8 rejected under 35 U.S.C. 101 because the claimed recitation of a use, without setting forth any steps involved in the process, are withdrawn in light of the cancelation of claims 7 and 8.
Claims 7 and 8 rejected under 35 U.S.C. 112(b) or 35 U.S.C. 112 (pre-AIA ), second paragraph, are withdrawn in light of the cancelation of claims 7 and 8.
Claims 1-5, 7, and 8 rejected on the basis that it contains an improper Markush grouping of alternatives, are withdrawn in light of the claim amendment.
Claims 1-5 and 7- 8 rejected under 35 U.S.C. 102 (a)(1) as being anticipated by Sim et al (US2019/0047993 A1), are withdrawn in light of the claim amendment.
Claim 6 rejected under 35 U.S.C. 102 (a)(1) as being anticipated by Sim et al (US2019/0047993 A1) in view of Piris-Villaespesa et al (Front Pharmacol. 2020 Apr 14; 11:443), are withdrawn in light of the claim amendment.
Claims 1-5 and 7-8 rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1 and 5 of U.S. Patent No. US10,442,796 B2, are withdrawn in light of the claim amendment canceling claims 1-5 and 7-8.
Claim 6 rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1 and 5 of U.S. Patent No. US10,442,796 B2, is withdrawn in light of the claim amendment.
Claims 1-5 and 7-8 provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-3 and 5-6 of copending Application No. 18/006,582 (reference application), are withdrawn in light of the claim amendment canceling claims 1-5 and 7-8.
Claim 6 provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-3 and 5-6 of copending Application No. 18/006,582 (reference application), is withdrawn in light of the claim amendment.
New Rejection necessitated by claim amendment
Claim Rejections - 35 USC § 103
In the event the determination of the status of the application as subject to AIA 35 U.S.C. 102 and 103 (or as subject to pre-AIA 35 U.S.C. 102 and 103) is incorrect, any correction of the statutory basis (i.e., changing from AIA to pre-AIA ) for the rejection will not be considered a new ground of rejection if the prior art relied upon, and the rationale supporting the rejection, would be the same under either status.
The following is a quotation of 35 U.S.C. 103 which forms the basis for all obviousness rejections set forth in this Office action:
A patent for a claimed invention may not be obtained, notwithstanding that the claimed invention is not identically disclosed as set forth in section 102, if the differences between the claimed invention and the prior art are such that the claimed invention as a whole would have been obvious before the effective filing date of the claimed invention to a person having ordinary skill in the art to which the claimed invention pertains. Patentability shall not be negated by the manner in which the invention was made.
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 6 and 9-11 are rejected under 35 U.S.C. 103 as being unpatentable over Sim et al (US2019/0047993 A1) in view of Piris-Villaespesa et al (Front Pharmacol. 2020 Apr 14; 11:443) Martelli et al (Int. J. Mol. Sci. June 1 2020, 21(11), 3987), and Crew et al (US2006/0063773 A1).
Sim teaches a teach a method for the treatment, prevention, and alleviation of acute myeloid leukemia, the method comprising administering a pharmaceutical composition comprising as an active ingredient, a 2,3,5-substituted thiophene compound, preferably (S)-5-((3-fluorophenyl) ethynyl)-N-(piperidin-3-yl)-3-ureidothiophene-2-carboxamide
PNG
media_image1.png
470
781
media_image1.png
Greyscale
. (See claims 1, 9, 10, and paragraph [0299].)
This compound corresponds to compound of Example 22. Moreover, Sim teaches the 2,3,5-substituted thiophene compound is excellent in ability to inhibit activity of Kit among other proteins. (See paragraph [0023].)
Sim does not teach systematic mastocytosis wherein the systematic mastocytosis is caused by substitution of valine or histidine for aspartic acid at amino acid position 816 of c-kit protein. Moreover, Sim does not teach systematic mastocytosis wherein the systematic mastocytosis is caused by substitution of valine for glycine at amino acid position 560 of c-kit protein.
Piris-Villaespesa teaches systemic mastocytosis is a rare and heterogeneous disease characterized by mast cell proliferation and activation. KIT is a transmembrane tyrosine kinase which plays a key role in mast cell growth, differentiation and survival. After interaction with its ligand, the stem cell factor, KIT dimerizes activating downstream pathways involving multiple tyrosine kinases (PI3K, JAK/STAT, RAS/ERK). Activating mutations in KIT are detected in most cases of systemic mastocytosis, being the most common KIT D816V. Therefore, since the emergence of tyrosine kinase inhibitors, KIT inhibition has been an attractive approach when facing mastocytosis treatment. (See Abstract.) Moreover, Piris-Villaespesa teaches the most frequent KIT mutation found in SM (systemic mastocytosis) is the D816V KIT mutation, which consists of the replacement of aspartic acid by valine in position 816 of the protein receptor. (See last paragraph of the left column of page 443.)
