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 .
Claims 1-2, 4-9, 11-12, 14, 22, 25, 33, 36, 41 and 42 are pending.
Claims 4-8 are withdrawn from further consideration by the examiner, 37 C.F.R. 1.142(b) as being drawn to non-elected inventions.
Claims 1-2, 9, 11-12, 14, 22, 25, 33, 36, 41 and 42, drawn to a method of depleting T cells in a subject having an autoimmune disease that read on (A) anti-CD5 antibody 5D7, (B) SEQ ID NO: 282 and 283 as the heavy and light chain variable region amino acid sequences, (C) SLE as the species of autoimmune disease, (D) amatoxin as the species of cytotoxin, are being acted upon in this Office Action.
Priority
Applicant’ claim priority to provisional application 62/857,744, filed June 5, 2019, is acknowledged.
Information Disclosure Statement
The information disclosure statement (IDS) submitted on June 25, 2025 has been considered by the examiner and an initialed copy of the IDS is included with this Office Action.
Specification
The objection to the specification is withdrawn in view of the sequence listing submitted on July 17, 2025.
Objection and Rejection Withdrawn
The objection to claim 38 is withdrawn in light of the claim has been canceled.
The rejection of claims 1, 2, 9, 12, 33 and 36 under 35 U.S.C. 112(b) or 35 U.S.C. 112 (pre-AIA ), second paragraph is withdrawn in view of the claim amendment.
The written description and enablement rejection of claims 1-3, 9, 11-12, 14, 16, 18-22, 25, 33 and 36-38 under 35 U.S.C. 112(a) or 35 U.S.C. 112 (pre-AIA ), first paragraph are withdrawn in view of the claim amendment.
The rejection of claims 1-3, 14, 16, 18, 33 and 37 under 35 U.S.C. 102(a)(1) as being anticipated by WO8906968 publication published August 10, 1989; PTO 1449) is withdrawn in view of the amendment to claim 1.
The rejection of claims 1, 2, 9, 11, 14, 33 and 36 under 35 U.S.C. 102(a)(1) as being anticipated by Uno et al (WO2016/071856 publication published May 12, 2016; PTO 1449) is withdrawn in view of the amendment to claim 1.
The rejection of claims 1-2, 9, 11, 18, 36 and 38 are rejected under 35 U.S.C. 102 (a)(1) as being anticipated by WO2008121160 publication (published Oct 9, 2008; PTO 1449) is withdrawn in view of the amendment to claim 1.
The rejection of claims 1 and 3 under 35 U.S.C. 102 (a)(1) as being anticipated by US Patent No. 5,869,619 (Studnicka hereafter, issued February 9, 1999; PTO 1449) is withdrawn in view of the amendment to claim 1.
The rejection of clams 1, 12, 18-22 and 25 under 35 U.S.C. 103 as being unpatentable over WO2008121160 publication (published Oct 9, 2008; PTO 1449) in view of Anderl et al (WO2010/115629, PTO 1449) is withdrawn in view of the claim amendment. The addition of Anderl does not cure the deficiency of the WO2008121160 publication.
The rejection of claims 1-3, 9, 11-12, 14, 16, 18-22, 25, 33 and 36-38 on the ground of nonstatutory obviousness-type double patenting as being unpatentable over claims 1-13 of U.S. Patent No. 12,251,448 is withdrawn in view of the terminal disclaimer filed in 12,251,448 (17/244,721).
New ground of rejections necessitated by the amendment filed July 17, 2025
Claim Rejections - 35 USC § 103
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 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.
The factual inquiries set forth in Graham v. John Deere Co., 383 U.S. 1, 148 USPQ 459 (1966), that are applied for establishing a background for determining obviousness under 35 U.S.C. 103(a) 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.
This application currently names joint inventors. In considering patentability of the claims under pre-AIA 35 U.S.C. 103(a), the examiner presumes that the subject matter of the various claims was commonly owned at the time any inventions covered therein were made absent any evidence to the contrary. Applicant is advised of the obligation under 37 CFR 1.56 to point out the inventor and invention dates of each claim that was not commonly owned at the time a later invention was made in order for the examiner to consider the applicability of pre-AIA 35 U.S.C. 103(c) and potential pre-AIA 35 U.S.C. 102(e), (f) or (g) prior art under pre-AIA 35 U.S.C. 103(a).
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 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.
Claims 1-2, 9, 11, 12, 14, 22, 25, 36, 41 and 42 are rejected under 35 U.S.C. 103 as being unpatentable over WO2008121160 publication (of record, published Oct 9, 2008; PTO 1449) in view of Anderl (WO2016142049, newly cited, published September 15, 2016; PTO 892).
