`“x
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`
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`
`UNITED STATES PATENT AND TRADEMARK OFFICE
`
`UNITED STATES DEPARTMENT OF COMMERCE
`United States Patent and Trademark Office
`Address: COMIVHSSIONER FOR PATENTS
`PO. Box 1450
`Alexandria1 Virginia 22313-1450
`wwwusptogov
`
`
`
`
`
`14/042,656
`
`09/30/2013
`
`Yukari HATAOKA
`
`069804—0374
`
`9443
`
`20277
`7590
`0mm
`MCDERMOTT WILL&EMERY LLP —
`The McDermott Building
`HAQ, SHAFIQUL
`500 North Capitol Street, NW.
`WASHINGTON, DC 20001
`
`PAPER NUMBER
`
`1678
`
`NOTIFICATION DATE
`
`DELIVERY MODE
`
`08/24/2016
`
`ELECTRONIC
`
`Please find below and/0r attached an Office communication concerning this application or proceeding.
`
`The time period for reply, if any, is set in the attached communication.
`
`Notice of the Office communication was sent electronically on above—indicated "Notification Date" to the
`following e—mail address(es):
`
`ipdocketmwe @ mwe.com
`
`PTOL—90A (Rev. 04/07)
`
`

`

`
`Application No.
`Applicant(s)
`
` 14/042,656 HATAOKA, YUKARI
`Examiner
`Art Unit
`AIA (First Inventorto File)
`Office Action Summary
`
`1678SHAFIQUL HAQ if?“
`
`-- The MAILING DA TE of this communication appears on the cover sheet with the correspondence address --
`Period for Reply
`
`A SHORTENED STATUTORY PERIOD FOR REPLY IS SET TO EXPIRE 3 MONTHS FROM THE MAILING DATE OF
`THIS COMMUNICATION.
`Extensions of time may be available under the provisions of 37 CFR 1.136(a).
`after SIX (6) MONTHS from the mailing date of this communication.
`If NO period for reply is specified above, the maximum statutory period will apply and will expire SIX (6) MONTHS from the mailing date of this communication.
`Failure to reply within the set or extended period for reply will, by statute, cause the application to become ABANDONED (35 U.S.C. § 133).
`Any reply received by the Office later than three months after the mailing date of this communication, even if timely filed, may reduce any
`earned patent term adjustment. See 37 CFR 1.704(b).
`
`In no event, however, may a reply be timely filed
`
`-
`-
`
`Status
`
`1)IXI Responsive to communication(s) filed on 06/30/2016.
`[I A declaration(s)/affidavit(s) under 37 CFR 1.130(b) was/were filed on
`
`2b)lX| This action is non-final.
`2a)I:| This action is FINAL.
`3)I:I An election was made by the applicant in response to a restriction requirement set forth during the interview on
`
`
`; the restriction requirement and election have been incorporated into this action.
`
`4)|:I Since this application is in condition for allowance except for formal matters, prosecution as to the merits is
`closed in accordance with the practice under EX parte Quay/e, 1935 CD. 11, 453 O.G. 213.
`
`3) D Interview Summary (PT0_413)
`1) E Notice of References Cited (PTO-892)
`Paper No(s)/Mai| Date.
`.
`.
`—
`4) I:I Other'
`2) E Information Disclosure Statement(s) (PTO/SB/08a and/or PTO/SB/08b)
`
`Paper No(s)/Mai| Date .
`U.S. Patent and Trademark Office
`PTOL-326 (Rev. 11-13)
`
`Office Action Summary
`
`Part of Paper No./Mai| Date 20160817
`
`Disposition of Claims*
`5)|XI Claim(s) M is/are pending in the application.
`5a) Of the above claim(s) fl is/are withdrawn from consideration.
`6 III Claim s) _ is/are allowed.
`s E? is/are rejected.
`
`is/are objected to.
`
`) )
`
`_
`
`
`are subject to restriction and/or election requirement.
`9)|:l Claim(s
`)
`* If any claims have been determined allowable, you may be eligible to benefit from the Patent Prosecution Highway program at a
`
`participating intellectual property office for the corresponding application. For more information, please see
`htt
`://www.usoto. ov/ atentS/init events"
`h/index.‘s
`
`
`
`
`
`, or send an inquiry to PF"I-Ifeedback{<‘buspto.qov.
`
`Application Papers
`
`10)I:I The specification is objected to by the Examiner.
`11)IXI The drawing(s) filed on 9/30/2013 is/are: a)lZl accepted or b)I:I objected to by the Examiner.
`Applicant may not request that any objection to the drawing(s) be held in abeyance. See 37 CFR 1.85(a).
`
`Replacement drawing sheet(s) including the correction is required if the drawing(s) is objected to. See 37 CFR 1.121 (d).
`
`Priority under 35 U.S.C. § 119
`12)IZI Acknowledgment is made of a claim for foreign priority under 35 U.S.C. §119(a)-(d) or (f).
`Certified copies:
`
`b)I:I Some” c)I:I None of the:
`a)I:I All
`1.I:I Certified copies of the priority documents have been received.
`2.I:I Certified copies of the priority documents have been received in Application No.
`3le Copies of the certified copies of the priority documents have been received in this National Stage
`
`application from the International Bureau (PCT Rule 17.2(a)).
`** See the attached detailed Office action for a list of the certified copies not received.
`
`Attachment(s)
`
`
`
`

