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 .
In the event the determination of the status of the application as subject to AIA 35 U.S.C. 102 and 103 (or as subject to pre-AIA 35 U.S.C. 102 and 103) is incorrect, any correction of the statutory basis (i.e., changing from AIA to pre-AIA ) for the rejection will not be considered a new ground of rejection if the prior art relied upon, and the rationale supporting the rejection, would be the same under either status.
Examiner Change
The examiner of your application in the USPTO has changed. To aid in correlating any papers for this application, all further correspondence regarding this application should be directed to Examiner Omar Ramadan, Art Unit 1678.
Election/Restrictions
Applicant’s election without traverse of species I-VI in the reply filed on 12/17/2025 is acknowledged. Briefly the Applicant elected the following species: Species I of a cell lysate, species II of beads, species III of GFP, species IV of the protein of SEQ ID No. 71, species V of the protein of SEQ ID 71. And species VI of the second sample being an immune library and the polypeptide binder being an immune single variable domain (ISVD). Claims are not subject to a restriction requirement. The Applicant cancelled claims 15-17.
Thus, claims 1-14 and 18-20 are pending and are under examination.
Priority
This application is the U.S. National Stage (371) application of PCT/EP2022/067256, filed on 06/23/2022, which claims priority to two Foreign Applications: EP21181405.8 filed on 06/24/2021 and EP21181272.2 filed on 06/23/2021.
Receipt is acknowledged of certified copies of papers required by 37 CFR 1.55.
Information Disclosure Statement
The information disclosure statement (IDS) submitted on 12/19/2023 has been received. The submission is in compliance with the provisions of 37 CFR 1.97. Accordingly, the information disclosure statement is being considered by the examiner and all references are considered except where they were lined through.
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 8 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.
Regarding claim 8, the claim recites the limitation “magnetic” in parenthesis “()” as “ wherein the surface comprises (magnetic) beads”. It is not clear if the beads need to be magnetic or not because the presence of parenthesis in this case does not tell a skilled artisan if “magnetic” is a required limitation or not. A skilled artisan would not have been able to determine the scope of the claim from its language, and thus claim 8 is rendered indefinite.
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.
(a)(2) the claimed invention was described in a patent issued under section 151, or in an application for patent published or deemed published under section 122(b), in which the patent or application, as the case may be, names another inventor and was effectively filed before the effective filing date of the claimed invention.
Claims 1-4, 7-9, 11-14, and 18-20 are rejected under 35 U.S.C. 102(a)(1) and (a)(2) as being anticipated by Steyaert et al. (US 2024/0027467 A1, priority to 12/20/2019).
Regarding claim 1, Steyaert teaches a method of isolating a polypeptide binder ([0164]; [0194]; [0296], [0298]).
Steyaert teaches mixing a first protein binding agent that is immobilized on a surface and specifically binds a target protein with a first sample comprising the target protein ([0296], [0298]; [0345]; [0351]).
Steyaert teaches to obtain an immobilized complex of the first protein binding agent and the target protein on the surface ([0007], “In Nanobody-exchange chromatography (shortened herein
as NANEX), the protein of interest or target protein is captured by a first (immobilized) Nanobody, called Nanotrapper or trapper”).
Steyaert teaches providing to the immobilized complex of the first binding agent and the target protein a second sample that comprises a plurality of polypeptide binders to create a mixture ([0296, [0298]]).
Steyaert teaches adding to the mixture of the immobilized complex of the first binding agent, the target protein and plurality of polypeptide binders a third sample comprising a second protein binding agent ([0301]).
Steyaert teaches the second protein binding agent competes with the first binding agent for specifically binding to the target protein ([0010]).
Steyaert teaches that the specific binding the target protein by the second protein binding agent displaces the first binding agent from the target protein ([0010]).
Steyaert teaches eluting the second protein binding agent bound to the target protein so as to isolate a polypeptide binder bound to the target protein ([0011]).
Regarding claim 2, Steyaert teaches that the rate constant of dissociation (k0ff value) of the second protein binding agent is lower or equal as compared to the k0ff value of the first binding agent ([0002]).
