DETAILED ACTION
The present application, filed on or after March 16, 2013, is being examined under the first inventor to file provisions of the AIA .
A request for continued examination under 37 CFR 1.114, including the fee set forth in 37 CFR 1.17(e), was filed 11/24/25 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and the fee set forth in 37 CFR 1.17(e) has been timely paid, the finality of the previous Office action has been withdrawn pursuant to 37 CFR 1.114.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 11/24/25 has been entered.
Claims 21-25, 27-29, 32 and 43-46 have been amended.
Claims 21-35, 39-46 are pending.
Claim 26 is withdrawn as being directed to non-elected species.
Claims 21-25, 27-35, and 39-46 are being acted upon.
The following is a quotation of 35 U.S.C. 112(a):
(a) IN GENERAL.—The specification shall contain a written description of the invention, and of the manner and process of making and using it, in such full, clear, concise, and exact terms as to enable any person skilled in the art to which it pertains, or with which it is most nearly connected, to make and use the same, and shall set forth the best mode contemplated by the inventor or joint inventor of carrying out the invention.
The following is a quotation of 35 U.S.C. 112 (pre-AIA ), first paragraph:
The specification shall contain a written description of the invention, and of the manner and process of making and using it, in such full, clear, concise, and exact terms as to enable any person skilled in the art to which it pertains, or with which it is most nearly connected, to make and use the same and shall set forth the best mode contemplated by the inventor of carrying out his invention.
Claims 21-25, 27-35, and 39-46 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 enablement requirement. The claim(s) contains subject matter which was not described in the specification in such a way as to enable one skilled in the art to which it pertains, or with which it is most nearly connected, to make and/or use the invention.
The specification disclosure is insufficient to enable one skilled in the art to practice the invention as claimed without an undue amount of experimentation. Undue experimentation must be considered in light of factors including: the breadth of the claims, the nature of the invention, the state of the prior art, the level of one of ordinary skill in the art, the level of predictability of the art, the amount of direction provided by the inventor, the existence of working examples, and the quantity of experimentation needed to make or use the invention, in re Wands, 858 F.2d at 737, 8 USPQ2d at 1404 (Fed. Cir. 1988).
“The amount of guidance or direction needed to enable the invention is inversely related to the amount of knowledge in the state of the art as well as the predictability in the art.” In re Fisher, 427 F.2d 833, 839, 166 USPQ 18, 24 (CCPA 1970). The “amount of guidance or direction” refers to that information in the application, as originally filed, that teaches exactly how to make or use the invention. The more that is known in the prior art about the nature of the invention, how to make, and how to use the invention, and the more predictable the art is, the less information needs to be explicitly stated in the specification. In contrast, if little is known in the prior art about the nature of the invention and the art is unpredictable, the specification would need more detail as to how to make and use the invention in order to be enabling (MPEP 2164.03)” The MPEP further states that physiological activity can be considered inherently unpredictable.
The claims are directed to a method for the treatment of a cancer in an individual in need thereof, comprising administering recombinant immune cells that comprises a chimeric polypeptide having as scFV that binds to a tumor-associated antigen. Claim 21 is not limited to tumor associated expressed by the cancer in the individual, and claim 21 does not even require that transcriptional regulator is actually released. For example, see claim 22, which further limits the method to contact between the ligand and the scFV and release of the transcriptional regulator. In other words, claim 21 does not require such contact. Likewise, claims 32 and 34 specify that the scFV binds to a target tumor cell and claim 34 recites that the scFV binds to a ligand on the surface of a tumor cell. In other words, claim 21 encompasses intracellular antigens or tumor antigens that are not expressed on the cancer or target cell. Therefore, the dependent claims make clear that claim 21 is specifically intending to encompass cancer treating methods wherein the chimeric polypeptide binds to a genus of tumor associated antigens that are distinct from those expressed in the cancer to be treated, and wherein the administered immune cell does not even need to recognize its targeted ligand in order to treat the cancer. For example, claim 21 would encompass a method of treating a CD19+ leukemia, wherein the chimeric receptor targets a breast tumor associated antigen. Claim 21 also encompasses targeting a genus of intracellular tumor antigens.