Martelli teaches in recent years, molecular characterization and management of patients with systemic mastocytosis (SM) have greatly benefited from the application of advanced technologies. Highly sensitive and accurate assays for KIT D816V mutation detection and quantification have allowed the switch to non-invasive peripheral blood testing for patient screening; allele burden has prognostic implications and may be used to monitor therapeutic efficacy. (See Abstract.) Moreover, Martelli teaches Activating mutations of KIT play a crucial role in the pathogenesis of systemic mastocytosis (SM) by enabling the proliferation and survival of abnormal mast cells (MCs) in affected tissues. The first identification of gain-of-function mutations occurred in the HMC-1 human MCL cell line, which was found to harbor a constitutively activated KIT receptor. Sequencing of KIT cDNA revealed two heterozygous point mutations resulting in a valine to glycine amino acid substitution at codon 560 (V560G) and in an aspartate to valine substitution at codon 816 (D816V). Kitayama et al. expressed the murine equivalents of D816V and V560G mutations in Ba/F3 cell lines, finding that they lead to growth factor-independent proliferation in vitro and tumorigenicity when injected into nude mice. (See last paragraph of page 3.)
Crew teaches a compound represented by the formula (I)
PNG
media_image2.png
728
468
media_image2.png
Greyscale
having cKIT activity for treating tumors or cancers such as mastocytosis/mast cell leukemia among others. (See Abstract, claim 1, and paragraph [0079].)
It would have been prima facie obvious to one of ordinary skill in the art at the time the invention was filed to modify the method of Sim by including systemic mastocytosis that is caused by substitution of valine or histidine for aspartic acid at amino acid position 816 of c-kit protein and systemic mastocytosis that is caused by substitution of valine for glycine at amino acid position 560 of c-kit protein to give Applicant’s claimed invention. One would have been motivated to do so, because Piris-Villaespesa teaches Kit is activated or detected in most cases of systemic mastocytosis and inhibiting of Kit has been an attractive approach when facing mastocytosis treatment and because Piris-Villaespesa teaches the most frequent KIT mutation found in SM is the D816V KIT mutation, which consists of the replacement of aspartic acid by valine in position 816 of the protein receptor, and also because Martelli teaches Sequencing of KIT cDNA revealed two heterozygous point mutations resulting in a valine to glycine amino acid substitution at codon 560 (V560G) and in an aspartate to valine substitution at codon 816 (D816V) in systemic mastocytosis and lastly because di-substituted thiophene compounds similar in core structure as the instant compound as having cKit inhibitory activity for treating mastocytosis as taught by Crew. One would reasonably expect the method of Sim to be effective for treating systemic mastocytosis that systemic mastocytosis that is caused by substitution of valine or histidine for aspartic acid at amino acid position 816 of c-kit protein and that is caused by substitution of valine for glycine at amino acid position 560 of c-kit protein in addition to acute myeloid leukemia with success by inhibiting the activity of Kit among other proteins.
Acknowledgement is made of the receipt and entry of Applicant’s remarks/arguments filed on October 14, 2025.
Applicant’s argument
Applicant argues that although the compound of Example 22 is shown in Sim to be useful for AML, there is no teaching or suggestion in Sim for the use of this compound for mastocytosis. Moreover, the amendments to the claims recite specific mutations at specific positions of c-kit. There is no teaching or suggestion from the combination of Sim and Piris-Villaespesa that the compound of Example 22 of Sim has inhibitory activity with respect to the specific mutations at specific positions of c-kit recited in claims 6 and 9. Also, Piris-Villaespesa (abstract), notes that "[i]nitial reports showed that only the rare KIT D816V negative cases were responsive to tyrosine kinase inhibitors." Accordingly, contrary to the Examiner's assertions, one skilled in the art would not be motivated to try kinase inhibitors to treat mastocytosis caused by D816V. Furthermore, there would be no reasonable expectation of success for one of ordinary skill in the art to apply the compound of Example 22 of Sim to mastocytosis caused by specific mutations at specific positions of c-kit.