Regarding claim 3, Steyaert teaches that the second and/or first protein binding agent comprises an antigen-binding domain ([0007], “The purification method allows to displace competing binders for a protein of interest, and is based on the finding that when using a Nanobody, or by extension an immunoglobulin single variable domain (ISVD) antigen-binding domain, as
a displacer the displacement kinetics is different as compared to what is expected for conventional antibody antigen-binding domains”).
Regarding claim 4, Steyaert teaches that the antigen-binding domain comprises an immunoglobulin single variable domain (ISVD) comprising an ISVD fused to a scaffold protein via at least two sites ([0019]; page 72, claim 7).
Regarding claim 7, Steyaert teaches that after eluting the second protein binding agent bound to the target protein so as to isolate a polypeptide binder bound to the target protein (step d of claim 1), the steps of claim 1 (a to d) are repeated at least once to enrich the number of polypeptide binders eluting in step d of claim 1 ([0156]).
Regarding claim 8, Steyaert teaches that the surface comprises magnetic beads ([0154], page 34, Example 27, “High-Throughput Nanobody Exchange Chromatography (NANEX) Purification of Diverse GFP-Tagged Fusion Proteins from Yeast (S. cerevisae) Cell Lysates Using Nb CA15816 as an Immobilized Trapper on Magnetic, Tosyl-Activated Dynabeads®, and Nb CA12760 as a Stripper”).
Regarding claim 9, Steyaert teaches that the first sample comprising the target protein in step a of claim 1 comprises a complex mixture ([0353]).
Regarding claim 11, Steyaert teaches that the first and/or second protein binding agent specifically binds to a heterologous tag present on the target protein ([0354]).
Regarding claim 12, Steyaert teaches that the tag on the target protein is GFP ([0354]).
Steyaert teaches that the first protein binding agent comprises the CDRs of SEQ ID No: 71 ([0299]; [0312], “SEQ ID No: 3”, “CA15816”). SEQ ID No: 71 of the instant application conforms to CA15816 GFP-trapper (Specification, page 58 of 60, line 32, “SEQ ID NO:71: CA15816 GFP-trapper …”; See sequence alignment of Seq ID No. 3 of Steyaert et al. to Seq ID No. 71 of the instant application).
CLUSTAL O(1.2.4) multiple sequence alignment
SEQID71 QVQLVESGGGLVQAGGSLRLSCAASGRTFSTAAMGWFRQAPGKERDFVAGIYWAAGSTYY 60
SEQID3 QVQLVESGGGLVQAGGSLRLSCAASGRTFSTAAMGWFRQAPGKERDFVAGIYWAAGSTYY 60
************************************************************
SEQID71 ADSAKGRFTISRDNAKNTVYLQMDSLKPEDTAVYYCAARRRGFTLAPTRANEYDYWGQGT 120
SEQID3 ADSAKGRFTISRDNAKNTVYLQMDSLKPEDTAVYYCAARRRGFTLAPTRANEYDYWGQGT 120
************************************************************
SEQID71 QVTVSS---------- 126
SEQID3 QVTVSSHHHHHHEPEA 136
******
Regarding claim 13, Steyaert teaches that the target protein immobilized on the surface is a protein complex comprising at least one or more additional proteins (Page 19, [0176], “Furthermore, said complex comprising the target protein of interest and the displacer, may also contain further proteins bound to said target protein, as part of a protein-protein complex that is isolated from the sample through NANEX purification.”).
Regarding claim 14, Steyaert teaches that step a) and b) of claim 1 are replaced by two steps as an example of the embodiments ([0298]).
Steyaert teaches mixing a target protein sample with a sample comprising a plurality of polypeptide binders to obtain a mixture ([0298]).
Steyaert teaches obtaining an immobilized complex on a surface by adding the mixture of a target protein with a plurality of polypeptide binders to a first protein binding agent, which is preferably immobilized on a surface or subsequently immobilized ([0298]).
Regarding claim 18, Steyaert teaches that the scaffold protein domain comprises HopQ or YgjK ([0172]).
Regarding claim 19, Steyaert teaches that the steps of claim 1 are repeated at least twice to enrich the number of polypeptide binders eluting in step d of claim 1 (([0156])). Steyaert teaches that depending on the nature of the sample, and the amount of target protein present in the sample, as well as on the first protein binding agent following step a) or b) of the method of the present invention, the elution in step c) using the second protein binding agent may be repeated ([0156]).