The state of the art is such that treating cancer is extremely unpredictable due the heterogeneous nature of the disease and there are numerous challenges in effective treatment (see for example, Carey, 2010). Immune cells expressing chimeric receptors, are used to treat cancer by a mechanism which involves the chimeric receptor recognizing a cell surface antigen expressed by the cancer cell in a subject (see Shirzadian). The recognition can be used to induce a variety of effector functions. For example, upon binding of the CAR to a cancer antigen, the immune cell can be induced to express cytokines or chemokines which stimulate immune cells, or the immune cell can induced to destroy or kill the cancer cells (see Shirzadian). However, using immune cells comprising a chimeric polypeptide as broadly encompassed by the claimed method of cancer treatment would be highly unpredictable.
See also claim 27, which specifically recites that the administered immune cell “modulates” any activity of any target cell in the individual. Page 39 of the instant specification discloses that “modulating” includes ,e.g. stimulating or inhibiting an activity of a target cell. Thus, claim 27 would encompass both stimulating and inhibiting any activity of any target cell in the individual, including stimulating cancer cell activity. While the state of the art is such that targeted immune cells can be used to destroy or kill cancer cells, using targeting immune cells to stimulate or inhibit any activity of any target cell in the individual as a means of treating cancer would be highly unpredictable.
Given the unpredictability of the art and the breadth of the instant claims, the instant specification must provide a sufficient an enabling disclosure commensurate in scope with the instant claims. However, no guidance or examples are provided for treating cancer as broadly encompassed in the present claims, i.e. wherein the chimeric polypeptide targets an intracellular antigen, an antigen not expressed by the cancer, or wherein a target cancer cell activity is “modulated”. Thus, based on the unpredictability of the art, the breadth of the claims, and the lack of guidance provided by the instant specification, it would require undue experimentation to perform the method as broadly claimed.
To overcome the rejection, it is suggested to amend claim 21 to recite wherein the selected ligand is a tumor associated antigen that is expressed on the surface of the cancer cells, and binding of extracellular binding domain to the selected ligand induces proteolytic cleavage and release of the transcriptional regulator, thereby treating the cancer in the individual. The dependent claims should also be amended accordingly. For example, Claim 22 could be amended to recite that the released transcriptional regulatory modulates an activity of the recombinant immune cells. Claim 27 could be amended to recite that the recombinant immune cell destroy or kills the cancer cells in the individual. Claim 28 could be amended to recite that the cancer cells are tumor cells and claim 29 could be cancelled. Claims 32 and 44 could be cancelled, with claim 33 could be amended to depend from claim 21 and limit the individual to a human.
Claims 21-25, 27-35, and 39-46 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. This is a new matter rejection.
The specification and the claims as originally filed do not provide support for the invention as now claimed, specifically:
A chimeric polypeptide that does not comprise “a heterodimerization domain (HD)” (Claim 21, and dependent claims).
Applicant indicates that support for the new limitations can be found in paragraphs 27, 45, and Fig. 1.
A review of the specification fails to reveal support for the new limitations.