`

`Application/Control Number: 14/042,656
`
`Art Unit: 1678
`
`Page 2
`
`The present application is being examined under the pre-AlA first to invent provisions.
`
`DETAILED ACTION
`
`1. Claims 1-21 are pending.
`
`Response to Election-Restriction
`
`1. Applicant’s election of Group I
`
`(claims 1-9)
`
`in response to restriction/election
`
`requirement mailed on 05/25/2016 is acknowledged and entered.
`
`Because applicant did not traverse the restriction requirement, the election has
`
`been treated as an election without traverse (MPEP § 818.03(a)). Accordingly, the
`
`restriction requirement is deemed proper and is made FINAL.
`
`In response to election of species requirement Applicant did not elect a single
`
`species but however, upon a further review of the claims, the election of species
`
`requirement has been withdrawn.
`
`Therefore, claims 10-21 are withdrawn from further consideration as being
`
`directed to a non-elected invention. See 37 CFR 1.142(b) and MPEP § 821.03.
`
`Applicants preserve their right to file a divisional on the non-elected subject matter.
`
`2. Therefore claims 1-9 are examined on merits in this office action.
`
`Claim Rejections - 35 USC § 103
`
`3. The following is a quotation of 35 U.S.C.103(a) which forms the basis for all
`
`obviousness rejections set forth in this Office action:
`
`(a) A patent may not be obtained though the invention is not identically disclosed or described as set
`forth in section 102 of this title, if the differences between the subject matter sought to be patented and
`
`