Regarding claim 20, Steyaert teaches that the complex mixture of claim 9 is a cell lysate ([0154], page 34, Example 27).
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 (PHOSITA) to which the claimed invention pertains. Patentability shall not be negated by the manner in which the invention was made.
The factual inquiries for establishing a background for determining obviousness under 35 U.S.C. 103 are summarized as follows:
1. Determining the scope and contents of the prior art.
2. Ascertaining the differences between the prior art and the claims at issue.
3. Resolving the level of ordinary skill in the pertinent art.
4. Considering objective evidence present in the application indicating obviousness or nonobviousness.
Claims 5-6 and 10 are rejected under 35 U.S.C. 103 as being unpatentable over Steyaert et al. (US 2024/0027467 A1, priority to 12/20/2019) as applied to claim 1 above, and further in view of Kabir et al. (BMC Biotechnology 2009, 9:99).
Regarding claims 5-6 and 10, Steyaert teaches or suggests all of the limitations of the claim, but fails to teach the following limitations.
Regarding claim 5, Steyaert does not teach that the second sample comprising a plurality of polypeptide binders comprises a display library of binding agents.
Regarding claim 6, Steyaert does not teach that the display library is an immune library.
Regarding claim 10, Steyaert does not teach that the complex mixture of claim 9 was applied as an immunogen for obtaining the plurality of polypeptide binders
Regarding claim 5, Kabir teaches that the second sample comprising a plurality of polypeptide binders comprises a display library of binding agents (Page 11 of 16; left column, “Previously,
we established a large mouse scFv phage display library (2.8 × 1010 CFU/ml), and we attempted to isolate antigen-specific scFvs by using nmAb-KT as a model antigen”).
Regarding claim 6, Kabir teaches that the display library is an immune library (Page 11 of 16, left and right columns, “after proper selection of the library, phage-displaying anti-idiotypic scFv antibodies represented the internal image of the original antigen HM-1 and thus might be effective as a vaccine”).
Regarding claim 10, Kabir teaches that the complex mixture was applied as an immunogen for obtaining the plurality of polypeptide binders (Page 2 of 16, left column, second paragraph, “In this study, we investigated the de novo selection of DNA that encodes scFvs specific to the immunogen, HM-1 killer toxin (HM-1)-neutralizing monoclonal antibodies (nmAb-KT) from splenocytes of a hyper-immunized mouse”).
It would have been obvious for a PHOSITA before the effective filing date of the application to combine the immune display library of Kabir with the isolation method of Steyaert to isolate binding agents for therapeutic purposes because Kabir’s produced antibodies with superior binding properties and cytocidal activity as compared to other methods (Abstract, conclusion) and used immunogens to find the right antibody (Page 2 of 16, left column, second paragraph). A skilled artisan would have been motivated to combine the above methods to expediate the discovery of therapeutic antibodies. A PHOSITA would have had a reasonable expectation of success in combining the methods of Kabir and Steyaert because both are methods directed to isolating binding agents or antibodies.
It would have been obvious for a PHOSITA to screen for antibodies using the immune library of Kabir and the isolation method of Steyaert to isolate promising antibodies for therapeutic purposes.
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 1-14 and 18-20 are provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-2, 4-5, 7, 9-10, 14-15, 26 and 27 of copending Application No. 17/786,724 in view of Kabir et al. (BMC Biotechnology 2009, 9:99) and Abdiche et al. (PLoS One, 2017 Jan 6;12(1)).
This is a provisional nonstatutory double patenting rejection because the patentably indistinct claims have not in fact been patented.
Although the claims at issue are not identical, they are not patentably distinct from each other because:
Regarding claim 1 pertaining to a method of isolating a polypeptide binder, mixing a first protein binding agent that is immobilized on a surface and specifically binds a target protein with a first sample to specifically bind to a target protein in the sample to obtain an immobilized complex of the first protein binding agent and the target protein, providing to the immobilized complex of the first binding agent and the target protein a second sample that comprises a plurality of polypeptide binders to create a mixture, adding to the mixture of the immobilized complex of the first binding agent, the target protein and plurality of polypeptide binders a third sample comprising a second protein binding agent, competing the second protein binding agent with the first binding agent for specifically binding the second binding agent to the target protein, displacing the first binding agent from the target protein by the specific binding of the target protein by the second protein binding agent, and eluting the second protein binding agent bound to the target protein so as to isolate a polypeptide binder bound to the target protein; ‘724 teaches a method for the purification of a target protein by mixing the first protein binding agent with a sample containing the target protein, adding to the mix, a second protein binding agent that competes with the first binding gent for binding to the target protein to displace the first binding agent from the target protein and collecting the eluting second protein binding agent bound to the target protein (See claim 1 of ‘724).