The original claims and specification disclose a chimeric polypeptide that does not comprise a heterodimerization domain of a Notch receptor. However, in the present claims, the limitation “of a Notch receptor” has been deleted, thus significantly altering the claim scope. Paragraph 27 and 45 discloses that the chimeric receptor does not require notch NRR, which does not provide support for the negative limitation of not comprising any heterodimerization domain. Figure 1 depicts a specific example in which the notch NRR (LNR/HD) is deleted. In other words, the specification contemplates chimeric polypeptides in which notch NRR is deleted such that the only sequence linking the extracellular domain to the transmembrane domain is, for example, SEQ ID NO :27 (see Fig. 1, Table 1, for example). This does not provide support for the presently claimed negative limitation which has a different scope and excludes chimeric polypeptides comprising any heterodimerization domain anywhere in the chimeric polypeptide. For example, the claims would excluded intracellular domains having heterodimerization domains. The specification does not provide support for the specific negative limitation of the instant claims. See MPEP 2173.05(i). Any negative limitation or exclusionary proviso must have basis in the original disclosure. If alternative elements are positively recited in the specification, they may be explicitly excluded in the claims. However, the negative limitation of the instant claims is not an alternative positively recited limitation the specification. The mere absence of a positive recitation is not basis for an exclusion and silence will not generally suffice to support a negative claim limitation. The original disclosure does not have basis for the claimed negative limitation.
To overcome the new matter rejection, Applicant could consider a claim that limits element b) to a linking polypeptide consisting of SEQ ID NO: 27 or SEQ ID NO: 19, and adding language to indicate that the linking polyepitope is directly linked to both the C-terminus of the scFv and the N-terminus of the transmembrane domain. The instant specification throughout including in Fig. 1 and Table 1 provide support for such a limitation, since it is clear that the specification contemplated chimeric polypeptides wherein the only sequence linking the extracellular scFV to the transmembrane domain is a linking region consisting of SEQ ID NO: 27 or SEQ ID NO: 19. Limiting the linking region in this manner could potentially also overcome the prior art rejection below. Although the chimeric polypeptides made obvious below comprises SEQ ID NO: 27, they would comprise other structural domains from heterologous polypeptides in addition to SEQ ID NO: 27 between the C-terminus of the scFV and the N terminus of transmembrane domain.
The following is a quotation of 35 U.S.C. 103 which forms the basis for all obviousness rejections set forth in this Office action:
A patent for a claimed invention may not be obtained, notwithstanding that the claimed invention is not identically disclosed as set forth in section 102, if the differences between the claimed invention and the prior art are such that the claimed invention as a whole would have been obvious before the effective filing date of the claimed invention to a person having ordinary skill in the art to which the claimed invention pertains. Patentability shall not be negated by the manner in which the invention was made.
Claim 21-25, 27-35, and 39-46 is/are rejected under 35 U.S.C. 103 as being unpatentable over WO2018/039247, in view of Hayward et al., October 2018 and Deatherage, 2017 (all of record).
WO2018/039247 teaches a host cell (i.e. recombinant cells) expressing, from a nucleic acid, a proteolytically cleavable chimeric polypeptide comprising, from N-terminal to C-terminal, an extracellular domain comprising a binding member, a proteolytically cleavable notch receptor polypeptide transmembrane domain comprising a proteolytic cleavage site, and an intracellular domain comprising a transcriptional activator, wherein the binding of the binding member causes cleavage at the proteolytic cleavage site, thereby release the intracellular domain (see page 2-3, in particular). WO2018/039247 teaches that the nucleic acid further comprises a transcriptional control element responsive to the transcriptional activator operatively linked to a nucleic acid sequence encoding a CAR (see page 3, in particular). WO2018/039247 teaches a method of treating a subject for a neoplasia comprising administering to the subject an effective amount of the host cells (see page 5, in particular). WO2018/039247 teaches that upon binding to its ligand in vivo in the treated subject, cleavage is induced thereby releasing the intracellular domain, activating the transcriptional control element and cause the CAR to be expressed (see page 3-5, 23, in particular). WO2018/039247 explains that for example, the chimeric polypeptide can be specific for a tumor antigen, and that chimeric polypeptide is activated upon recognition of the tumor antigen after contact with the tumor in the subject (i.e. “contacting” the cell with the selected ligand, see page 30, in particular). WO2018/039247 further explains that the CAR is induced, whereby the CAR is specific for a tumor antigen and kills the tumor cells expressing the tumor antigen (i.e. modulates the activity of a cancer target cell in the individual). WO2018/039247 teaches treating human subjects and using human cells (See paragraphs 94 and 331, in particular). WO2018/039247 teaches cancer cells including B cell lymphoma, and ovarian cancer (see page 37, in particular).