`

`Application/Control Number: 14/042,656
`
`Art Unit: 1678
`
`Page 3
`
`the prior art are such that the subject matter as a whole would have been obvious at the time the
`invention was made to a person having ordinary skill in the art to which said subject matter pertains.
`Patentability shall not be negatived by the manner in which the invention was made.
`
`4. Claims 1-9 are rejected under 35 U.S.C. 103(a) as being unpatentable over Wagner
`
`et a/ (US 6,406,921 B1) in view of Chen (2010/0113476) and Besselink (Applied
`
`Biochemistry and Biotechnology 1993).
`
`Wagner discloses protein arrays on a substrate (Abstract). Wagner discloses a
`
`protein immobilized substrate wherein the substrate comprises a self-assembled
`
`monolayer 7 linked to affinity molecule 8, which is in turn is linked to a protein (Fig.
`
`6) (Col. 14,
`
`line 5 to col.15,
`
`line 4; col. 18,
`
`lines 29-44). Wagner teaches that an
`
`affinity tag enhances site-specific immobilization of protein onto the monolayer
`
`(col.3,
`
`lines 56-58). Wagner teaches that affinity tag confer enhanced binding or
`
`reaction of the protein with Y (col. 12, lines 59-67). Wagner teaches that affinity tag
`
`allows for common immobilization strategy to be used with multiple different proteins
`
`(col.13, lines 9-12). Wagner teaches that affinity tag may be an amino acids capable
`
`of immobilizing a protein (col. 5, line 40) and in a preferred embodiment, affinity tag
`
`comprises at least one amino acid (col.13,
`
`lines 23-24). Wagner teaches that the
`
`affinity tag may be a lone monolayer reactive amino acids such as cysteine, lysine,
`
`histidineI arginineI tyrosine and glutamine (col.13, lines 16-19 and 21-22). Wagner
`
`teaches that the affinity tag is a component of a layer of affinity tag molecules
`
`immobilized on the monolayer (col.14,
`
`lines 11-13) and the affinity tag can be a
`
`single amino acid
`
`(col.5,
`
`lines 36-45; col. 13,
`
`lines 16-19; col.20,
`
`lines 26-30).
`
`Wagner further teaches that amino acid tag interact with Y functional group of the
`
`monolayer molecule (col.13, lines 21-23) wherein the Y functional group can be a
`
`

`

`Application/Control Number: 14/042,656
`
`Art Unit: 1678
`
`Page 4
`
`carboxylic acid activated to a reactive ester (See Figs 4 and 5; col. 11, lines 30-45
`
`and col.20, lines 1-12). Wagner further teaches that the protein can be antibody or
`
`antibody fragment (Col.7, lines 45-47).
`
`Wagner does not have specific disclosure for
`
`the antibody linked to the
`
`carboxylic acid group of a self-assembled monolayer through the single amino acid
`
`wherein the amino group of the single amino acid formed a peptide bond with the
`
`carboxylic acid of the self-assembled monolayer and the carboxylic acid group of the
`
`single amino acid formed a peptide bond with an amino group of the antibody.
`
`Chen teaches that single amino acid linker helps to retain activity of bound
`
`compound and sometimes surpassing peptidyl linkers (paragraph [0135]).
`
`Besselink discloses -glycine NHS surface suitable for immobilization of amine
`
`containing compound (Abstract and Scheme 1). Besselink teaches NHS activated
`
`surface having glycine (-glycine-NHS) is more stable than NHS activated surface
`
`without glycine (page 242, 3rd paragraph) and the surface activated with —glycine-
`
`NHS is more active for immobilization of amine containing compound (Fig.10; page
`
`240, see “Discussion” and page 244, last paragraph).
`
`From the forgoing description in mind,
`
`it would have been a prima facie obvious
`
`at the time the invention was made, for one of ordinary skill
`
`in the art to have
`
`considered attaching the antibody to the self-assembled monolayer because
`
`Wagner teaches immobilization of proteins on the array and the protein can be an
`
`specific binding partner such as an antibody or antibody fragment for detection of
`
`analyte (Col.7,
`
`lines 45-47; Col.17,
`
`lines 25-30 and Col.18,
`
`lines 12-21). One of
`
`

