Prosecution Insights
Last updated: April 19, 2026
Application No. 18/327,651

CHIMERIC TRANSMEMBRANE PROTEINS AND USES THEREOF

Non-Final OA §102§103§112
Filed
Jun 01, 2023
Examiner
NGUYEN, QUANG
Art Unit
1631
Tech Center
1600 — Biotechnology & Organic Chemistry
Assignee
Kite Pharma Inc.
OA Round
1 (Non-Final)
38%
Grant Probability
At Risk
1-2
OA Rounds
3y 11m
To Grant
91%
With Interview

Examiner Intelligence

Grants only 38% of cases
38%
Career Allow Rate
280 granted / 734 resolved
-21.9% vs TC avg
Strong +53% interview lift
Without
With
+52.7%
Interview Lift
resolved cases with interview
Typical timeline
3y 11m
Avg Prosecution
65 currently pending
Career history
799
Total Applications
across all art units

Statute-Specific Performance

§101
1.9%
-38.1% vs TC avg
§103
37.9%
-2.1% vs TC avg
§102
15.8%
-24.2% vs TC avg
§112
27.8%
-12.2% vs TC avg
Black line = Tech Center average estimate • Based on career data from 734 resolved cases

Office Action

§102 §103 §112
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 . Applicant’s amendment filed on 01/06/2026 has been entered. Claims 1-20 are pending in the present application. Applicant’s election of Group I, drawn to a protein comprising a transmembrane domain of an alpha chain of interleukin-7 receptor with one or more modifications, in the reply filed on 01/06/2026 is acknowledged. Because applicant did not distinctly and specifically point out the supposed errors in the restriction requirement, the election has been treated as an election without traverse (MPEP § 818.01(a)). With respect to the elected Group I, Applicant also elected the following species: (i) SEQ ID NO: 6 as a species of a transmembrane domain with one or more modifications; (ii) SEQ ID NO: 22 as a species of an extracellular interleukin-15 domain; (iii) SEQ ID NO: 36 as a species of an extracellular sushi domain of the alpha chain of interleukin-15 receptor. Accordingly, claims 9-20 were withdrawn from further consideration because they are directed to non-elected inventions. Therefore, claims 1-8 are examined on the merits herein with the above elected species. Claim Rejections - 35 USC § 112 The following is a quotation of the first paragraph 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 the first paragraph of pre-AIA 35 U.S.C. 112: 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 1-8 are rejected under 35 U.S.C. 112(a) or 35 U.S.C. 112 (pre-AIA ), first paragraph, because the specification, while being enabling for: A protein comprising a transmembrane domain of an alpha chain of interleukin-7 receptor and an intracellular domain of an alpha chain of interleukin-7 receptor, wherein the transmembrane domain comprises the sequence of SEQ ID NO: 6 or 8; does not reasonably provide enablement for any other protein as encompassed broadly by the instant claims. The specification does not enable any person skilled in the art to which it pertains, or with which it is most nearly connected, to make and use the invention commensurate in scope with these claims. The factors to be considered in the determination of an enabling disclosure have been summarized as the quantity of experimentation necessary, the amount of direction or guidance presented, the state of the prior art, the relative skill of those in the art, the predictability or unpredictability of the art and the breadth of the claims. Ex parte Forman, (230 USPQ 546 (Bd Pat. Appl & Unt, 1986); In re Wands, 858 F.2d 731, 8 USPQ 2d 1400 (Fed. Cir. 1988)). When read in light of the present specification, the sole purpose for a protein that includes a transmembrane domain of an alpha chain of interleukin-7 receptor with one or more modifications (e.g., a modified transmembrane domain with the sequence of SEQ ID NO: 2, 4, 6, or 8) is to increase downstream signaling for such protein via homodimerization as compared to a corresponding protein that includes a wildtype transmembrane domain of an alpha chain of interleukin-7 receptor (see at least Summary, particularly first full paragraph at page 2; and Figs. 2 and 4). The instant specification is not enabled for the instant broadly claimed invention for the reasons discussed below. 