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 .
DETAILED ACTION
Election/Restrictions
Applicant’s election with traverse in the reply filed on 07/10/2025 is acknowledged and considered persuasive. Upon further consideration, the Examiner is withdrawing the restriction requirement filed 04/10/2025. All groups and species will be under examination in the instant Office Action.
Claims 1-3, 6-7, 10, 12-13, 16, 19, 22-23, 26-34, 37, 50, and 55-57 are under consideration.
Claim Rejections - 35 USC § 112
The following is a quotation of 35 U.S.C. 112(b):
(b) CONCLUSION.—The specification shall conclude with one or more claims particularly pointing out and distinctly claiming the subject matter which the inventor or a joint inventor regards as the invention.
The following is a quotation of 35 U.S.C. 112 (pre-AIA ), second paragraph:
The specification shall conclude with one or more claims particularly pointing out and distinctly claiming the subject matter which the applicant regards as his invention.
Claim 12 is rejected under 35 U.S.C. 112(b) or 35 U.S.C. 112 (pre-AIA ), second paragraph, as being indefinite for failing to particularly point out and distinctly claim the subject matter which the inventor or a joint inventor (or for applications subject to pre-AIA 35 U.S.C. 112, the applicant), regards as the invention.
Instant claim 12 recites the term “optionally”. The phrase “optionally” is interpreted as "for example" which renders the claim indefinite because it is unclear whether the limitation(s) following the phrase are part of the claimed invention. For the purposes of examination, the instant claims will be interpreted without the optional limitations as they are not required or claimed as necessary to the invention.
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 1-3, 6-7, 10, 12-13, 16, 19, 22-23, 26-34, 37, 50, and 55-57 are rejected under 35 U.S.C. 103 as being unpatentable over Rollins et al. (WO 2018/083645 A1, in IDS filed 08/29/2022), in view of Shenoy et al. (WO 2018/211517 A1, in IDS filed 08/29/2022), and Eakin et al. 2014 (in instant PTO-892).
Rollins discloses “an anti-P-selectin antibody or binding fragment thereof, for use according to any one of the claims 1 to 9, wherein the antibody or binding fragment thereof is provided to the subject in a loading dose of between 2.5 mg/kg to 7.5 mg/kg, or preferably 2.5 mg/kg to 5 mg/kg”, see reference’s claim 10. Rollins also discloses that the “anti-P-selectin antibody or binding fragment thereof, preferably crizanlizumab or a binding fragment thereof, for use in the prevention of a sickle cell pain crisis”, see Brief Summary of Invention. The instant specification discloses “the present invention provides a pharmaceutical composition comprising crizanlizumab that has light chain and heavy chain amino acid sequences of SEQ ID NO: 10 and SEQ ID NO: 9”, see pg.2. Thus, the anti-P-selectin antibody referred to as “crizanlizumab” taught by Rollins is a match for instant SEQ ID NOs: 9 and 10. This meets the limitations of instant claims 1-3 wherein the antibody against human P-selectin is crizanlizumab.
However, Rollins does not disclose a formulation for the crizanlizumab antibody. Shenoy remedies this deficiency.
Shenoy describes a protein agent formulation comprising: (i) one or more protein agents with a molecular weight from about 120 kDa to about 250 kDa at a concentration between about 150 mg/mL to about 300 mg/mL or 10-2000 mg/ml of 50-1000 mg/ml (see claim 11), (ii) phosphate buffer at a concentration between about 15 mM to about 50 mM., (iii) one or more viscosity-reducing agent(s) that comprises a combination of nicotinic acid (acid form) and tryptophan, present at a concentration between 5 mM and 100 mM each and tonicity modifiers which include sucrose, mannitol and/or sodium chloride (10-1000 mM, see paragraph [250]). Crizanlizumab is one of the possible protein agents.
Shenoy also discloses that “formulation has a pH between about 4.0 and 8.0” depending on the buffer used, see claim 1. Shenoy also discloses the use of a “viscosity-reducing agent is or comprises one or more of sodium chloride, ammonium chloride, ammonium acetate, ammonium sulphate, calcium chloride, sodium thiocyanate, and combinations thereof” and a “viscosity-reducing agent is or comprises one or more of polysorbate 80 [or] polysorbate 20”, see paragraphs [0193-0194]. Shenoy also teaches that “the composition herein may be in either aqueous or lyophilized form”, see paragraph [0147].
