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 .
Applicant's amendment and remarks, filed 4/14/26, are acknowledged.
Claims 1-4, 6, 10-19 and 21-31 have been cancelled.
Claims 32-50 have been added and are pending.
Claims 46-50 are withdrawn from further consideration by the examiner, 37 CFR 1.142(b), as being drawn to a non-elected invention. It is noted that Applicant previously elected SEQ ID NO: 20 as the species of CAR construct from those recited in previous claim 20 (which corresponds to new claim 32). In the last office action, a CD20 binding domain comprising SEQ ID NO: 17-18 was rejoined (SEQ ID NO: 17-18 are present in the CAR construct of SEQ ID NO; 16 of the instant claims). Therefore, SEQ ID NO; 16 and 20 are under examination and claims 38-39 are withdrawn as being directed to non-elected species.
Claims 32-37 and 40-45 are being acted upon.
In view of Applicant’s cancellation of the previously pending claims, the rejections from the previous office action are withdrawn.
The following are new grounds of rejection necessitated by Applicant’s claim amendments.
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 32-35, 40-45 is/are rejected under 35 U.S.C. 103 as being unpatentable over WO 2015/187528 (of record), in view of US 2018/0162939, US 2016/0362472 (of record), and US 2015/0197771 (of record).
WO 2015/187528 teaches a CD19 CAR that has a signal peptide, CD19scFV, CD8 hinge/transmembrane domain, CD28 signaling domain and a CD3zeta signal domain (see SEQ ID NO: 1) that is 100% identical to residues 1-502 of SEQ ID NO: 16 of the instant claims (see attached alignment). WO 2015/187528 teaches nucleic acids encoding said CAR for expression in CAR T cells (i.e. host cells) and that it is useful for targeting malignant B cells in a pharmaceutical composition.
The reference differs from the claimed invention in that it does not explicitly teach that the nucleic acids further encode a cleavage site a second CAR comprising a CD20 CAR sequence, i.e. residues 503-1034 of SEQ ID NO: 16).
The ‘939 publication teaches engineering T cells to express two distinct CAR constructs, each having a signal peptide, antigen recognition domain, hinge/transmembrane domain, and intracellular signaling domain, wherein the hinge/transmembrane domain and signal peptide and intracellular domains can be the same, but wherein the antigen binding domains are different (See paragraphs 309, in particular). The ‘939 publication teaches that doing so is advantageous since it allows a single engineered cell to target multiple antigens, thus reducing tumor recurrence (See paragraph 314, in particular). The ‘939 publication teaches that the first CAR can bind to CD19 and the second CAR can bind to CD20, and teaches an exemplary construct in SEQ ID NO: 3 (see paragraph 322, in particular). The ‘939 publication teaches that each CAR includes CD3 zeta, but that it is advantageous to use different co-stimulatory domains in the two CAR to avoid interaction, for example one CAR having CD28 and one CAR having 4-1BB signaling domain (see paragraph 338, in particular). The ‘939 publication teaches that CAR constructs consist of modular units and that the two different CAR can be linked by a cleaving peptide such as P2A, F2A, or others, for dual expression (see paragraph 27, 437, and 592, and in particular). The ‘939 publication teaches a particular signal peptide-CD20 scFV antigen binding domain for use in said dual CAR constructs, shown in residues 510-772 of SEQ ID NO: 3, which is 100% identical to the CD20 scFV present as residues 535-597 of SEQ ID NO: 16. The ‘939 publication also teaches a 4-1BB intracellular domain identical to the 4-1BB signaling domain of the instant application (see residues 333-374 of SEQ ID NO: 3).