1. The breadth of the claims With respect to the elected species, the instant claims encompass at least any protein (e.g., a protein without an intracellular domain and/or an ectodomain; and not necessarily limited to a cytokine receptor having an intracellular domain) as long as it comprises a transmembrane domain of an alpha chain of interleukin-7 receptor with one or more modifications, wherein the transmembrane domain with one of more modifications has a sequence of SEQ ID NO: 6 (e.g., a sequence of 2, 3, 4, 5, 6, 7 or more amino acids of the 28-amino-acid sequence of SEQ ID NO: 6); the same protein further comprising an intracellular domain of an alpha chain of interleukin-7 receptor comprising a sequence of SEQ ID NO: 45 (e.g., a sequence of 2, 3, 4, 5, 10, 20, 40, 50 or more amino acids of the 195-amino-acid sequence of SEQ ID NO: 45); the same protein further comprising an extracellular domain of an alpha chain of interleukin-7 receptor comprising a sequence of SEQ ID NO: 11 (e.g., a sequence of 2, 3, 4, 5, 10, 20, 40, 50 or more amino acids of the 220-amino-acid sequence of SEQ ID NO: 45); or the same protein further comprising an extracellular interleukin-15 domain having a sequence of SEQ ID NO: 22 (e.g., a sequence of 2, 3, 4, 5, 10, 20, 40, 50 or more amino acids of the 114-amino-acid sequence of SEQ ID NO: 22) and an extracellular sushi domain from an alpha chain of interleukin-15 receptor comprising SEQ ID NO:36. 2. The state and the unpredictability of the prior art Before the effective filing date of the present application (06/05/2020), little was known about a protein comprising a transmembrane domain of an alpha chain of interleukin-7 receptor with a sequence of SEQ ID NO: 6 or 8 as claimed broadly by the instant claims as evidenced at least by the teachings of Shum et al (WO 2018/038945), Anderson et al (WO 2016/174461), Lofquist et al (WO 2010/003108) and Jacques et al (US 10,358,477). Moreover, the physiological art is already recognized as unpredictable (MPEP 2164.03). 3. The amount of direction or guidance provided Apart from disclosing a protein comprising a transmembrane domain of an alpha chain of interleukin-7 receptor with one or more modifications (e.g., a modified transmembrane domain with the sequence of SEQ ID NO: 2, 4, 6, or 8) and an intracellular domain of an alpha chain of interleukin-7 receptor, wherein the modified transmembrane domain facilitates homodimerization of the protein to induce an increased downstream STAT5 signaling pathway as compared to a corresponding protein that includes a wildtype transmembrane domain of an alpha chain of interleukin-7 receptor, and thereby activating immune cells such as T cells (see at least Summary, particularly first full paragraph at page 2; and Figs. 2 and 4); the instant specification failed to provide sufficient guidance for an ordinary skilled artisan on how to make and use any other proteins as encompassed broadly by the instant claims, particularly those that do not even include any intracellular domain of any receptor, let alone without an intracellular domain of an alpha chain of interleukin-7 receptor. For example, without the presence of an intracellular domain of an alpha chain of interleukin-7 receptor what is the use of a protein containing the disclosed modified transmembrane domain of an alpha chain of interleukin-7 receptor? Additionally, apart from the modified transmembrane domain comprising the sequence of SEQ ID NO: 6 the instant specification fails to provide sufficient guidance for a skill in the art on how to make and use any fragment of SEQ ID NO: 6 of any length, and yet such fragments of SEQ ID NO:6 still retain the ability to facilitate homodimerization to induce downstream signaling pathway. Similarly, the instant specification also fails to provide sufficient guidance for a skill in the art on how to make and use any fragment of any length for the intracellular domain of an alpha chain of