WO2018/039247 teaches that binding member comprises an antibody scFV specific for a cancer antigen (see page 2, in particular). WO2018/039247 teaches that the extracellular domain may be joined to the rest of the polypeptide via a peptide linker (see page 35 in particular). WO2018/039247 teaches that the proteolytic cleavage site is cleaved by a gamma-secretase (see page 2, in particular). WO2018/039247 also teach that the extracellular domain is a binding member that specifically binds to a target protein present on a human cell or cancer cell, such as PSMA (See page 3 and 4-443 in particular). WO2018/039247 teaches that the chimeric polypeptide includes the sequence RKRRR, i.e. a stop membrane transfer sequence, see page 49, in particular). WO2018/039247 teaches that the intracellular domain comprises a GAL4-VP64 transcriptional activator (see pages 64-65, in particular). WO2018/039247 teaches that the chimeric polypeptide can additionally include a signal sequence, a tag, or a nuclear localization signal (see page 78, in particular). WO2018/039247 teaches that the Notch receptor polypeptide comprises a notch regulatory region, and that it may include or exclude the LIN12/notch repeat domains or one or more heterodimerization domains, and includes a transmembrane domain of notch receptor (see page 48-49 and 61, in particular).
WO2018/039247 does not explicitly teach a chimeric polypeptide that does not comprise a LNR nor a heterodimerization domain of a Notch receptor.
Hayward et al. teach that Notch’s proteolytic switch has been exploited to develop chimeric receptors, and that the switch operates via the negative regulatory region (NRR) comprising the NLR and HD domains, such that upon ligand binding, a conformation change is induced allowing proteolytic cleavage (see pages 3-4, in particular). Hayward et al. also teaches alternative proteolytic regions for use in notch-proteolytic switch signaling systems. For example, Hayward teaches that NRR comprising the LNR and HD domains of Notch can be replaced with AXL, MertK, Tyro3, Her2, or CD44 regions (i.e. regions without a heterodimerization domain), while retaining the Notch transmembrane regions (see page 8, in particular) to provide a proteolytic switch. Hayward et al. teach that doing so can be used to screen for modulators of proteolysis and that said domains are smaller and structurally simpler and might permit more facile trafficking and expression compared to the Notch regulatory region (see pages 18-19, in particular).
Deatherage teaches the structure and amino acid residues of different regions of the Notch 1 receptor, and teaches that it consists of an EGF domain, an NRR domain comprising NLR and HD, a juxtamembrane/transmembrane domain, and in intracellular domain (see Fig. 1). Deatherage teaches that said juxtamembrane and transmembrane domain has a sequence of VQSETVEPPPAQLH, which comprises SEQ ID NO: 27 of the instant application (See Fig. 1, in particular). Deatherage teaches that the juxtamembrane region helps to absorb the strain that the transmembrane domain might experience (See page 5, in particular).
Therefore, it would have been prima facie obvious to one of ordinary skill in the art at the time the invention was made to produce the chimeric receptor of WO2018/039247, using the AXL, MertK, Tyro3, Her2, or CD44 regions in place of NRR, as taught by Hayward, to provide a chimeric antigen receptor that does not comprise Notch LNR or a HD. The ordinary artisan at the time the invention was made would have been motivated to do so and have a reasonable expectation of success because Hayward teaches that said domains are smaller and structurally simpler and might permit more facile trafficking and expression. Said domains can also be considered a “linker”.