This meets the limitations of instant claim 7 wherein the pH is anywhere from 5.5 to 7.5, instant claim 10 wherein the buffer is a phosphate buffer, instant claims 12 and 13 wherein the formulation contains a stabilizer that is sucrose in the claimed concentrations, instant claims 16 and 32-34 wherein the isotonizing agent is sodium chloride in the claimed concentration, instant claims 19 and 29-31 wherein the surfactant is polysorbate 80 in the claimed concentration, instant claims 22 and 23 wherein the concentration of crizanlizumab is 5 mg/ml to 50 mg/ml, instant claims 26-28 wherein the stabilizer is sucrose at the claimed concentration, instant claim 34 wherein the composition can be packaged into a lyophilized form, and instant claims 50 and 57 wherein the formulation with crizanlizumab is used in a method of treating pain associated with sickle cell disease.
Rollins and Shenoy do not teach the occurrence of a charge variant referred to as “iso-crizanlizumab”. Eakin et al. remedies this deficiency.
Eakin et al. teaches that “a ubiquitous post-translational modification observed in proteins is isomerization of aspartic acid to isoaspartic acid (isoAsp). This non-enzymatic post-translational modification occurs spontaneously in proteins and plays a role in aging, autoimmune response, cancer, neurodegeneration, and other diseases”, see Abstract. Eakin et al. also teaches that “although parameters including temperature and pH have been investigated and shown Asp isomerization increases in mildly acidic buffers, these buffers are the favored formulation for antibodies because other modifications including aggregation, oxidation and deamidation tend to be minimized at pH 4-6”, see Introduction. This meets the limitations of instant claim 6 wherein the charge variants spontaneously arise after storage in solution.
It would be obvious at the time of the instant invention to use the antibody in formulation taught by Rollins and Shenoy, which is a human anti-P-selectin antibody in a formulation that results in the treatment of pain associated with sickle cell disease, with the teachings of Eakin et al. which shows the spontaneous modification of aspartic acid in antibodies to iso-aspartic acid in acidic conditions. One would be motivated to combine the antibody with the formulation with the expectation of creating charge variants of the crizanlizumab antibody as it is placed in the same formulation as claimed.
Therefore, claims are rejected as obvious over Rollins, Shenoy, and Eakin.
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 1-3, 6-7, 10, 12-13, 16, 19, 22-23, 26-34, 37, 50, and 55-57 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-10 of U.S. Patent No. 9,556,266 B2, hereinafter ‘266, in view of Shenoy et al. (WO 2018/211517 A1, in IDS filed 08/29/2022), and Eakin et al. 2014 (in instant PTO-892). Although the claims at issue are not identical, they are not patentably distinct from each other because they both disclose the same antibody in a method of treating sickle cell disease.
‘266 recites a method of treating sickle cell disease in a subject comprising administering a humanized antibody, or binding fragment thereof, comprising a light chain variable region having CDR1, CDR2, and CDR3 of SEQ ID NOs: 1, 2, and 3, respectively, and a heavy chain variable region having CDR1, CDR2, and CDR3 of SEQ ID NOs: 4, 5, and 6, respectively, and wherein the humanized antibody has binding specificity for P-selectin (issued claims 1-4). Further, the humanized antibody can be administered by subcutaneous, intramuscular, or intravenous injection (issued claim 5) and at multiple administrations to the subject (issued claim 10). These CDRs are drawn to the antibody “crizanlizumab”, which is taught in the instant claims.
‘266 does not specifically recite the formulation in which the antibody is comprised in. Shenoy remedies this deficiency.
Shenoy describes a protein agent formulation comprising: (i) one or more protein agents with a molecular weight from about 120 kDa to about 250 kDa at a concentration between about 150 mg/mL to about 300 mg/mL or 10-2000 mg/ml of 50-1000 mg/ml (see claim 11), (ii) phosphate buffer at a concentration between about 15 mM to about 50 mM., (iii) one or more viscosity-reducing agent(s) that comprises a combination of nicotinic acid (acid form) and tryptophan, present at a concentration between 5 mM and 100 mM each and tonicity modifiers which include sucrose, mannitol and/or sodium chloride (10-1000 mM, see paragraph [250]). Crizanlizumab is one of the possible protein agents.