interleukin-7 receptor with SEQ ID NO: 45; and yet such a fragment is still capable of inducing a downstream signaling, particularly inducing the STAT5 signaling pathway that is useful for activating T cells in the context of immunotherapy. Moreover, the instant specification also fails to provide sufficient guidance on how to make and use any fragment of an extracellular domain of an alpha chain of interleukin-7 receptor with SEQ ID NO: 11 and/or any fragment an extracellular interleukin-15 domain with SEQ ID NO: 22 or 24 as encompassed broadly by the instant claims. Since the prior art before the effective filing date of the present application failed to provide sufficient guidance regarding to the aforementioned issues, it is incumbent upon the present application to do so. Given the state of the prior art, coupled with the lack of sufficient guidance provided by the present application, it would have required undue experimentation for a skilled artisan to make and use the instant invention as claimed broadly. As set forth in In re Fisher, 166 USPQ 18 (CCPA 1970), compliance with 35 USC 112, first paragraph requires: That scope of claims must bear a reasonable correlation to scope of enablement provided by specification to persons of ordinary skill in the art; in cases involving predictable factors, such as mechanical or electrical elements, a single embodiment provides broad enablement in the sense that, once imagined, other embodiments can be made without difficulty and their performance characteristics predicted by resort to known scientific laws; in cases involving unpredictable factors, such as most chemical reactions and physiological activity, scope of enablement varies inversely with degree of unpredictability of factors involved. Moreover, the courts have also stated that reasonable correlation must exist between scope of exclusive right to patent application and scope of enablement set forth in the patent application (27 USPQ2d 1662 Ex parte Maizel.). Accordingly, due to the lack of sufficient guidance provided by the specification regarding to the issues set forth above, the state and unpredictability of the relevant art, and the breadth of the instant claims, it would have required undue experimentation for one skilled in the art to make and use the instant broadly claimed invention. Claim Rejections - 35 USC § 102 The following is a quotation of the appropriate paragraphs of 35 U.S.C. 102 that form the basis for the rejections under this section made in this Office action: A person shall be entitled to a patent unless – (a)(1) the claimed invention was patented, described in a printed publication, or in public use, on sale, or otherwise available to the public before the effective filing date of the claimed invention. Claims 1-2 and 4 are rejected under 35 U.S.C. 102(a)(1) as being anticipated by Shum et al (WO 2018/038945). The instant claims encompass a protein comprising a transmembrane domain of an alpha chain of interleukin-7 receptor with one or more modifications, wherein the transmembrane domain with one or more modifications has a sequence of SEQ ID NO: 6 (elected species). Shum et al already disclosed a constitutive active engineered cytokine receptor in which the transmembrane domain and endo-domain are able to provide an activating signal separately from any input to the corresponding exodomain for which they are operably linked, for enhancing expansion of immune cells (e.g., T cells) for immunotherapy, wherein the transmembrane domain comprises one or more mutations that cause or facilitate homodimerization, and therefore signaling, in the absence of binding of the cognate cytokine (see Abstract; particularly paragraphs [0005]-[0011], [0052]; and Figs. 1-3). Shum et al taught specifically that the receptor comprise at least one exodomain, a transmembrane domain, and at least one endo-domain, wherein the endo-domain is derived from a cytokine receptor and wherein the exodomain is derived from the same or a different molecule that the transmembrane and endo-domain components, or the