`

`Application/Control Number: 14/042,656
`
`Art Unit: 1678
`
`Page 5
`
`ordinary skill would be motivated to attached the antibody in the self-assembled
`
`monolayer through the affinity tag (e.g. amino acid) because Wagner teaches that
`
`affinity tag enhances site-specific immobilization of protein onto the monolayer,
`
`confer enhanced binding or
`
`reaction of
`
`the protein and allows for common
`
`immobilization strategy to be used with multiple different proteins.
`
`It would have
`
`been a prima facie obvious at the time the invention was made, for one of ordinary
`
`skill
`
`in the art
`
`to have attached the antibody to the self-assembled monolayer
`
`through a single amino acid linker because Wagner teaches attaching protein
`
`through an affinity tag wherein the affinity molecule may be a single amino acid (col.
`
`13, lines 16-19; col.20, lines 26-30) and because Wagner teaches that the affinity
`
`tag can a component of a layer immobilized on the monolayer (col.14, lines 11-13).
`
`One of ordinary skill in the art would be motivated to use single amino acid linker to
`
`link protein to the surface because Chen teaches that single amino acid linker helps
`
`to retain activity of bound compound and sometimes surpassing peptidyl
`
`linkers
`
`(paragraph [0135]). Moreover, one of ordinary skill
`
`in the art would be motivated to
`
`provide activated single amino acid, such as glycine-NHS on a carboxyl surface to
`
`immobilize a protein because Besselink teaches NHS activated surface having
`
`glycine (-glycine-NHS) is more stable than NHS activated surface without glycine
`
`(page 242, 3rd paragraph) and the surface activated with —glycine-NHS is more
`
`active for immobilization of amine containing compound (Fig.10; page 240, see
`
`“Discussion” and page 244, last paragraph).
`
`In addition, one of ordinary skill
`
`in the
`
`art would have had a reasonable expectation of success of using the monolayer of
`
`

`

`Application/Control Number: 14/042,656
`
`Art Unit: 1678
`
`Page 6
`
`Wagner having the carboxylic acid group to provide glycine having activated NHS
`
`group because Wagner teaches activation process for the carboxylic group (Figs. 4
`
`and 5 and Besselink teaches the process of immobilizing glycine through its amino
`
`group to activated surface and then activating the carboxyl group of the glycine to
`
`provide the -glycine-NHS surface highly stable and highly reactive to immobilized
`
`amine containing compounds.
`
`5. Claims 1-9 are rejected under 35 U.S.C. 103(a) as being unpatentable over Hatoka
`
`(US 8,980,645 B2) alone or further in view of in view of over Wagner et a/ (US
`
`6,406,921 B1).
`
`Hatoka throughout the reference disclose method of immobilization of Protein A
`
`to self-assembled monolayer through one molecule of amino acid (see claims 1-9
`
`and Fig 1).
`
`Hatoka, do not mention immobilization of other commonly known specific
`
`binding protein such as an antibody to self-assembled monolayer through one
`
`molecule of amino acid.
`
`Wagner discloses protein arrays on a substrate (Abstract). Wagner discloses a
`
`protein immobilized substrate wherein the substrate comprises a self-assembled
`
`monolayer 7 linked to affinity molecule 8, which is in turn is linked to a protein (Fig.
`
`6) (Col. 14,
`
`line 5 to col.15,
`
`line 4; col. 18,
`
`lines 29-44). Wagner teaches that an
`
`affinity tag enhances site-specific immobilization of protein onto the monolayer
`
`(col.3,
`
`lines 56-58). Wagner teaches that affinity tag confer enhanced binding or
`
`reaction of the protein with Y (col. 12, lines 59-67). Wagner teaches that affinity tag
`
`