Examiner’s response
In response, Applicant’s argument is not persuasive. It may well be true that the combination of Sim and Piris-Villaespesa that the compound of Example 22 of Sim has inhibitory activity with respect to the specific mutations at specific positions of c-kit recited in claims 6 and 9. However, Sim clearly teaches compound of Example 22 can exhibit cKit inhibitory activity and tyrosine kinase activity and Piris-Villaespesa clearly teaches mutations at specific positions of c-kit recited in claims 6 and 9 are implicated in systemic mastocytosis and tyrosine kinase can be used to treat systemic mastocytosis caused by D816V.Moreover, Crew teaches compounds of the formula (I) that contains similar core (trisubstituted thiophene) as the compound as taught by Sim as having cKIT- inhibitory activity that are used for treating mastocytoskis. Therefore, while Sim provides the broad teaching of the compound of Example 22 exhibiting inhibitory activity for any mutations at any positions of cKit and while Piris-Villaespesa teaches the most frequent KIT mutation found in SM is the D816V KIT mutation, which consists of the replacement of aspartic acid by valine in position 816 of the protein receptor and Martelli teaches Sequencing of KIT cDNA revealed two heterozygous point mutations resulting in a valine to glycine amino acid substitution at codon 560 (V560G) and in an aspartate to valine substitution at codon 816 (D816V) in systemic mastocytosis, one would reasonably expect the compound of example 22 to be effective for treating systemic mastocytosis implicated or caused by an aspartate to valine substitution at codon 816 (D816V) (claim 6) and a valine to glycine amino acid substitution at codon 560 (V560G) (claim 9) and also because Crew teaches compounds of the formula (I) that contains similar core (trisubstituted thiophene) as the compound as taught by Sim as having cKIT- inhibitory activity that are used for treating mastocytoskis.
New Rejection necessitated by claim amendment
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 6 and 9-11 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1 and 10 of U.S. Patent No. US10,442,796 B2 in view of Piris-Villaespesa et al (Front Pharmacol. 2020 Apr 14; 11:443), Martelli et al (Int. J. Mol. Sci. June 1 2020, 21(11), 3987), Crew et al (US2006/0063773 A1).
The U.S. patent claims teach a method for the treatment, prevention, and alleviation of acute myeloid leukemia, the method comprising administering a pharmaceutical composition comprising as an active ingredient, a 2,3,5-substituted thiophene compound, preferably (S)-5-((3-fluorophenyl) ethynyl)-N-(piperidin-3-yl)-3-ureidothiophene-2-carboxamide
PNG
media_image1.png
470
781
media_image1.png
Greyscale
as the active ingredient. (See claims 1 and 10)
Although, the U.S. patent claims do not teach the compound is excellent in ability to inhibit activity of Kit among other proteins, the specification of the U.S. patent claims disclose the compound is excellent in ability to inhibit activity of Kit. (See paragraph [0023].)
The U.S. patent claims do not teach systematic mastocytosis wherein the systematic mastocytosis is caused by substitution of valine or histidine for aspartic acid at amino acid position 816 of c-kit protein. Moreover, the U.S. patent claims do not teach systematic systematic mastocytosis wherein the systematic mastocytosis is caused by substitution of valine for glycine at amino acid position 560 of c-kit protein.
Piris-Villaespesa teaches systemic mastocytosis is a rare and heterogeneous disease characterized by mast cell proliferation and activation. KIT is a transmembrane tyrosine kinase which plays a key role in mast cell growth, differentiation and survival. After interaction with its ligand, the stem cell factor, KIT dimerizes activating downstream pathways involving multiple tyrosine kinases (PI3K, JAK/STAT, RAS/ERK). Activating mutations in KIT are detected in most cases of systemic mastocytosis, being the most common KIT D816V. Therefore, since the emergence of tyrosine kinase inhibitors, KIT inhibition has been an attractive approach when facing mastocytosis treatment. (See Abstract.) Moreover, Piris-Villaespesa teaches the most frequent KIT mutation found in SM (systemic mastocytosis) is the D816V KIT mutation, which consists of the replacement of aspartic acid by valine in position 816 of the protein receptor. (See last paragraph of the left column of page 443.)
Martelli teaches in recent years, molecular characterization and management of patients with systemic mastocytosis (SM) have greatly benefited from the application of advanced technologies. Highly sensitive and accurate assays for KIT D816V mutation detection and quantification have allowed the switch to non-invasive peripheral blood testing for patient screening; allele burden has prognostic implications and may be used to monitor therapeutic efficacy. (See Abstract.) Moreover, Martelli teaches Activating mutations of KIT play a crucial role in the pathogenesis of systemic mastocytosis (SM) by enabling the proliferation and survival of abnormal mast cells (MCs) in affected tissues. The first identification of gain-of-function mutations occurred in the HMC-1 human MCL cell line, which was found to harbor a constitutively activated KIT receptor. Sequencing of KIT cDNA revealed two heterozygous point mutations resulting in a valine to glycine amino acid substitution at codon 560 (V560G) and in an aspartate to valine substitution at codon 816 (D816V). Kitayama et al. expressed the murine equivalents of D816V and V560G mutations in Ba/F3 cell lines, finding that they lead to growth factor-independent proliferation in vitro and tumorigenicity when injected into nude mice. (See last paragraph of page 3.)