transmembrane domain and the exodomain are from the same molecule and the endo-domain is from a different molecule, but the receptor is still constitutively active because the molecule includes a mutation that twists the transmembrane domain and/or endo-domain (paragraph [0052]). In a specific embodiment, a constitutive engineered cytokine receptor comprises an insertion of a trimer peptide of cysteine, proline, threonine (CPT) into the transmembrane domain of the IL-7Rα receptor, including the transmembrane domain having SEQ ID NO: 2 that is 100% identical to the elected sequence of SEQ ID NO: 6 of the present application (paragraphs [0074]-[0077]; attached sequence search below). Shum et al stated “The constitutively active cytokine receptor comprises one or more endo-domains. In some cases, the endo-domain is from the same molecule as the transmembrane domain, although in other cases it is not….Immunostimulatory cytokine endo-domains useful for receptors of the disclosure include IL-7Ra receptor alpha, CD122 (the common receptor beta of IL-2 and IL-15), IL-21 receptor alpha, IL-23 receptor alpha, and IL-12 receptor alpha and IL-6 receptor, for example” (paragraph [0080]); and “In some embodiments the endo-domain is selected based on the desired downstream pathway. For example, the endo-domain may be selected based on the desired for the signal to be transmitted via JAK1, STAT5, STAT4, JAK3, STAT3, and so on…In certain cases the signaling pathway includes STAT5. STAT5 is a major downstream signaling node of immunostimulatory cytokines IL-15 and IL-7, both of which are known to be useful in activating T-cells in the context of immunotherapy” (paragraphs [0081]-[0082]). Accordingly, the teachings of Shum et al meet every limitation of the instant claims. Therefore, the reference anticipates the instant claims. Claim Rejections - 35 USC § 103 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. Claims 1-5 are rejected under 35 U.S.C. 103 as being unpatentable over Shum et al (WO 2018/038945) in view of Anderson et al (WO 2016/174461) and Lofquist et al (WO 2010/003108). Shum et al already disclosed a constitutive active engineered cytokine receptor in which the transmembrane domain and endo-domain are able to provide an activating signal separately from any input to the corresponding exodomain for which they are operably linked, for enhancing expansion of immune cells (e.g., T cells) for immunotherapy, wherein the transmembrane domain comprises one or more mutations that cause or facilitate homodimerization, and therefore signaling, in the absence of binding of the cognate cytokine (see Abstract; particularly paragraphs [0005]-[0011], [0052]; and Figs. 1-3). Shum et al taught specifically that the receptor comprise at least one exodomain, a transmembrane domain, and at least one endo-domain, wherein the endo-domain is derived from a cytokine receptor and wherein the exodomain is derived from the same or a different molecule than the transmembrane and endo-domain components, or the transmembrane domain and the exodomain are from the same molecule and the endo-domain is from a different molecule, but the receptor is still constitutively active because the molecule includes a mutation that twists the transmembrane domain and/or endo-domain (paragraph [0052]). In a specific embodiment, a constitutive engineered cytokine receptor comprises an insertion of a trimer peptide of cysteine, proline, threonine (CPT) into the transmembrane domain of the IL-7Rα receptor, including the transmembrane domain having SEQ ID NO: 2 that is 100% identical to the elected sequence of SEQ ID NO: 6 of the present application (paragraphs [0074]-[0077]; attached sequence search below). Shum et al stated “The constitutively active cytokine receptor comprises one or more endo-domains. In some cases, the endo-domain is from the same molecule as the transmembrane domain, although in other cases it is not….Immunostimulatory cytokine endo-domains useful for receptors of the disclosure include IL-7Ra receptor alpha, CD122 (the common receptor