Furthermore, it would be obvious to do so, such that the NRR region, which lies N-terminal to residue 1721 as depicted in Figure 1 of Deatherage, is replaced. This would result in a chimeric polypeptide lacking Notch LNR and HD, but retaining SEQ ID NO: 27, which is part of the TM/JMD region that is C-terminal to the NRR domain, as taught by Deatherage (See Fig. 1). The ordinary artisan would be motivated to do so since Deatherage teaches that the NRR region residues N-terminal to residue 1721, and that the juxtamembrane region residing C-terminally to residue 1721 helps to absorb the strain that the transmembrane domain might experience. Additionally, said Notch1 transmembrane domain shares amino acids in common with transmembrane domains of Notch2,3, or 4 (such as the sequence “LL”, and can be considered a transmembrane domain “from” human Notch2, 3 or 4. Alternatively, WO2018/039247 also teaches using transmembrane regions sharing 80-90% identity from other equivalent, homologous proteins, and discloses Notch2-4 as examples of other related Notch proteins, and selecting homologous residues from those transmembrane domains would be obvious.
Applicant’s arguments filed 11/24/25 have been fully considered, but they are not persuasive.
Applicant argues that the SEA like domains used in Hayward function as heterodimerization domains and are not within the scope of the instant claims, which as amended, exclude any heterodimerization domains.
As noted above, Hayward teach other embodiments such as AXL, MertK, Tyro3, Her2, or CD44 regions which would fall within the scope of the instant, i.e. they are not heterodimerization domains.
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 USPTO Internet website contains terminal disclaimer forms which may be used. Please visit www.uspto.gov/patent/patents-forms. The 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/process/file/efs/guidance/eTD-info-I.jsp.
Claims 21-25, 27-35, and 39-46 are rejected on the ground of nonstatutory double patenting as being unpatentable over the claims of U.S. Patent No. 9,670,281, 9,834,608, 10,590,182, 10,822,387, 10,836,808, or 11,617,766, in view of Hayward et al., 20018 and WO 2018/039247 and Deatherage, 2017 (all of record).
The issued patents all claim a chimeric polypeptide, or a nucleic acid encoding said chimeric polypeptide, or methods of making or using said polypeptides for treating cancer, wherein the polypeptide comprises, from N-terminal to C-terminal, an scFV that binds to an antigen, a Notch regulatory region comprising LNR and heterodimerization domain, a transmembrane domain comprising a S3 proteolytic cleavage site, and an intracellular domain comprising a transcription activator. The patents claim that the binding of the scFV to the antigen induces proteolytic cleavage thereby releasing the intracellular domain. The patents claim cleavage by gamma secretase, a stop transfer sequence, and a cell expressing said polypeptide. It would be obvious to substitute the LNR/heterodimerization domains with the domains of Hayward and Deatherage, for the same reasons set forth above. Furthermore, it would be obvious use an scFV specific for tumor antigen such as PSMA and a Gal4-VP64 as a transcription activator and to administer the polypeptides in a T cell expressing them for inducing expression of a CAR, because WO 2018/039247 teaches that doing so is useful for targeting human cancer cells in therapeutic applications.
21-25, 27-35, and 39-46 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-11, of patent 11,401,332, or claims 1-30 of 11,202,801 in view of Hayward et al., 2018 and WO 2018/039247 and Deatherage, 2017 (all of record).
The ‘332 patent claims a host cell comprising a chimeric polypeptide comprising from N-terminal to C-terminal, an extracellular domain that binds to peptide-MHC (i.e. ligand binding), a proteolytically cleavable Notch receptor polypeptide comprising one or more proteolytic cleavage sites, and an intracellular domain comprising a transcriptional activator, wherein binding of the peptide-MHC induces cleavage. The ‘332 patent claims that the binding member is an antibody scFV, that the peptide is a cancer peptide. The ‘332 patent claims that the host cell also comprises nucleic acid encoding a CAR and that binding the chimeric receptor to it ligand induces expression the CAR. It would be obvious to include the domains of Hayward (i.e. linking domains) and Deatherage for the same reasons set forth above. The claims of the ‘801 patent also claim the same subject matter as the ‘332 patent Furthermore, it would be obvious use an scFV specific for tumor antigen such as PSMA and a Gal4-VP64 as a transcription activator, and to administer the host cells to treat cancer because WO 2018/039247 teaches that doing so is useful for targeting human cancer cells in therapeutic applications.