`

`Application/Control Number: 14/042,656
`
`Art Unit: 1678
`
`Page 7
`
`allows for common immobilization strategy to be used with multiple different proteins
`
`(col.13, lines 9-12). Wagner teaches that affinity tag may be an amino acids capable
`
`of immobilizing a protein (col. 5, line 40) and in a preferred embodiment, affinity tag
`
`comprises at least one amino acid (col.13, lines 23-24). Wagner teaches that the
`
`affinity tag may be a lone monolayer reactive amino acids such as cysteine, lysine,
`
`histidineI arginineI tyrosine and glutamine (col.13, lines 16-19 and 21-22). Wagner
`
`teaches that the affinity tag is a component of a layer of affinity tag molecules
`
`immobilized on the monolayer (col.14,
`
`lines 11-13) and the affinity tag can be a
`
`single amino acid
`
`(col.5,
`
`lines 36-45; col. 13,
`
`lines 16-19; col.20,
`
`lines 26-30).
`
`Wagner further teaches that amino acid tag interact with Y functional group of the
`
`monolayer molecule (col.13, lines 21-23) wherein the Y functional group can be a
`
`carboxylic acid activated to a reactive ester (See Figs 4 and 5; col. 11, lines 30-45
`
`and col.20, lines 1-12). Wagner further teaches that the protein can be antibody or
`
`antibody fragment (Col.7, lines 45-47).
`
`Therefore, given the fact that Protein A is a specific binding protein that
`
`is
`
`immobilized through one molecule of amino acid (Hatoka),
`
`immobilization of other
`
`commonly known specific binding protein such as an antibody using the similar
`
`method would be obvious to one of ordinary skill in the art. Moreover, given the fact
`
`that Wagner teaches other specific binding proteins such as an antibody for
`
`immobilization of array surface utilizing amino acid activated to reactive ester,
`
`it
`
`would be obvious to one of ordinary skill
`
`in the art at the time the invention was
`
`made to consider utilizing the single amino acid containing surface of Hatoka for
`
`

`

`Application/Control Number: 14/042,656
`
`Art Unit: 1678
`
`Page 8
`
`immobilization of specific binding protein such as an antibody with a reasonable
`
`expectation of success.
`
`6. Claims 1-9 are rejected under 35 U.S.C. 103(a) as being unpatentable over Hatoka
`
`(US 8,785,143 B2) alone or further in view of in view of over Wagner et a/ (US
`
`6,406,921 B1).
`
`Hatoka
`
`throughout
`
`the
`
`reference disclose method of
`
`immobilization
`
`of
`
`streptavidin to self-assembled monolayer through one molecule of amino acid (see
`
`claims 12 and Fig 1).
`
`Hatoka, do not mention immobilization of other commonly known specific
`
`binding protein such as an antibody to self-assembled monolayer through one
`
`molecule of amino acid.
`
`Wagner discloses protein arrays on a substrate (Abstract). Wagner discloses a
`
`protein immobilized substrate wherein the substrate comprises a self-assembled
`
`monolayer 7 linked to affinity molecule 8, which is in turn is linked to a protein (Fig.
`
`6) (Col. 14,
`
`line 5 to col.15,
`
`line 4; col. 18,
`
`lines 29-44). Wagner teaches that an
`
`affinity tag enhances site-specific immobilization of protein onto the monolayer
`
`(col.3,
`
`lines 56-58). Wagner teaches that affinity tag confer enhanced binding or
`
`reaction of the protein with Y (col. 12, lines 59-67). Wagner teaches that affinity tag
`
`allows for common immobilization strategy to be used with multiple different proteins
`
`(col.13, lines 9-12). Wagner teaches that affinity tag may be an amino acids capable
`
`of immobilizing a protein (col. 5, line 40) and in a preferred embodiment, affinity tag
`
`comprises at least one amino acid (col.13, lines 23-24). Wagner teaches that the
`
`