Regarding claims 1, 9, 11, 36, the WO2008121160 publication teaches T cell depletion therapy (see p. 76, p. 75, line 23, claim 25) by depleting CD5.sup.+ cells in a subject, e.g., humans (see p. 73, line 15, in particular) comprising administering, to said subject, an effective amount of an antibody-drug conjugate or immunoconjugate (see p. 57, line 35) comprising a humanized anti-CD5 antibody (5D7) that binds to human CD5 wherein the anti-CD5 antibody conjugated to various toxins (see p. 58) via a flexible linker, e.g., (GS)n, (GSGGS)n, (GGGGS)n and (GGGS)n where n is an integer of at least one, or chemical crosslinking such as polyethylene glycol (PEG), or linker comprises a disulfide bond (52, line 40-11), see p. 62, for depleting a mammal of a cell expressing CD5.
The WO2008121160 publication teaches the anti-CD5 antibody comprises a VH comprising the amino acid sequence of SEQ ID NO: 19, which is 100% identical to the claimed SEQ ID NO: 282, and comprises the reference CDR-H1 of SEQ ID NO: 29, CDR-H2 of SEQ ID NO: 30 and CDR-H2 of SEQ ID NO: 31, see sequence alignment below, 3 CDRs in bold:
Query Match 100.0%; Score 635; Length 120;
Best Local Similarity 100.0%;
Matches 120; Conservative 0; Mismatches 0; Indels 0; Gaps 0;
Qy 1 QVTLKESGPVLVKPTETLTLTCTFSGFSLSTSGMGVGWIRQAPGKGLEWVAHIWWDDDVY 60
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 1 QVTLKESGPVLVKPTETLTLTCTFSGFSLSTSGMGVGWIRQAPGKGLEWVAHIWWDDDVY 60
Qy 61 YNPSLKSRLTITKDASKDQVSLKLSSVTAADTAVYYCVRRRATGTGFDYWGQGTLVTVSS 120
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 61 YNPSLKSRLTITKDASKDQVSLKLSSVTAADTAVYYCVRRRATGTGFDYWGQGTLVTVSS 120
And a VL comprising the amino acid sequence of SEQ ID NO: 21, which is 100% identical to the claimed SEQ ID NO: 283 and comprises CDR-L1 of SEQ ID NO: 32, CDR-L2 of SEQ ID NO: 33 and CDR-L3 of SEQ ID NO: 34, see, p. 100-101, see sequence alignment below, 3 CDRs in bold:
Query Match 100.0%; Score 560; Length 106;
Best Local Similarity 100.0%;
Matches 106; Conservative 0; Mismatches 0; Indels 0; Gaps 0;
Qy 1 NIVMTQSPSSLSASVGDRVTITCQASQDVGTAVAWYQQKPDQSPKLLIYWTSTRHTGVPD 60
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 1 NIVMTQSPSSLSASVGDRVTITCQASQDVGTAVAWYQQKPDQSPKLLIYWTSTRHTGVPD 60
Qy 61 RFTGSGSGTDFTLTISSLQPEDIATYFCHQYNSYNTFGSGTKLEIK 106
||||||||||||||||||||||||||||||||||||||||||||||
Db 61 RFTGSGSGTDFTLTISSLQPEDIATYFCHQYNSYNTFGSGTKLEIK 106
The WO2008121160 publication teaches the subject has various diseases, e.g., autoimmune disease as per claims 1-2, or T cell malignancy, e.g., T-cell acute lymphoblastic leukemia (T-ALL), anaplastic large cell lymphoma (ALCL), peripheral T-cell lymphoma (PTCL), cutaneous T-cell, lymphoma (CTCL) as per claims 9, 11, 36, see p 7, abstract, in particular. Examples of autoimmune diseases include, for example, rheumatoid arthritis (RA), systemic lupus erythematosus (SLE or lupus), multiple sclerosis, Sjogren's syndrome, and idiopathic thrombocytopenia purpura (ITP), see p. 4, line29-33. Various T-cell mediated autoimmune diseases exist including Crohn's disease, psoriasis, organ transplantation rejection, graft versus host disease (GVHD), p. 7, line 33-35. Suitable toxins include diptheria A chain, exotoxin A chain, ricin A chain, abrin A chain, curcin, crotin, phenomycin, enomycin and the like, calicheamicin, auristatins, geldanamycin, maytansine, and duocarmycins and analogs, see p. 58, in particular.