Shenoy also discloses that “formulation has a pH between about 4.0 and 8.0” depending on the buffer used, see claim 1. Shenoy also discloses the use of a “viscosity-reducing agent is or comprises one or more of sodium chloride, ammonium chloride, ammonium acetate, ammonium sulphate, calcium chloride, sodium thiocyanate, and combinations thereof” and a “viscosity-reducing agent is or comprises one or more of polysorbate 80 [or] polysorbate 20”, see paragraphs [0193-0194]. Shenoy also teaches that “the composition herein may be in either aqueous or lyophilized form”, see paragraph [0147].
This meets the limitations of instant claim 7 wherein the pH is anywhere from 5.5 to 7.5, instant claim 10 wherein the buffer is a phosphate buffer, instant claims 12 and 13 wherein the formulation contains a stabilizer that is sucrose in the claimed concentrations, instant claims 16 and 32-34 wherein the isotonizing agent is sodium chloride in the claimed concentration, instant claims 19 and 29-31 wherein the surfactant is polysorbate 80 in the claimed concentration, instant claims 22 and 23 wherein the concentration of crizanlizumab is 5 mg/ml to 50 mg/ml, instant claims 26-28 wherein the stabilizer is sucrose at the claimed concentration, instant claim 34 wherein the composition can be packaged into a lyophilized form, and instant claims 50 and 57 wherein the formulation with crizanlizumab is used in a method of treating pain associated with sickle cell disease.
‘266 and Shenoy do not teach the occurrence of a charge variant referred to as “iso-crizanlizumab”. Eakin et al. remedies this deficiency.
Eakin et al. teaches that “a ubiquitous post-translational modification observed in proteins is isomerization of aspartic acid to isoaspartic acid (isoAsp). This non-enzymatic post-translational modification occurs spontaneously in proteins and plays a role in aging, autoimmune response, cancer, neurodegeneration, and other diseases”, see Abstract. Eakin et al. also teaches that “although parameters including temperature and pH have been investigated and shown Asp isomerization increases in mildly acidic buffers, these buffers are the favored formulation for antibodies because other modifications including aggregation, oxidation and deamidation tend to be minimized at pH 4-6”, see Introduction. This meets the limitations of instant claim 6 wherein the charge variants spontaneously arise after storage in solution.
It would be obvious at the time of the instant invention to use the antibody in formulation taught by ‘266 and Shenoy, which is a human anti-P-selectin antibody known as “crizanlizumab” in a formulation that results in the treatment of pain associated with sickle cell disease, with the teachings of Eakin et al. which shows the spontaneous modification of aspartic acid in antibodies to iso-aspartic acid in acidic conditions. One would be motivated to combine the antibody with the formulation with the expectation of creating charge variants of the crizanlizumab antibody as it is placed in the same formulation as claimed.
Claims 1-3, 6-7, 10, 12-13, 16, 19, 22-23, 26-34, 37, 50, and 55-57 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-7 of U.S. Patent No. 8377440B2, hereinafter ‘440, in view of in view of Shenoy et al. (WO 2018/211517 A1, in IDS filed 08/29/2022), and Eakin et al. 2014 (in instant PTO-892). Although the claims at issue are not identical, they are not patentably distinct from each other because they both disclose the same antibody in a method of treating sickle cell disease.
‘440 recites a humanized antibody, or binding fragment thereof, comprising an immunoglobulin light chain variable region comprising SEQ ID NO: 36, and an immunoglobulin heavy chain variable region comprising SEQ ID NO: 40, and wherein the humanized antibody has binding specificity for P-selectin (issued claim 1). The VL and VH chains of SEQ ID NOs: 36 and 40 correspond to that of crizanlizumab, which is taught in the instant claims.
‘440 does not specifically recite the formulation in which the antibody is comprised in. Shenoy remedies this deficiency.