Similarly, the ‘472 publication teaches a nucleic acid encoding i) first CAR that binds to CD19, and ii) a second CAR that binds to CD20, wherein a nucleic acid sequence encoding a protease cleavage site, such as F2A, is situated between the nucleic acid sequences encoding i) and ii) such that a cell can express a fusion protein comprising i) and ii), which protein is subsequently separated into two polypeptides by proteolytic cleavage (i.e. one or more polypeptides encoded by said nucleic acid, see paragraph 63, and page 10, in particular). The ‘472 publication teaches said nucleic acid in a vector, and an immune effector T cell comprising said vector, wherein the cells express the encoded proteins (See page 7, in particular). The ‘472 publication also teaches that in some embodiments, the CD19 CAR and CD20 CAR both comprise a CD3zeta signaling domain, but can comprise different costimulatory domains, i.e. the CD19 CAR comprises a CD28 signaling domain and the CD20 CAR comprise a 41BB signaling domain (See page 10, in particular). Thus, the ‘472 publication suggests a CD19/CD20 bicistronic CAR, wherein the elements can be arranged as follows: leader-CD19VLlinkerCD19VH-CD8hingetransm-CD28-CD3-F2A-leader-CD20VLlinkerCD20VH-CD8hingetransm-41BB-CD3. This is the same configuration as present in SEQ ID NO: 16 of the instant application. Moreover, the ‘472 publication teaches that the leader, CD28, CD3, 41BB sequences that are identical to those found in SEQ ID NO: 16 of the instant claims.
The ‘771 publication teaches an F2A cleavage peptide comprising SEQ ID NO: 35, which is identical to SEQ ID NO: 10 of the instant application. The ‘771 publication teaches that the F2A peptide can be used in an expression vector to encode a polypeptide that can be cleaved at the 2A peptide to generate separate polypeptides (see Table 3, page 9, 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 further include a nucleic acid sequence encoding a cleavable linker and CD20 CAR for co-expression, as taught by the ‘472 publication and the ‘939 publication. The ordinary artisan would be motivated to do so with a reasonable expectation of success, because the ‘939 publication teaches that it allows a single engineered cell to target multiple antigens, thus reducing tumor recurrence. For example, one could follow the guidance of the ‘939 publication which teaches that the two CAR constructs can be designed each having the same hinge/transmembrane domain and signal peptide, but wherein the antigen binding domains are different. Such as CD20 CAR construct could be produced recombinantly by starting with the CD19 CAR of WO 2015/187528 and swapping out the CD19 binding domain with the CD20 binding domain of the ‘939 publication. To achieve the advantageous different signaling for the second Car, one could also swap out the CD28 co-stimulatory region for the 4-1BB signaling domain taught in either the ‘939 or ‘472 publication. Doing so would result in second CD20 CAR polypeptide having 100% identity with residues 535-1034 of SEQ ID NO: 16 (see attached alignment, wherein the top sequence is SEQ ID NO: 16 of the instant application, and the bottom sequence represents the CD19 CAR of WO 2015/187528, with CD19 binding domain swapped for CD20 binding domain of the ‘939 publication, and CD28 costimulatory is swapped for 4-1BB of the ‘939 or ‘472 publication). All that is left is to account for residues 503-534 of SEQ ID NO: 16, which correspond to the peptide cleavage of SEQ ID NO: 35 of the ‘771 publication. Therefore, one could select from known peptide cleavage sites used for dual expression, such as SEQ ID NO: 35, and engineer the construct such that it is placed between the CD19 and CD20 CAR elements. Doing so would involve choosing among a finite number of predictable options which could be pursued with a reasonable expectation of success. A person of ordinary skill has good reason to pursue the known options within his or her technical grasp. If this leads to the anticipated success, it is likely the product not of innovation but of ordinary skill and common sense (see KSR International Co. V. Telefex Inc 82 USPQ2d 1385). These modifications above would result in a polypeptide 100% identical to SEQ ID NO: 16. Regarding the nucleic acid of SEQ ID NO: 15, selecting from known codons that could be used to produce the nucleotide sequence of SEQ ID NO: 16 would involve choosing among a finite number of predictable options.
Claim 32-33, 36-37, 40-45 is/are rejected under 35 U.S.C. 103 as being unpatentable over WO 2015/187528, in view of US 2016/0362472, US 20070014720 and US 2015/0197771 (all of record).
WO 2015/187528 teaches a CD19 CAR that has a signal peptide, CD19scFV, CD8 hinge/transmembrane domain, CD28 signaling domain and a CD3zeta signal domain (see SEQ ID NO: 1) that is 100% identical to residues 1-502 of SEQ ID NO: 16 of the instant claims (see attached alignment). WO 2015/187528 teaches nucleic acids encoding said CAR for expression in CAR T cells (i.e. host cells) and that it is useful for targeting malignant B cells in a pharmaceutical composition.