Claim 2 is included as administering same antibody drug conjugate (ADC) inherently depletes endogenous CD5+ T cells in the thymus of the subject. Since the Patent Office does not have the facilities for examining and comparing the conjugate of the instant invention to those of the prior art, the burden is on applicant to show that the prior art conjugate is different from the claimed conjugate. See In re Best, 562 F.2d 1252, 195 USPQ 430(CCPA 1977).
Regarding claim 9, the WO2008121160 publication teaches the subject has T cell malignancy, e.g., T cell acute lymphoblastic leukemia, T-ALL, T cell lymphoma see p. 36-37, p. 74.
Regarding claim 11, the WO2008121160 publication teaches that the T cell malignancy is a T-cell acute lymphoblastic leukemia/lymphoma (T-ALL), enteropathy-type T-cell lymphoma, hepatosplenic T-cell lymphoma, anaplastic large cell lymphoma (ALCL), cutaneous T-cell lymphoma (CTCL), see p. 74-76.
Regarding claim 12, the WO2008121160 publication teaches that the T cell malignancy is a relapsed chronic lymphocytic leukemia (CLL), see p. 4, refractory CLL, see p. 4, in particular.
Regarding claim 14, the WO2008121160 publication teaches that the antibody has an isotype of IgG1, see Figure 2, p. 93, in particular.
Regarding claim 42, the WO2008121160 publication teaches that the Fc comprises a mutation, e.g., leucine at position 234 has been substituted for Alanine, aka 234A, see p. 8, p. 15. Likewise, leucine (L) at position 235 has been substituted for Alanine (aka 235A, p. 8, p. 15), all positions numbering according to the EU index of Kabat, see p. 9, in particular.
The WO2008121160 publication does not teach the cytotoxin is an amatoxin via a cleavable linker as per claims 1, wherein the antibody drug conjugate (ADC) is represented by the formula Ab-Z-L-Am wherein the Ab is the anti-CD5 antibody or antigen-binding fragment thereof, L is a linker, Z is a chemical moiety, and Am is an amatoxin represented by formula (I) as per claim 22 and 25 via a Cys118, orCys265, numbering according to the EU index as in Kabat as per claim 41.
However, Anderl teaches amatoxin-antibody conjugate of generic formula:
Ama - L-X-S- Ab, wherein Ama is an amatoxin, L is a linker, X is a moiety resulting from coupling of a thiol group to a thiol-reactive group, S is the sulphur atom of a cysteine amino acid residue, and Ab is an antibody sequence, or a functional antibody fragment, comprising said cysteine residue, wherein said cysteine residue is selected from the list of heavy chain 118Cys, heavy chain 239Cys, and heavy chain 265Cys, in particular: heavy chain 118Cys, and heavy chain 265Cys, see entire document, p. 5, para. [0018] to [0020], [0025], [0085] to [0087], reference claims 1-3, in particular.
Anderl teaches that the cleavable linker is Val-Ala-PAB, and the Z is a thioreactive group, e.g., maleimide or maleidopropanamido (aka chemical moiety), see Example 22, in particular.
PNG
media_image1.png
475
815
media_image1.png
Greyscale
The amatoxin-linker is conjugated to the cysteine at position 118 on the heavy chain (HC-A118C), HC-S239C; HC-D265C of antibody Trastuzumab, see para. [0032], [0033]. The conjugate is useful for treating HER-2 positive cancer, see para. [0023].
Regarding claims 22, 25, he reference amatoxin above wherein R1 is OH, R2 is OH, R3 is H, R4 is H, R5 is RC, R6 is H, R7 is H, R8 is NH2, R9 is OH, Rc is L-Z wherein L is cleavable linker Val-Ala-PAb, and Z is maleimide, the reactive substituent present within the antibody is S (thiol group).
In view of the combined teachings of the references, it would have been prima facie obvious to a person of ordinary skill in the art before the effective filling date of the claimed invention to have substitute Anderl’s anti-HER2 antibody linked to the amatoxin via a cleavable linker for WO2008121160 publication’s anti-CD5 antibody and then administering the anti-CD5 antibody drug conjugate to a human subject in order to deplete depleting CD5+ T cells in the subject having autoimmune or CD 5 expressing T cell malignancies, e.g., T-cell acute lymphoblastic leukemia (T-ALL), anaplastic large cell lymphoma (ALCL), peripheral T-cell lymphoma (PTCL), cutaneous T-cell, lymphoma (CTCL).
Claim 12 is included as it is within the purview of one of ordinary skilled to treat T cell malignancy that is relapsed, and refractory, absence of any unexpected results.