Shenoy describes a protein agent formulation comprising: (i) one or more protein agents with a molecular weight from about 120 kDa to about 250 kDa at a concentration between about 150 mg/mL to about 300 mg/mL or 10-2000 mg/ml of 50-1000 mg/ml (see claim 11), (ii) phosphate buffer at a concentration between about 15 mM to about 50 mM., (iii) one or more viscosity-reducing agent(s) that comprises a combination of nicotinic acid (acid form) and tryptophan, present at a concentration between 5 mM and 100 mM each and tonicity modifiers which include sucrose, mannitol and/or sodium chloride (10-1000 mM, see paragraph [250]). Crizanlizumab is one of the possible protein agents.
Shenoy also discloses that “formulation has a pH between about 4.0 and 8.0” depending on the buffer used, see claim 1. Shenoy also discloses the use of a “viscosity-reducing agent is or comprises one or more of sodium chloride, ammonium chloride, ammonium acetate, ammonium sulphate, calcium chloride, sodium thiocyanate, and combinations thereof” and a “viscosity-reducing agent is or comprises one or more of polysorbate 80 [or] polysorbate 20”, see paragraphs [0193-0194]. Shenoy also teaches that “the composition herein may be in either aqueous or lyophilized form”, see paragraph [0147].
This meets the limitations of instant claim 7 wherein the pH is anywhere from 5.5 to 7.5, instant claim 10 wherein the buffer is a phosphate buffer, instant claims 12 and 13 wherein the formulation contains a stabilizer that is sucrose in the claimed concentrations, instant claims 16 and 32-34 wherein the isotonizing agent is sodium chloride in the claimed concentration, instant claims 19 and 29-31 wherein the surfactant is polysorbate 80 in the claimed concentration, instant claims 22 and 23 wherein the concentration of crizanlizumab is 5 mg/ml to 50 mg/ml, instant claims 26-28 wherein the stabilizer is sucrose at the claimed concentration, instant claim 34 wherein the composition can be packaged into a lyophilized form, and instant claims 50 and 57 wherein the formulation with crizanlizumab is used in a method of treating pain associated with sickle cell disease.
‘440 and Shenoy do not teach the occurrence of a charge variant referred to as “iso-crizanlizumab”. Eakin et al. remedies this deficiency.
Eakin et al. teaches that “a ubiquitous post-translational modification observed in proteins is isomerization of aspartic acid to isoaspartic acid (isoAsp). This non-enzymatic post-translational modification occurs spontaneously in proteins and plays a role in aging, autoimmune response, cancer, neurodegeneration, and other diseases”, see Abstract. Eakin et al. also teaches that “although parameters including temperature and pH have been investigated and shown Asp isomerization increases in mildly acidic buffers, these buffers are the favored formulation for antibodies because other modifications including aggregation, oxidation and deamidation tend to be minimized at pH 4-6”, see Introduction. This meets the limitations of instant claim 6 wherein the charge variants spontaneously arise after storage in solution.
It would be obvious at the time of the instant invention to use the antibody in formulation taught by ‘440 and Shenoy, which is a human anti-P-selectin antibody known as “crizanlizumab” in a formulation that results in the treatment of pain associated with sickle cell disease, with the teachings of Eakin et al. which shows the spontaneous modification of aspartic acid in antibodies to iso-aspartic acid in acidic conditions. One would be motivated to combine the antibody with the formulation with the expectation of creating charge variants of the crizanlizumab antibody as it is placed in the same formulation as claimed.
Claims 1-3, 6-7, 10, 12-13, 16, 19, 22-23, 26-34, 37, 50, and 55-57 are provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claim 19 of copending Application No.18/516,831, hereinafter ‘831, in view of in view of Shenoy et al. (WO 2018/211517 A1, in IDS filed 08/29/2022), and Eakin et al. 2014 (in instant PTO-892). Although the claims at issue are not identical, they are not patentably distinct from each other because they both disclose the same antibody in a method of treating sickle cell disease.