Claims 21-25, 27-35, and 39-46 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-2, 6, 10, -15, 17-18, 20, 23-27, 31, 35-37, 41, 52, 62, 65 of co-pending 17/763,110, or claims 1-3, 6-11, 13-14, 16, 19-21, 23-24, 28, 32-33, 37, 48, 58, 61 of 17/763,116, in view of WO 2018/039247 and Hayward et al., 2018 and Deatherage, 2017 (all of record).
The applications claim a chimeric polypeptide, wherein the polypeptide comprises, from N-terminal to C-terminal, an scFV that binds to ligand, a linking polypeptide having sequence identity to a Notch juxtamembrane domain, a transmembrane domain comprising a proteolytic cleavage site, and an intracellular domain comprising a transcription activator. The applications claim that the binding of the scFV to the antigen induces proteolytic cleavage thereby releasing the intracellular domain. The applications claim that the chimeric polypeptide does not comprise LNR and HD domain of a notch receptor. The applications claim cleavage by gamma secretase, a stop transfer sequence, and a cell expressing said polypeptide. The applications claim that the ligand is PSMA and that the intracellular domain comprises Gal4-VP64. The applications claim administering recombinant cells comprising the chimeric polypeptides to treat a health condition. Additionally, it would be obvious to express a CAR from the cells to treat cancer because WO 2018/039247 teaches that doing so is useful for targeting human cancer cells in therapeutic applications. Furthermore, using the claimed Notch juxtamembrane domain would be obvious over Hayward and Deatherage for the reason set forth above.
This is a provisional nonstatutory double patenting rejection
Claims 21-25, 27-35, 37, and 39-47 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-13, of patent 12,090,170, or the claims of 12,144,826, in view of Hayward et al., 2018 Deatherage, 2017, and WO 2018/039247. The patents claim a method of treating cancer comprising administering to a subject a genetically modified cell expressing a binding triggered transcriptional switch (i.e. a chimeric polypeptide) comprising an extracellular domain that binds to BCAN (a tumor antigen), a transmembrane domain and one or more protease cleavage domains, and a transcriptional activation, wherein binding release the transcriptional activator that binds to a regulatory sequence and activates expression of a CAR. The other features of the chimeric polypeptide and the cancer treatment method would be obvious based on the teachings of Hayward et al., 2018, Deatherage, and WO 2018/039247 for the same reasons set forth above.
Claims 21-25, 27-35, 37, and 39-47 are rejected on the ground of nonstatutory double patenting as being unpatentable over the claims of co-pending 17/762,685, 17/763,122 or 17/762,687, 17,995,765, 17/995,751, 18/043,716, 18/178,440, 18/551,931, 18/552,131, 18/552,141, 18,912,410, 17/069,717, 17/763,122, 18/737,881, 18/393,538, 18/630,828, 17/841,595, 18/551,935, 19/075,639, 19/104,008, or 19/104,002, in view of Hayward, Deatherage, and WO 2018/039247.
The applications all claim a chimeric polypeptide acting via proteolytic cleavage site having various features of the present claims, including an intracellular domain comprising a transcription activator. The other features of the instant claims are obvious over Hayward, Deatherage, and WO 2018/039247 for the reasons set forth above.
This is a provisional nonstatutory double patenting rejection.
Applicant’s statement that the double patenting rejections be held in abeyance until allowance is acknowledged.
No claim is allowed.
Any inquiry concerning this communication or earlier communications from the examiner should be directed to AMY E JUEDES whose telephone number is (571)272-4471. The examiner can normally be reached on M-F from 7am to 3pm.
If attempts to reach the examiner by telephone are unsuccessful, the examiner’s supervisor, Misook Yu can be reached on 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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Amy E. Juedes
Patent Examiner
Technology Center 1600
/AMY E JUEDES/Primary Examiner, Art Unit 1644