The reference differs from the claimed invention in that it does not explicitly teach that the nucleic acids further encode a cleavage site a second CAR comprising a CD20 CAR sequence, i.e. residues 503-1041 of SEQ ID NO: 20.
The ‘472 publication teaches a nucleic acid encoding i) first CAR that binds to CD19, and ii) a second CAR that binds to CD20, wherein a nucleic acid sequence encoding a protease cleavage site, such as F2A, is situated between the nucleic acid sequences encoding i) and ii) such that a cell can express a fusion protein comprising i) and ii), which protein is subsequently separated into two polypeptides by proteolytic cleavage (i.e. one or more polypeptides encoded by said nucleic acid, see paragraph 63, and page 10, in particular). The ‘472 publication teaches said nucleic acid in a vector, and an immune effector T cell comprising said vector, wherein the cells express the encoded proteins (See page 7, in particular). The ‘472 publication teaches a pharmaceutical composition of said immune effector cells (see pages 8-9 and paragraph 118, in particular). The ‘472 publication teaches that the CD19 CAR comprises an anti-CD19 scFV, a hinge and transmembrane domain, and an intracellular signaling domain (See pages 14-16, in particular). The ‘472 publication teaches that said scFV is in the form of leader sequence, light chain variable region-linker-heavy chain variable region (see page 16, in particular). The ‘472 publication teaches a leader sequence of SEQ ID NO: 13, which is identical to SEQ ID NO:3 of the instant application. The ‘472 publication teaches that the intracellular signaling domain comprises CD28 or 4-1BB costimulatory domain and a CD3 zeta sequence (see pages 14-16 and Fig 1, in particular). The ‘472 publication also teaches that in some embodiments, the CD19 CAR and CD20 CAR both comprise a CD3zeta signaling domain, but can comprise different costimulatory domains, i.e. the CD19 CAR comprises a CD28 signaling domain and the CD20 CAR comprise a 41BB signaling domain (See page 10, in particular).The ‘472 publication teaches a CD3 zeta of SEQ ID NO: 17, which is identical to Seq ID NO: 9 of the instant application, and a 4-1BB sequence of SEQ ID NO: 16, which is identical to SEQ ID NO: 14 of the instant application. The ‘472 publication teaches a CD28 sequence identical to SEQ ID NO: 8 of the instant application (see page 23, 129-130 and Fig. 1, SEQ ID NO: 1317, in particular). Likewise, the ‘472 publication teaches that the CD20 CAR can comprise a leader sequence, an scFV (i.e. VL, linker, VH), a hinge/transmembrane domain, and an intracellular signaling domain (See page 16, in particular). The ‘472 publication teaches that the VH/Vl of the CAR can be fully human (see paragraphs 391, 521, 598, 635, or 929, in particular). Thus, the ‘472 publication teaches a fully human CD19/CD20 bicistronic CAR, wherein the elements can be arranged as follows: leader-CD19VLlinkerCD19VH-CD8hingetransm-CD28-CD3-F2A-leader-CD20VLlinkerCD20VH-CD8hingetransm-41BB-CD3. This is the same configuration as present in SEQ ID NO: 20 of the instant application. Moreover, the ‘472 publication teaches that the leader, CD28, CD3, 41BB sequences that are identical to those found in SEQ ID NO: 20 of the instant claims. The ‘472 publication explains that it can be beneficial for the CAR antigen binding domain to be derived from the same species in which it will ultimately be used, for example, in humans it may be beneficial for the antigen binding domain to comprise human antibody fragments (See paragraph 636, in particular).. The ‘472 publication explains that CD19 antigen loss in B cell cancers is a problem that could result in relapse after treatment with CD19-CAR T cells, and that including a second CAR of a different antigen specificity can solve this problem and more effectively treat cancer (See paragraphs 1518-1523, in particular).
The ‘720 publication teaches anti-CD20 binding domains having a VH of SEQ ID NO: 46 and a VL of SEQ I DNO: 48, which are 100% identical to SEQ ID 21 and 22 of the instant application (i.e. a 2.1.2 CD20 binding domain). The ‘720 publication teaches that the binding domains can be in the form of an scFV and that the CD20 binding domains are fully human and can target CD20 malignant cells for immunotherapy (see page 1 and 11, in particular).