Regarding claim 2 pertaining that the rate constant of dissociation (k0ff value) of the second protein binding agent is lower or equal as compared to the k0ff value of the first binding agent, ‘724 teaches that the rate constant of dissociation (koff value) of the second protein binding agent is lower or equal as compared to the koff value of the first binding agent (See claim 1 of ‘724).
Regarding claim 3 pertaining to that the second and/or first protein binding agent comprises an antigen-binding domain, ‘724 teaches that a second protein binding agent comprises an immunoglobulin single variable domain (ISVD) or a functional variant thereof specifically binding the target protein which competes with the first binding agent for binding to the target protein (See claim 1 of ‘724).
Regarding claim 4 pertaining to that the antigen-binding domain comprises an immunoglobulin single variable domain (ISVD) comprising an ISVD fused to a scaffold protein via at least two sites, ‘724 teaches the binding agents specifically bind a scaffold protein domain of the target protein comprising an antigen-binding chimeric protein, wherein the antigen-binding chimeric protein is an ISVD fused to a scaffold protein via at least two sites (See claim 7 of ‘724).
Regarding claim 7 pertaining to that after eluting the second protein binding agent bound to the target protein so as to isolate a polypeptide binder bound to the target protein (step d of claim 1), the steps of claim 1 (a to d) are repeated at least once to enrich the number of polypeptide binders eluting in step d of claim 1, ‘724 teaches repeating the steps of claims 1-15 using a 3rd and 4th protein binding agent instead of, or in addition to the 1st and 2nd protein binding agents (See claim 16 of ‘724).
Regarding claim 9 pertaining that the first sample comprising the target protein in step a of claim 1 comprises a complex mixture, ‘724 teaches that the sample of claim 1 is a biological
sample, a complex mixture, a cellular sample, or an in vitro sample (See claim 15 of ‘724).
Regarding claim 11 pertaining to that the first and/or second protein binding agent specifically binds to a heterologous tag present on the target protein, ‘724 teaches that the binding agents
specifically bind a tag on the target protein selected from the group consisting of GFP, mCherry, OST, SMT3, and EPEA (See claims 5 and 26 of ‘724).
Regarding claim 12 pertaining to that the tag of claim 11 is GFP, ‘724 teaches that the binding agents specifically bind a tag on the target protein selected from the group consisting of GFP, mCherry, OST, SMT3, and EPEA (See claims 5 and 26 of ‘724).
Regarding claim 18 pertaining to that the scaffold protein domain comprises HopQ or YgjK, ‘724 teaches that the scaffold protein domain comprises HopQ, Ygjk, or a derivative thereof (See claim 27 of ‘724).
Regarding claim 19 pertaining to that the steps of claim 1 are repeated at least twice to enrich the number of polypeptide binders eluting in step d of claim 1, ‘724 teaches repeating steps
a) to c) of the method of claims 1-15, using a 3rd and 4th protein binding agent instead of, or in
addition to the 1st and 2nd protein binding agents (See claim 16 of ‘724).
Regarding claim 20 pertaining to that the complex mixture is a biological sample, a cell lysate, or a proteome sample, ‘724 teaches that the sample is a biological sample, a complex mixture, a cellular sample, or an in vitro sample (See claim 15 of ‘724).
Regarding claim 1, ‘724 does not teach providing to the immobilized complex of the first binding agent and the target protein a second sample that comprises a plurality of polypeptide binders to create a mixture.
Regarding claim 5 pertaining to that the second sample comprising a plurality of polypeptide binders comprises a display library of binding agents, ‘724 does not teach that the second sample comprising a plurality of polypeptide binders comprises a display library of binding agents.
Regarding claim 6 pertaining to that the display library is an immune library, ‘724 does not teach that the display library is an immune library.