beta of IL-2 and IL-15), IL-21 receptor alpha, IL-23 receptor alpha, and IL-12 receptor alpha and IL-6 receptor, for example” (paragraph [0080]); and “In some embodiments the endo-domain is selected based on the desired downstream pathway. For example, the endo-domain may be selected based on the desired for the signal to be transmitted via JAK1, STAT5, STAT4, JAK3, STAT3, and so on…In certain cases the signaling pathway includes STAT5. STAT5 is a major downstream signaling node of immunostimulatory cytokines IL-15 and IL-7, both of which are known to be useful in activating T-cells in the context of immunotherapy” (paragraphs [0081]-[0082]). Shum et al did not teach specifically using the intracellular domain having a sequence of SEQ ID NO: 45, or the extracellular domain having a sequence of SEQ ID NO: 11 for the disclosed constitutive active engineered cytokine receptor comprising the transmembrane domain of the IL-7Rα receptor with SEQ ID NO: 2. Before the effective filing date of the present application (06/22/2018), Anderson et al already disclosed using the IL7-R endo-domain of SEQ ID NO: 15 that is 100% identical to SEQ ID NO: 45 of the present application for an endo-domain of a chimeric antigen receptor (CAR) to be expressed in a T cell (see at least Abstract; page 2, lines 27-29; page 14, lines 12-16; and attached sequence search below). Additionally, Lofquist et al already taught at least the extracellular domain/ectodomain of IL7Rα having the first 240 amino acids of SEQ ID NO: 738 that is 100% identical to SEQ ID NO: 11 of the present application, as an IL7 antagonist for a multi-target fusion protein (see at least Abstract; particularly paragraphs [0072], [0074] and [0075]; and attached sequence search below). Accordingly, it would have been obvious for an ordinary skilled artisan to modify the teachings of Shum et al by also selecting the IL7-R endo-domain of SEQ ID NO: 15 and/or the extracellular domain/ectodomain of IL7Rα having the first 240 amino acids of SEQ ID NO: 738 for the disclosed constitutive active engineered cytokine receptor comprising the transmembrane domain of the IL-7Rα receptor with SEQ ID NO: 2, in light of the teachings of Anderson et al and Lofquist et al as set forth above. An ordinary skilled artisan would have been motivated to carry out the above modifications because the IL7-R endo-domain of SEQ ID NO: 15 and/or the extracellular domain/ectodomain of IL7Rα having the first 240 amino acids of SEQ ID NO: 738 are known in the prior art as taught by Anderson et al and Lofquist et al, respectively. Moreover, the primary Shum reference already taught explicitly that IL-7R receptor alpha endo-domain is useful for the disclosed constitutive active engineered cytokine receptor, and the exodomain can be derived from the same molecule as the transmembrane and endo-domain components. An ordinary skilled artisan would have a reasonable expectation of success in light of the teachings of Shum et al, Anderson et al and Lofquist et al; coupled with a high level of skill for an ordinary skilled artisan in the relevant art. The modified protein resulting from the combined teachings of Shum et al, Anderson et al and Lofquist et al as set forth above is indistinguishable and encompassed by the presently claimed method. Therefore, the claimed invention as a whole was prima facie obvious in the absence of evidence to the contrary. Claims 1 and 6-8 are rejected under 35 U.S.C. 103 as being unpatentable over Shum et al (WO 2018/038945) in view of Jacques et al (US 10,358,477). The instant claims encompass a protein comprising a transmembrane domain of an alpha chain of interleukin-7 receptor with one or more modifications, wherein the transmembrane domain with one or more modifications has a sequence of SEQ ID NO: 6 (elected species), wherein the protein further comprising an extracellular interleukin-15 domain, preferably the extracellular interleukin-15 domain comprising a sequence of SEQ ID NO: 22 (elected species), and an extracellular sushi domain from an alpha chain of interleukin-15 