The ‘771 publication teaches an F2A cleavage peptide comprising SEQ ID NO: 35, which is identical to SEQ ID NO: 10 of the instant application. The ‘771 publication teaches that the F2A peptide can be used in an expression vector to encode a polypeptide that can be cleaved at the 2A peptide to generate separate polypeptides (see Table 3, page 9, 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 further include a nucleic acid sequence encoding a CD20 CAR with a cleavage site between CD19 and CD20 CAR elements for co-expression, following the guidance provided in the ‘472 publication. The ordinary artisan would be motivated to do so with a reasonable expectation of success, because the ‘472 publication teaches that it solves the problem of antigen escape and more effectively treats cancer.
For example, to produce the second CD20 CAR, one could start with the CD19 CAR construct of WO 2015/187528, and swap the CD19 VH and VL for the fully human CD20 VH and VL of the ‘720 publication. One would be motivated to do so to provide a second CAR to reduce antigen escape, and one would particularly motivated to select the VH and VL of the ‘720 publication, since the reference teaches it is fully human, and the ‘472 publication teaches the advantages of using fully human CAR in human subjects. One would also find it obvious to replace the CD28 co-stimulatory region of the CD20 CAR with the 4-1BB sequence of the ‘472 publication to provide the different costimulatory region of the CD20 CAR as taught by the ‘472 publication. This would result a polypeptide having 100% identity with residues 535-1041 of SEQ ID NO: 20. All that is left is to account for are residues 503-524, which correspond to the peptide cleavage site of SEQ ID NO: 35 of the ‘771 publication. One could select from known peptide cleavage sites used for dual expression, and selecting SEQ ID NO: 35 from the ‘771 publication, and engineering it between the CD19 and CD20 CAR elements would result in a sequence identical to SEQ ID NO: 20 of the instant application. Doing so would involve choosing among a finite number of predictable options which could be pursued with a reasonable expectation of success. A person of ordinary skill has good reason to pursue the known options within his or her technical grasp. If this leads to the anticipated success, it is likely the product not of innovation but of ordinary skill and common sense (see KSR International Co. V. Telefex Inc 82 USPQ2d 1385). Regarding the nucleic acid of SEQ ID NO: 19, selecting from known codons that could be used to produce the nucleotide sequence of SEQ ID NO: 20 would involve choosing among a finite number of predictable options.
Applicant’s arguments filed 4/14/26 have been fully considered, but they are not persuasive.
Applicant argues that the cited references could not have predicted the advantageous technical effects of the claimed CARs of the claimed SEQ ID Nos.
Applicant cites the data in Examples 4-16, demonstrating the ability of certain of the CARs of the instant claim (asserted to be those of SEQ I DNO: 16, 20, and 24) to kill tumor cells or treat tumors.
This is not persuasive, since the cited references teach that the bicistronic CAR are used for killing tumor cells and treating tumors. In other words, these are not unexpected properties. Furthermore, unexpected results must be commensurate in scope with the instant claims, and the instant claims encompass SEQ ID NO: 2 and 28.
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.
Claims 32-37, 40-45 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-9, 13 of U.S. Patent No. of 10,287,350, in view of US 2016/0362472, US 2015/0197771, and US 20070014720 and US 2018/0162939.
The ‘350 patent claims a nucleic acid sequence encoding a CAR off SEQ ID NO: 1, and a cell expressing a vector comprising said CAR, and the use of said cells to treat B cell malignancy in a subject (i.e. as pharmaceutical composition). Said SEQ ID NO: 1 is identical to the CD19 scFV CAR encoded by residues 1-502 of SEQ ID NO: 20 of the instant application. Although the ‘350 patent does not specifically claim a second CAR encoded from the same nucleic acid, it would be obvious to encode a second CD20 CAR using a bicistronic cleavage site as taught by the ‘472 publication to allow targeting of multiple different antigens. Furthermore arriving at SEQ ID NO: 20 is obvious based on the teachings of the ‘472 publication, the ‘720 publication, and the ‘771 publication for the same reasons set forth above. Likewise, arriving at SEQ ID NO: 16 is obvious based on the teachings of the ‘472 publication, the ‘771 publication, and the ‘939 publication, for the same reason set forth above.