Regarding claim 8 pertaining to that the surface comprises (magnetic) beads, a resin, a column, a plate, or a chip, ‘724 does not teach a surface.
Regarding claim 10 pertaining that the complex mixture of claim 9 was applied as an immunogen for obtaining the plurality of polypeptide binders, ‘724 does not teach that the complex mixture of claim 9 was applied as an immunogen for obtaining the plurality of polypeptide binders.
Regarding claim 13 pertaining to that the target protein immobilized on the surface is a protein complex comprising at least one or more additional proteins, ‘724 does not teach that the target protein immobilized on the surface is a protein complex comprising at least one or more additional proteins.
Regarding claim 14 pertaining to step a) and b) of claim 1 are replaced by two steps as an example of the embodiments, mixing a target protein sample with a sample comprising a plurality of polypeptide binders to obtain a mixture, obtaining an immobilized complex on a surface by adding the mixture of a target protein with a plurality of polypeptide binders to a first protein binding agent, which is preferably immobilized on a surface or subsequently immobilized, ‘724 does not teach replacing steps step a) and b) of claim 1 as noted above.
Regarding claim 1, Kabir teaches providing an immobilized first binding agent (Figure I, “Antigen (nmAb-KT) immobilization & blocking”).
A skilled artisan would have been motivated to look for proteins that can bind to the target protein to identify a polypeptide binder or antibody as shown by Abdiche to form a transient sandwich complex (Fig 1. (B) “displace”, “TRANSIENT sandwich complex”) that can be displaced with a competing second binder as in ‘724 copending application (claim 1).
Regarding claim 5, Kabir teaches a sample comprising a plurality of polypeptide binders comprises a display library of binding agents (Page 11 of 16; left column, “Previously, we established a large mouse scFv phage display library (2.8 × 1010 CFU/ml), and we attempted to isolate antigen-specific scFvs by using nmAb-KT as a model antigen”).
Regarding claim 6, Kabir teaches that the display library is an immune library (Page 11 of 16, left and right columns, “after proper selection of the library, phage-displaying anti-idiotypic scFv antibodies represented the internal image of the original antigen HM-1 and thus might be effective as a vaccine”).
Regarding claim 8, Kabir teaches the surface comprises CM5 sensor chip (Page 11 of 16, Table 4, Ligand nmAb-KT was immobilized on the surface of a CM5 sensor chip).
Regarding claim 10, Kabir teaches that the complex mixture was applied as an immunogen for obtaining the plurality of polypeptide binders (Page 2 of 16, left column, second paragraph, “In this study, we investigated the de novo selection of DNA that encodes scFvs specific to the immunogen, HM-1 killer toxin (HM-1)-neutralizing monoclonal antibodies (nmAb-KT) from splenocytes of a hyper-immunized mouse”).
Regarding claim 13, ‘724 teaches that the sample is a complex mixture (See claim 15 of ‘724). A skilled artisan would have known that a complex mixture is made of different components including different proteins.
Regarding claim 14, a skilled artisan would have known that a variation of either binding the target protein before or after immobilization to a polypeptide binder is possible according to the experimental needs.
It would have been obvious to one of ordinary skill in the art before the filing date of the application to combine phage immune library of Kabir with the detection method of ‘624 because Kabir produced antibodies with superior binding properties and cytocidal activity as compared to other methods (Abstract, conclusion) and used immunogens to find the right antibody (Page 2 of 16, left column, second paragraph). The ordinary artisan would have been motivated to combine the displacement method with combined method of Kabir and ‘624 because Abdiche taught that the target protein is displaced with the binding antibody in a gentle and efficient way so that it can be used in designing therapeutic antibodies (Abstract). Therefore, such combinations would be considered an advantageous additives to ‘624 which also recognizes a need for improving the detection and purification of proteins.
Conclusion
No claims are allowed.
Any inquiry concerning this communication or earlier communications from the examiner should be directed to OMAR RAMADAN whose telephone number is (571)270-0754. The examiner can normally be reached Monday-Friday 8:30 am - 5:00 pm.
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/OMAR RAMADAN/Examiner, Art Unit 1678
/GREGORY S EMCH/Supervisory Patent Examiner, Art Unit 1678