‘831’s claims recite a method of reducing the frequency of sickle cell pain crisis comprising administering crizanlizumab or a binding fragment thereof, wherein the antibody is first provided in a loading phase, during which a subject receives two loading doses of crizanlizumab or a binding fragment thereof at an amount of 5 mg/kg and wherein the time interval between the two loading doses is 2 weeks (+/-3 days), and then further provided in a maintenance phase, during which the subject receives a plurality of maintenance doses of the antibody at an amount of 5 mg/kg and wherein the time interval between the plurality of maintenance doses is 4 weeks (+/-3 days).
‘831’s claims do not teach the formulation in which the antibody is comprised in. Shenoy remedies this deficiency.
Shenoy describes a protein agent formulation comprising: (i) one or more protein agents with a molecular weight from about 120 kDa to about 250 kDa at a concentration between about 150 mg/mL to about 300 mg/mL or 10-2000 mg/ml of 50-1000 mg/ml (see claim 11), (ii) phosphate buffer at a concentration between about 15 mM to about 50 mM., (iii) one or more viscosity-reducing agent(s) that comprises a combination of nicotinic acid (acid form) and tryptophan, present at a concentration between 5 mM and 100 mM each and tonicity modifiers which include sucrose, mannitol and/or sodium chloride (10-1000 mM, see paragraph [250]). Crizanlizumab is one of the possible protein agents.
Shenoy also discloses that “formulation has a pH between about 4.0 and 8.0” depending on the buffer used, see claim 1. Shenoy also discloses the use of a “viscosity-reducing agent is or comprises one or more of sodium chloride, ammonium chloride, ammonium acetate, ammonium sulphate, calcium chloride, sodium thiocyanate, and combinations thereof” and a “viscosity-reducing agent is or comprises one or more of polysorbate 80 [or] polysorbate 20”, see paragraphs [0193-0194]. Shenoy also teaches that “the composition herein may be in either aqueous or lyophilized form”, see paragraph [0147].
This meets the limitations of instant claim 7 wherein the pH is anywhere from 5.5 to 7.5, instant claim 10 wherein the buffer is a phosphate buffer, instant claims 12 and 13 wherein the formulation contains a stabilizer that is sucrose in the claimed concentrations, instant claims 16 and 32-34 wherein the isotonizing agent is sodium chloride in the claimed concentration, instant claims 19 and 29-31 wherein the surfactant is polysorbate 80 in the claimed concentration, instant claims 22 and 23 wherein the concentration of crizanlizumab is 5 mg/ml to 50 mg/ml, instant claims 26-28 wherein the stabilizer is sucrose at the claimed concentration, instant claim 34 wherein the composition can be packaged into a lyophilized form, and instant claims 50 and 57 wherein the formulation with crizanlizumab is used in a method of treating pain associated with sickle cell disease.
‘831 and Shenoy do not teach the occurrence of a charge variant referred to as “iso-crizanlizumab”. Eakin et al. remedies this deficiency.
Eakin et al. teaches that “a ubiquitous post-translational modification observed in proteins is isomerization of aspartic acid to isoaspartic acid (isoAsp). This non-enzymatic post-translational modification occurs spontaneously in proteins and plays a role in aging, autoimmune response, cancer, neurodegeneration, and other diseases”, see Abstract. Eakin et al. also teaches that “although parameters including temperature and pH have been investigated and shown Asp isomerization increases in mildly acidic buffers, these buffers are the favored formulation for antibodies because other modifications including aggregation, oxidation and deamidation tend to be minimized at pH 4-6”, see Introduction. This meets the limitations of instant claim 6 wherein the charge variants spontaneously arise after storage in solution.
It would be obvious at the time of the instant invention to use the antibody in formulation taught by ‘831 and Shenoy, which is a human anti-P-selectin antibody known as “crizanlizumab” in a formulation that results in the treatment of pain associated with sickle cell disease, with the teachings of Eakin et al. which shows the spontaneous modification of aspartic acid in antibodies to iso-aspartic acid in acidic conditions. One would be motivated to combine the antibody with the formulation with the expectation of creating charge variants of the crizanlizumab antibody as it is placed in the same formulation as claimed.
This is a provisional nonstatutory double patenting rejection.
Conclusion
No claims are allowed.
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/SELAM BERHANE/Examiner, Art Unit 1675
/AURORA M FONTAINHAS/Primary Examiner, Art Unit 1675
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