Crew teaches a compound represented by the formula (I)
PNG
media_image2.png
728
468
media_image2.png
Greyscale
having cKIT activity for treating tumors or cancers such as mastocytosis/mast cell leukemia among others. (See Abstract, claim 1, and paragraph [0079].)
It would have been prima facie obvious to one of ordinary skill in the art at the time the invention was filed to modify the method of the U.S. patent by including systemic mastocytosis that is caused by substitution of valine or histidine for aspartic acid at amino acid position 816 of c-kit protein and systemic mastocytosis that is caused by substitution of valine for glycine at amino acid position 560 of c-kit protein to give Applicant’s claimed invention. One would have been motivated to do so, because Piris-Villaespesa teaches Kit is activated or detected in most cases of systemic mastocytosis and inhibiting of Kit has been an attractive approach when facing mastocytosis treatment and because Piris-Villaespesa teaches the most frequent KIT mutation found in SM is the D816V KIT mutation, which consists of the replacement of aspartic acid by valine in position 816 of the protein receptor, and also because Martelli teaches Sequencing of KIT cDNA revealed two heterozygous point mutations resulting in a valine to glycine amino acid substitution at codon 560 (V560G) and in an aspartate to valine substitution at codon 816 (D816V) in systemic mastocytosis, and lastly because di-substituted thiophene compounds similar in core structure as the instant compound as having cKit inhibitory activity for treating mastocytosis as taught by Crew. One would reasonably expect the method of U.S. patent claims to be effective for treating systemic mastocytosis that systemic mastocytosis that is caused by substitution of valine or histidine for aspartic acid at amino acid position 816 of c-kit protein and that is caused by substitution of valine for glycine at amino acid position 560 of c-kit protein in addition to acute myeloid leukemia with success by inhibiting the activity of Kit among other proteins.
Claims 6 and 9-11 are rejected on the ground of nonstatutory double patenting as being unpatentable over claim 4 of U.S. Patent No. 18/006,582 in view of Piris-Villaespesa et al (Front Pharmacol. 2020 Apr 14; 11:443) and Martelli et al (Int. J. Mol. Sci. June 1 2020, 21(11), 3987), Crew et al (US2006/0063773 A1).
The copending claims teach a method for treating gastrointestinal stromal tumor comprising a step of administering, to a gastrointestinal stromal tumor patient, a pharmaceutical composition containing a compound represented by the following Formula 1 or a pharmaceutically acceptable salt thereof as an active ingredient: [Formula 1]
PNG
media_image3.png
351
593
media_image3.png
Greyscale
. (See claim 4.) Although, the copending claims do not teach the compound is excellent in ability to inhibit activity of Kit among other proteins, the specification of the U.S. patent claims discloses the compound is excellent in ability to inhibit activity of Kit. (See paragraph [00129].)
The copending claims do not teach The U.S. patent claims do not teach systematic mastocytosis wherein the systematic mastocytosis is caused by substitution of valine or histidine for aspartic acid at amino acid position 816 of c-kit protein. Moreover, the U.S. patent claims do not teach systematic systematic mastocytosis wherein the systematic mastocytosis is caused by substitution of valine for glycine at amino acid position 560 of c-kit protein.
Piris-Villaespesa teaches systemic mastocytosis is a rare and heterogeneous disease characterized by mast cell proliferation and activation. KIT is a transmembrane tyrosine kinase which plays a key role in mast cell growth, differentiation and survival. After interaction with its ligand, the stem cell factor, KIT dimerizes activating downstream pathways involving multiple tyrosine kinases (PI3K, JAK/STAT, RAS/ERK). Activating mutations in KIT are detected in most cases of systemic mastocytosis, being the most common KIT D816V. Therefore, since the emergence of tyrosine kinase inhibitors, KIT inhibition has been an attractive approach when facing mastocytosis treatment. (See Abstract.) Moreover, Piris-Villaespesa teaches the most frequent KIT mutation found in SM (systemic mastocytosis) is the D816V KIT mutation, which consists of the replacement of aspartic acid by valine in position 816 of the protein receptor. (See last paragraph of the left column of page 443.)