receptor, preferably one comprising the elected SEQ ID NO: 36. Shum et al already disclosed a constitutive active engineered cytokine receptor in which the transmembrane domain and endo-domain are able to provide an activating signal separately from any input to the corresponding exodomain for which they are operably linked, for enhancing expansion of immune cells (e.g., T cells) for immunotherapy, wherein the transmembrane domain comprises one or more mutations that cause or facilitate homodimerization, and therefore signaling, in the absence of binding of the cognate cytokine (see Abstract; particularly paragraphs [0005]-[0011], [0052]; and Figs. 1-3). Shum et al taught specifically that the receptor comprise at least one exodomain, a transmembrane domain, and at least one endo-domain, wherein the endo-domain is derived from a cytokine receptor and wherein the exodomain is derived from the same or a different molecule than the transmembrane and endo-domain components, or the transmembrane domain and the exodomain are from the same molecule and the endo-domain is from a different molecule, but the receptor is still constitutively active because the molecule includes a mutation that twists the transmembrane domain and/or endo-domain (paragraph [0052]). Shum et al further taught that the constitutively active cytokine receptor comprises one, two, or more exodomains; the exodomain is capable of binding a ligand but the signal itself is not transmitted, for example because of structural or other reasons; and the exodomain may or may not be from the same natural molecule as its corresponding transmembrane and/or endo-domain (paragraph [0059]). In a specific embodiment, a constitutive engineered cytokine receptor comprises an insertion of a trimer peptide of cysteine, proline, threonine (CPT) into the transmembrane domain of the IL-7Rα receptor, including the transmembrane domain having SEQ ID NO: 2 that is 100% identical to the elected sequence of SEQ ID NO: 6 of the present application (paragraphs [0074]-[0077]; attached sequence search below). Shum et al stated “The constitutively active cytokine receptor comprises one or more endo-domains. In some cases, the endo-domain is from the same molecule as the transmembrane domain, although in other cases it is not….Immunostimulatory cytokine endo-domains useful for receptors of the disclosure include IL-7Ra receptor alpha, CD122 (the common receptor beta of IL-2 and IL-15), IL-21 receptor alpha, IL-23 receptor alpha, and IL-12 receptor alpha and IL-6 receptor, for example” (paragraph [0080]); and “In some embodiments the endo-domain is selected based on the desired downstream pathway. For example, the endo-domain may be selected based on the desired for the signal to be transmitted via JAK1, STAT5, STAT4, JAK3, STAT3, and so on…In certain cases the signaling pathway includes STAT5. STAT5 is a major downstream signaling node of immunostimulatory cytokines IL-15 and IL-7, both of which are known to be useful in activating T-cells in the context of immunotherapy” (paragraphs [0081]-[0082]). Shum et al did not teach specifically that the disclosed constitutive active engineered cytokine receptor comprising the transmembrane domain of the IL-7Rα receptor with SEQ ID NO: 2, further comprising an extracellular interleukin-15 domain, preferably the extracellular interleukin-15 domain comprising a sequence of SEQ ID NO: 22, and an extracellular sushi domain from an alpha chain of interleukin-15 receptor, preferably one comprising the elected SEQ ID NO: 36; even though Shum et al also taught that the preferred signaling pathway is STAT5 which is a major downstream signaling node of immunostimulatory cytokines IL-15 and IL-7, both of which are known to be useful in activating T cells in the context of immunotherapy. Before the effective filing date of the present application (06/22/2018), Jacques et al already disclosed at least a fusion protein comprising a sushi-containing polypeptide (an amino acid sequence of the extracellular region of IL-15Ralpha) and an IL-15, preferably