One of ordinary skill in the art would have had an expectation of success at the time the invention was made to modify the method of WO2008121160 publication in view of Anderl et al because cysteine engineered anti-CD5 antibody allows site-specific conjugation of amatoxin to the heavy chain away from the antigen binding domain via cysteine thiol reactive group and the cleavable linker allows the amatoxin to be release once internalized by CD5 expressing cells, see para.[0066] to [0068].
One of ordinary skill in the art would be motivated to combine the teachings of WO2008121160 publication and Anderl because amatoxin inhibits mammalian RNA polymerase II (see para. [0045]) and the WO2008121160 publication teaches that T cell depletion therapy (see p. 76, p. 75, line 23, claim 25) by depleting CD5.sup.+ cells in a subject, e.g., humans (see p. 73, line 15, in particular) comprising administering, to said subject, an effective amount of an antibody-drug conjugate or immunoconjugate comprising anti-CD5 conjugated to any toxin (see p. 57, line 35).
A person of ordinary skill in the art is always motivated to pursue the known options within her or his technical grasp. If this leads to the anticipated success, it is likely the product not of innovation but of ordinary skill and common sense. KSR Int’l Co. v. Teleflex Inc., 550 U.S. 398, 416 (2007).
“The test of obviousness is not express suggestion of the cl aimed invention in any or all of the references but rather what the references taken collectively would suggest to those of ordinary skill in the art presumed to be familiar with them.” See In re Rosselet 146 USPQ 183, 186 (CCPA 1965).
“There is no requirement (under 35 USC 103(a)) that the prior art contain an express suggestion to combine known elements to achieve the claimed invention. Rather, the suggestion to combine may come from the prior art, as filtered through the knowledge of one skilled in the art.,” Motorola, Inc, v. Interdigital Tech. Corn., 43 USPQ2d 1481, 1489 (Fed. Cir. 1997).
Accordingly, the claimed invention as a whole was prima facie obvious to one of ordinary skill in the art before the effective filling date of the claimed invention especially in the absence of evidence to the contrary.
Claim 1 is rejected under 35 U.S.C. 103 as being unpatentable over WO2008121160 publication (of record, published Oct 9, 2008; PTO 1449) in view of Anderl (WO2016142049, newly cited, published September 15, 2016; PTO 892) as applied to claims 1-2, 9, 11, 12, 14, 22, 25, 36, 41 and 42 and further in view of WO2010145895 publication (published December 23, 2010; PTO 892).
The teachings of the WO2008121160 publication and Anderl have been discussed supra.
The WO2008121160 publication and Anderl do not teach the anti-CD5 antibody or antigen-binding portion thereof, comprising a heavy chain comprising a variable region (VH) comprising the amino acid sequence of SEQ ID NO: 291, and a light chain comprising a variable region (VL) comprising the amino acid sequence of SE ID NO: 290 as per claim 1.
However, the WO2010145895 publication teaches an anti-CD5 antibody or antigen-binding portion thereof, comprising a heavy chain comprising a variable region (VH) comprising the amino acid sequence of SEQ ID NO: 2, which is 100% identical to the claimed SEQ ID NO: 291, see sequence alignment below:
Query Match 100.0%; Score 644; Length 118;
Best Local Similarity 100.0%;
Matches 118; Conservative 0; Mismatches 0; Indels 0; Gaps 0;
Qy 1 EVQLQESGPGLVKPSQTLSLTCSVTGYSITSGYYWHWIRQFPGNKLEWMGYISYSGFTNY 60
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 1 EVQLQESGPGLVKPSQTLSLTCSVTGYSITSGYYWHWIRQFPGNKLEWMGYISYSGFTNY 60
Qy 61 KTSLINRISITHDTSENQFFLNLNSVTTEDTATYYCAGDRTGSWFAYWGQGTLVTVSA 118
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 61 KTSLINRISITHDTSENQFFLNLNSVTTEDTATYYCAGDRTGSWFAYWGQGTLVTVSA 118
and a light chain comprising a variable region (VL) comprising the amino acid sequence of SEQ ID NO: 1, which is 100% identical to the claimed SEQ ID NO: 290, see sequence alignment below:
Query Match 100.0%; Score 551; Length 107;
Best Local Similarity 100.0%;
Matches 107; Conservative 0; Mismatches 0; Indels 0; Gaps 0;
Qy 1 DIQVTQSPSSLSASLGERISLTCRTSQDISNYLNWFQQKPDGTFKRLIYATSSLDSGVPK 60
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 1 DIQVTQSPSSLSASLGERISLTCRTSQDISNYLNWFQQKPDGTFKRLIYATSSLDSGVPK 60
Qy 61 RFSGSGSGSDYSLTISSLESEDFADYYCLQYASYPFTFGSGTKLEIK 107
|||||||||||||||||||||||||||||||||||||||||||||||
Db 61 RFSGSGSGSDYSLTISSLESEDFADYYCLQYASYPFTFGSGTKLEIK 107
See p. 4, line 27-32, p. 7, line 5-13, p. 14, lines 6-9, in particular. The reference anti-CD5 antibody or antigen binding fragment thereof is useful for treating various T cell disease, such as T cell autoimmune diseases selected from the group consisting of rheumatoid arthritis, psoriasis, systemic lupus erythematosus, Castelman's disease, chronic thyroiditis (Hashimoto's thyroiditis), multiple sclerosis (MS), T cell related diseases such as graft versus host diseases for example, after bone marrow transplantation or activation of host T cell after graft rejections, such as after kidney transplantation (see p. 10) or T cell malignancies, see p. 11, lines 15-16, in particular.