Claims 32-37, 40-45 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-20 of U.S. Patent No. of 11,236,161, or claims 1-42 of 12,473,359, in view of US 2016/0362472, US 2015/0197771, US 20070014720 and US 2018/0162939.
The patents claim a nucleic acid sequence encoding a CD19 CAR of SEQ ID NO: 1. Said SEQ ID NO: 1 is identical to the CD19 scFv CAR encoded by residues 1-502 of SEQ ID NO: 20 of the instant application. Although the patents do not specifically claim a second CAR encoded from the vector, it would be obvious to encode a second CD20 CAR using a bicistronic cleavage site as taught by the ‘472 publication to allow targeting of multiple different B cell antigens. Furthermore arriving at SEQ ID NO: 20 and the other recited sequences is obvious based on the teachings of the ‘472 publication, the ‘720 publication, and the ‘771 publication for the same reasons set forth above. Likewise, arriving at SEQ ID NO: 16 is obvious based on the teachings of the ‘472 publication, the ‘771 publication, and the ‘939 publication, for the same reason set forth above.
Claims 32-37, 40-45 are provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-21 of copending Application No. 17/557,845, in view of US 2016/0362472, US 2015/0197771, US 20070014720 and US 2018/0162939.
The claims of the copending ‘845 application claims a CD19 CAR of SEQ ID NO: 1, nucleic acids and vectors encoding said CAR and methods of using said CAR. Said SEQ ID NO: 1 is identical to the CD19 scFV CAR encoded by residues 1-502 of SEQ ID NO: 20 of the instant application. Although the application does not specifically claim a second CAR encoded from the vector, it would be obvious to encode a second CD20 CAR using a bicistronic cleavage site as taught by the ‘472 publication to allow targeting of multiple different B cell antigens. Furthermore arriving at SEQ ID NO: 20 and the other recited sequences is obvious based on the teachings of the ‘472 publication, the ‘720 publication, and the ‘771 publication for the same reasons set forth above. Likewise, arriving at SEQ ID NO: 16 is obvious based on the teachings of the ‘472 publication, the ‘771 publication, and the ‘939 publication, for the same reason set forth above.
Claims 32-37, 40-45 are provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-32 of copending Application No. 18/282,919, in view of US 2016/0362472, US 2015/0197771, US 20070014720 and US 2018/0162939.
The ‘919 application claims a nucleic acid encoding a first CAR and a second CAR with a cleavage sequence position between the first and second CAR. The ‘919 application claims said nucleic acid sequence encodes SEQ ID NO: 71, which encodes a first CAR identical to that of the instant claim (i.e. having the same leader, CD19scFV, transmembrane/hinge, CD28 intracellular and CD3 zeta signaling domain sequences), and the identical CD20scFV, 4-1BB, and CD3 signaling domain sequences of the claim 20 of the instant claims. The only difference between SEQ ID NO: 71 of the ‘919 application and SEQ ID NO: 20 of the instant application is the leader sequence for the CD20 ScFV domain. However, as taught by the ‘472 publication, said leader sequence was known and selecting from known leader sequences for use in CAR constructs would involve choosing among a finite number of predictable options which could be pursued with a reasonable expectation of success. A person of ordinary skill has good reason to pursue the known options within his or her technical grasp. If this leads to the anticipated success, it is likely the product not of innovation but of ordinary skill and common sense (see KSR International Co. V. Telefex Inc 82 USPQ2d 1385). The ‘919 application further claims a vector and cells expressing the first and second CAR, as well as a pharmaceutical composition comprising said cells. Likewise, arriving at SEQ ID NO: 16 is obvious based on the teachings of the ‘472 publication, the ‘771 publication, and the ‘939 publication, for the same reason set forth above.
This is a provisional nonstatutory double patenting rejection.
No claim is allowed.
Applicant's amendment necessitated the new ground(s) of rejection presented in this Office action. Accordingly, THIS ACTION IS MADE FINAL. See MPEP § 706.07(a). 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 extension fee 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 date of this final action.
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
Prosecution Insights