the IL-15 is the human IL-15 of SEQ ID NO: 48 that is 100% identical to SEQ ID NO: 22 of the present application and the sushi containing polypeptide is SEQ ID NO: 22 that is 100% identical to SEQ ID NO: 36 of the present application, for stimulating the IL-15Rbeta/gamma signaling pathway, to thereby induce and/or stimulating the activation and/or proliferation and/or prevention of apoptosis of IL-15Rbeta/gamma-positive cells such as NK and/or T cells (Abstract; col. 7, line 29 continues to line 9 at col. 8; col. 8, lines 43-48; col. 17, lines 21-25; and attached sequence searches below). Jacques et al also taught that such fusion protein has 30 to150 fold increase in bioactivity, compared to wild type IL-15, and be more potent than the free association of IL-15 and soluble IL-15R alpha sushi domain (col. 7, lines 51-54). Accordingly, it would have been obvious for an ordinary skilled artisan to modify the teachings of Shum et al by also selecting the fusion protein comprising the sushi-containing polypeptide of SEQ ID NO: 22 and the human IL-15 of SEQ ID NO: 48 as an exodomain for the disclosed constitutive active engineered cytokine receptor comprising the transmembrane domain of the IL-7Rα receptor with SEQ ID NO: 2 for activating T cells, in light of the teachings of Jacques et al as set forth above. An ordinary skilled artisan would have been motivated to carry out the above modification because Jacques et al taught that the fusion protein comprising the sushi-containing polypeptide of SEQ ID NO: 22 and the human IL-15 of SEQ ID NO: 48 is capable of stimulating the IL-15Rbeta/gamma signaling pathway, to thereby induce and/or stimulating the activation and/or proliferation and/or prevention of apoptosis of IL-15Rbeta/gamma-positive cells such as NK and/or T cells. Moreover, the primary Shum reference already taught explicitly that the preferred signaling pathway is STAT5 which is a major downstream signaling node of immunostimulatory cytokines IL-15 and IL-7, both of which are known to be useful in activating T cells in the context of immunotherapy. An ordinary skilled artisan would have a reasonable expectation of success in light of the teachings of Shum et al and Jacques et al; coupled with a high level of skill for an ordinary skilled artisan in the relevant art. The modified protein resulting from the combined teachings of Shum et al and Jacques et al as set forth above is indistinguishable and encompassed by the presently claimed method. Therefore, the claimed invention as a whole was prima facie obvious in the absence of evidence to the contrary. Conclusion No claim is allowed. Any inquiry concerning this communication or earlier communications from the examiner should be directed to Quang Nguyen, Ph.D., at (571) 272-0776. If attempts to reach the examiner by telephone are unsuccessful, the examiner’s SPE, James Douglas (Doug) Schultz, Ph.D., may be reached at (571) 272-0763. To aid in correlating any papers for this application, all further correspondence regarding this application should be directed to Group Art Unit 1631; Central Fax No. (571) 273-8300. Any inquiry of a general nature or relating to the status of this application or proceeding should be directed to (571) 272-0547. Patent applicants with problems or questions regarding electronic images that can be viewed in the Patent Application Information Retrieval system (PAIR) can now contact the USPTO’s Patent Electronic Business Center (Patent EBC) for assistance. Representatives are available to answer your questions daily from 6 am to midnight (EST). The toll-free number is (866) 217-9197. When calling please have your application serial or patent number, the type of document you are having an image problem with, the number of pages and the specific nature of the problem. The Patent Electronic Business Center will notify applicants of the resolution of the problem within 5-7 business days. Applicants can also check PAIR to confirm that the problem has been corrected. The USPTO’s Patent Electronic Business Center is a complete service