Martelli teaches in recent years, molecular characterization and management of patients with systemic mastocytosis (SM) have greatly benefited from the application of advanced technologies. Highly sensitive and accurate assays for KIT D816V mutation detection and quantification have allowed the switch to non-invasive peripheral blood testing for patient screening; allele burden has prognostic implications and may be used to monitor therapeutic efficacy. (See Abstract.) Moreover, Martelli teaches Activating mutations of KIT play a crucial role in the pathogenesis of systemic mastocytosis (SM) by enabling the proliferation and survival of abnormal mast cells (MCs) in affected tissues. The first identification of gain-of-function mutations occurred in the HMC-1 human MCL cell line, which was found to harbor a constitutively activated KIT receptor. Sequencing of KIT cDNA revealed two heterozygous point mutations resulting in a valine to glycine amino acid substitution at codon 560 (V560G) and in an aspartate to valine substitution at codon 816 (D816V). Kitayama et al. expressed the murine equivalents of D816V and V560G mutations in Ba/F3 cell lines, finding that they lead to growth factor-independent proliferation in vitro and tumorigenicity when injected into nude mice. (See last paragraph of page 3.)
Crew teaches a compound represented by the formula (I)
PNG
media_image2.png
728
468
media_image2.png
Greyscale
having cKIT activity for treating tumors or cancers such as mastocytosis/mast cell leukemia among others. (See Abstract, claim 1, and paragraph [0079].)
It would have been prima facie obvious to one of ordinary skill in the art at the time the invention was filed to modify the method of the copending claims by including systemic mastocytosis that is caused by substitution of valine or histidine for aspartic acid at amino acid position 816 of c-kit protein and systemic mastocytosis that is caused by substitution of valine for glycine at amino acid position 560 of c-kit protein to give Applicant’s claimed invention. One would have been motivated to do so, because Piris-Villaespesa teaches Kit is activated or detected in most cases of systemic mastocytosis and inhibiting of Kit has been an attractive approach when facing mastocytosis treatment and because Piris-Villaespesa teaches the most frequent KIT mutation found in SM is the D816V KIT mutation, which consists of the replacement of aspartic acid by valine in position 816 of the protein receptor, and also because Martelli teaches Sequencing of KIT cDNA revealed two heterozygous point mutations resulting in a valine to glycine amino acid substitution at codon 560 (V560G) and in an aspartate to valine substitution at codon 816 (D816V) in systemic mastocytosis, and lastly because di-substituted thiophene compounds similar in core structure as the instant compound as having cKit inhibitory activity for treating mastocytosis as taught by Crew. One would reasonably expect the method of the copending claims to be effective for treating systemic mastocytosis that systemic mastocytosis that is caused by substitution of valine or histidine for aspartic acid at amino acid position 816 of c-kit protein and that is caused by substitution of valine for glycine at amino acid position 560 of c-kit protein in addition to acute myeloid leukemia with success by inhibiting the activity of Kit among other proteins.
Applicant’s argument
Applicant argues that here is no teaching or suggestion from the combination of the claims of the cited application and Piris-Villaespesa that the claimed compound has inhibitory activity with respect to the specific mutations at specific positions of c-kit recited in claims 6 and 9.
Examiner’s response
In response, Applicant’s argument is not persuasive because the new double patenting rejections shows there is motivation to use the method of the U.S. patent claims and the copending claims for treating systemic mastocytosis that systemic mastocytosis that is caused by substitution of valine or histidine for aspartic acid at amino acid position 816 of c-kit protein and that is caused by substitution of valine for glycine at amino acid position 560 of c-kit protein in addition to acute myeloid leukemia with success by inhibiting the activity of Kit among other proteins.
Conclusion
Claims 6 and 9-11 are not allowed.
THIS ACTION IS MADE FINAL. 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.\
Any inquiry concerning this communication or earlier communications from the examiner should be directed to JEAN P CORNET whose telephone number is (571)270-7669. The examiner can normally be reached Monday-Thursday from 7.00am-5.30pm.
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, Amy L Clark can be reached at 571-272-1310. The fax phone number for the organization where this application or proceeding is assigned is 571-273-8300.
Information regarding the status of published or unpublished applications may be obtained from Patent Center. Unpublished application information in Patent Center is available to registered users. To file and manage patent submissions in Patent Center, visit: https://patentcenter.uspto.gov. Visit https://www.uspto.gov/patents/apply/patent-center for more information about Patent Center and https://www.uspto.gov/patents/docx for information about filing in DOCX format. For additional questions, contact the Electronic Business Center (EBC) at 866-217-9197 (toll-free). If you would like assistance from a USPTO Customer Service Representative, call 800-786-9199 (IN USA OR CANADA) or 571-272-1000.
/JEAN P CORNET/ Primary Examiner, Art Unit 1628