`

`Application/Control Number: 14/042,656
`
`Art Unit: 1678
`
`Page 9
`
`affinity tag may be a lone monolayer reactive amino acids such as cysteine, lysine,
`
`histidineI arginineI tyrosine and glutamine (col.13, lines 16-19 and 21-22). Wagner
`
`teaches that the affinity tag is a component of a layer of affinity tag molecules
`
`immobilized on the monolayer (col.14,
`
`lines 11-13) and the affinity tag can be a
`
`single amino acid
`
`(col.5,
`
`lines 36-45; col. 13,
`
`lines 16-19; col.20,
`
`lines 26-30).
`
`Wagner further teaches that amino acid tag interact with Y functional group of the
`
`monolayer molecule (col.13, lines 21-23) wherein the Y functional group can be a
`
`carboxylic acid activated to a reactive ester (See Figs 4 and 5; col. 11, lines 30-45
`
`and col.20, lines 1-12). Wagner further teaches that the protein can be antibody or
`
`antibody fragment (Col.7, lines 45-47).
`
`Therefore, given the fact that Protein A is a specific binding protein that
`
`is
`
`immobilized through one molecule of amino acid (Hatoka),
`
`immobilization of other
`
`commonly known specific binding protein such as an antibody using the similar
`
`method would be obvious to one of ordinary skill in the art. Moreover, given the fact
`
`that Wagner teaches other specific binding proteins such as an antibody for
`
`immobilization of array surface utilizing amino acid activated to reactive ester,
`
`it
`
`would be obvious to one of ordinary skill
`
`in the art at the time the invention was
`
`made to consider utilizing the single amino acid containing surface of Hatoka for
`
`immobilization of specific binding protein such as an antibody with a reasonable
`
`expectation of success.
`
`Double Parenting
`
`

`

`Application/Control Number: 14/042,656
`
`Art Unit: 1678
`
`Page 10
`
`7. 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
`obviousness-type 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); and 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 a nonstatutory
`double patenting ground provided the conflicting application or patent either is
`shown to be commonly owned with this application, or claims an invention made as
`a result of activities undertaken within the scope of a joint research agreement.
`Effective January 1, 1994, a registered attorney or agent of record may sign a
`terminal disclaimer. A terminal disclaimer signed by the assignee must fully comply
`with 37 CFR 3.73(b).
`
`8. Claims 1-6 are rejected on the ground of nonstatutory double patenting as being
`
`unpatentable over claims 1-21 of U.S. Patent No. 8,871,457. Although the claims at
`
`issue are not identical, they are not patentably distinct from each other because the
`
`subject matter of the claims of instant application is fully disclosed in the claims of
`
`US patent 8,871,457. The claims of the US patent disclose method of immobilization
`
`of Glucose oxidase
`
`through one molecule
`
`of
`
`amino acid but,
`
`however,
`
`immobilization of other commonly known specific binding protein such as an
`
`antibody using the similar method would be obvious to one of ordinary skill in the art.
`
`9. Claims 1-6 are rejected on the ground of nonstatutory double patenting as being
`
`unpatentable over claims 1-9 of U.S. Patent No. 8,785,143. Although the claims at
`
`issue are not identical, they are not patentably distinct from each other because the
`
`

`

`Application/Control Number: 14/042,656
`
`Art Unit: 1678
`
`Page 11
`
`subject matter of the claims of instant application is fully disclosed in the claims of
`
`US patent 8,785,143. The claims of the US patent disclose method of immobilization
`
`of streptavidin but however,
`
`immobilization of other commonly known specific
`
`binding member protein such as an antibody using the similar method would be
`
`obvious to one of ordinary skill in the art.
`
`10.Claims 1-6 are rejected on the ground of nonstatutory double patenting as being
`
`unpatentable over claims 1-9 of U.S. Patent No. 8,980,645. Although the claims at
`
`issue are not identical, they are not patentably distinct from each other because the
`
`subject matter of the claims of instant application is fully disclosed in the claims of
`
`US patent 8,871,457. The claims of the US patent disclose method of immobilization
`
`of Protein A through one molecule of amino acid but, however,
`
`immobilization of
`
`other commonly known specific binding protein such as an antibody using the similar
`
`method would be obvious to one of ordinary skill in the art.
`
`Conclusion
`
`11.No claims are allowed.
`
`12.Any inquiry concerning this communication or earlier communications from the
`
`examiner should be directed to SHAFIQUL HAQ whose telephone number is
`
`(571)272-6103. The examiner can normally be reached on 7 AM to 3:30 P.M..
`
`