center supporting all patent business on the Internet. The USPTO’s PAIR system provides Internet-based access to patent application status and history information. It also enables applicants to view the scanned images of their own application file folder(s) as well as general patent information available to the public. /QUANG NGUYEN/Primary Examiner, Art Unit 1631 Mutant IL-7 cytokine receptor alpha transmembrane domain, SEQ ID 2. WO2018038945-A1. Query Match 100.0%; Score 141; Length 28; Best Local Similarity 100.0%; Matches 28; Conservative 0; Mismatches 0; Indels 0; Gaps 0; Qy 1 PILLTCPTISILSFFSVALLVILACVLW 28 |||||||||||||||||||||||||||| Db 1 PILLTCPTISILSFFSVALLVILACVLW 28 IL7R endodomain polypeptide sequence, SEQ ID 15. WO2016174461-A1. Query Match 100.0%; Score 1025; Length 195; Best Local Similarity 100.0%; Matches 195; Conservative 0; Mismatches 0; Indels 0; Gaps 0; Qy 1 KKRIKPIVWPSLPDHKKTLEHLCKKPRKNLNVSFNPESFLDCQIHRVDDIQARDEVEGFL 60 |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||| Db 1 KKRIKPIVWPSLPDHKKTLEHLCKKPRKNLNVSFNPESFLDCQIHRVDDIQARDEVEGFL 60 Qy 61 QDTFPQQLEESEKQRLGGDVQSPNCPSEDVVITPESFGRDSSLTCLAGNVSACDAPILSS 120 |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||| Db 61 QDTFPQQLEESEKQRLGGDVQSPNCPSEDVVITPESFGRDSSLTCLAGNVSACDAPILSS 120 Qy 121 SRSLDCRESGKNGPHVYQDLLLSLGTTNSTLPPPFSLQSGILTLNPVAQGQPILTSLGSN 180 |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||| Db 121 SRSLDCRESGKNGPHVYQDLLLSLGTTNSTLPPPFSLQSGILTLNPVAQGQPILTSLGSN 180 Qy 181 QEEAYVTMSSFYQNQ 195 ||||||||||||||| Db 181 QEEAYVTMSSFYQNQ 195 Human IL7Ralpha ectodomain protein SEQ ID NO:738. WO2010003108-A2. Query Match 100.0%; Score 1166; Length 240; Best Local Similarity 100.0%; Matches 220; Conservative 0; Mismatches 0; Indels 0; Gaps 0; Qy 1 GESGYAQNGDLEDAELDDYSFSCYSQLEVNGSQHSLTCAFEDPDVNITNLEFEICGALVE 60 |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||| Db 20 GESGYAQNGDLEDAELDDYSFSCYSQLEVNGSQHSLTCAFEDPDVNITNLEFEICGALVE 79 Qy 61 VKCLNFRKLQEIYFIETKKFLLIGKSNICVKVGEKSLTCKKIDLTTIVKPEAPFDLSVVY 120 |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||| Db 80 VKCLNFRKLQEIYFIETKKFLLIGKSNICVKVGEKSLTCKKIDLTTIVKPEAPFDLSVVY 139 Qy 121 REGANDFVVTFNTSHLQKKYVKVLMHDVAYRQEKDENKWTHVNLSSTKLTLLQRKLQPAA 180 |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||| Db 140 REGANDFVVTFNTSHLQKKYVKVLMHDVAYRQEKDENKWTHVNLSSTKLTLLQRKLQPAA 199 Qy 181 MYEIKVRSIPDHYFKGFWSEWSPSYYFRTPEINNSSGEMD 220 |||||||||||||||||||||||||||||||||||||||| Db 200 MYEIKVRSIPDHYFKGFWSEWSPSYYFRTPEINNSSGEMD 239 Sequence 22, Patent No. 10358477 Query Match 100.0%; Score 342; Length 62; Best Local Similarity 100.0%; Matches 62; Conservative 0; Mismatches 0; Indels 0; Gaps 0; Qy 1 CPPPMSVEHADIWVKSYSLYSRERYICNSGFKRKAGTSSLTECVLNKATNVAHWTTPSLK 60 |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||| Db 1 CPPPMSVEHADIWVKSYSLYSRERYICNSGFKRKAGTSSLTECVLNKATNVAHWTTPSLK 60 Qy 61 CI 62 || Db 61 CI 62 Sequence 48, Patent No. 10358477 Query Match 100.0%; Score 581; Length 114; Best Local Similarity 100.0%; Matches 114; Conservative 0; Mismatches 0; Indels 0; Gaps 0; Qy 1 NWVNVISDLKKIEDLIQSMHIDATLYTESDVHPSCKVTAMKCFLLELQVISLESGDASIH 60 |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||| Db 1 NWVNVISDLKKIEDLIQSMHIDATLYTESDVHPSCKVTAMKCFLLELQVISLESGDASIH 60 Qy 61 DTVENLIILANNSLSSNGNVTESGCKECEELEEKNIKEFLQSFVHIVQMFINTS 114 |||||||||||||||||||||||||||||||||||||||||||||||||||||| Db 61 DTVENLIILANNSLSSNGNVTESGCKECEELEEKNIKEFLQSFVHIVQMFINTS 114
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Prosecution Timeline

Jun 01, 2023
Application Filed
Jan 28, 2026
Non-Final Rejection — §102, §103, §112 (current)

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Study what changed to get past this examiner. Based on 5 most recent grants.

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Prosecution Projections

1-2
Expected OA Rounds
38%
Grant Probability
91%
With Interview (+52.7%)
3y 11m
Median Time to Grant
Low
PTA Risk
Based on 734 resolved cases by this examiner. Grant probability derived from career allow rate.

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