In view of the combined teachings of the references, it would have been prima facie obvious to a person of ordinary skill in the art before the effective filling date of the claimed invention to substitute a known anti-CD5 antibody or antigen binding fragment thereof in the amatoxin conjugated anti-CD5 antibody or antigen binding fragment thereof via a cleavable linker for depleting CD5+ T cells in a human subject of WO2008121160 publication and Anderl for the WO2010145895 publication’s anti-CD5 antibody or antigen-binding portion thereof to arrive at the claimed invention with a reasonable expectation of success, e.g., depleting CD5+ T cells for treating CD5+ mediated autoimmune disease such as rheumatoid arthritis, multiple sclerosis (MS), systemic lupus erythematosus, graft versus host disease or CD5 expressing T cell malignancy.
One of ordinary skill in the art would have been motivated to do so because the WO2010145895 publication teaches that CD5 binding molecule is useful for treating T cell malignancies, autoimmune diseases and graft rejections, see reference claim 11 and the WO2008121160 publication teaches that cytotoxin conjugated anti-CD5 antibody or antigen binding fragment thereof is useful for treating a human subject having various autoimmune diseases, including but not limited to rheumatoid arthritis (RA), systemic lupus erythematosus (SLE or lupus), multiple sclerosis, Sjogren's syndrome, and idiopathic thrombocytopenia purpura (ITP), see p. 4, line29-33 or various T cell malignancies, e.g., T-cell acute lymphoblastic leukemia (T-ALL), anaplastic large cell lymphoma (ALCL), peripheral T-cell lymphoma (PTCL), cutaneous T-cell, lymphoma (CTCL) as per claims 9, 11, 36, see p 7, abstract, in particular. Further, “the substitution of a known element, e.g., anti-CD5 antibody or antigen-binding fragment thereof for another, e.g., anti-CD5 antibody or antigen binding fragment thereof is likely to be obvious when it does no more than yield predictable results.” KSR Int’l Co. v. Teleflex Inc., 550 U.S. 398, 416 (2007).
One of ordinary skill in the art would be motivated to combine the teachings of WO2010145895 publication and Anderl because amatoxin inhibits mammalian RNA polymerase II (see para. [0045]) and the WO2008121160 publication teaches that T cell depletion therapy (see p. 76, p. 75, line 23, claim 25) by depleting CD5.sup.+ cells in a subject, e.g., humans (see p. 73, line 15, in particular) comprising administering, to said subject, an effective amount of an antibody-drug conjugate or immunoconjugate comprising anti-CD5 conjugated to any toxin (see p. 57, line 35).
A person of ordinary skill in the art is always motivated to pursue the known options within her or his technical grasp. If this leads to the anticipated success, it is likely the product not of innovation but of ordinary skill and common sense. KSR Int’l Co. v. Teleflex Inc., 550 U.S. 398, 416 (2007).
“The test of obviousness is not express suggestion of the cl aimed invention in any or all of the references but rather what the references taken collectively would suggest to those of ordinary skill in the art presumed to be familiar with them.” See In re Rosselet 146 USPQ 183, 186 (CCPA 1965).
“There is no requirement (under 35 USC 103(a)) that the prior art contain an express suggestion to combine known elements to achieve the claimed invention. Rather, the suggestion to combine may come from the prior art, as filtered through the knowledge of one skilled in the art.,” Motorola, Inc, v. Interdigital Tech. Corn., 43 USPQ2d 1481, 1489 (Fed. Cir. 1997).
Accordingly, the claimed invention as a whole was prima facie obvious to one of ordinary skill in the art before the effective filling date of the claimed invention especially in the absence of evidence to the contrary.
Conclusion
SEQ ID NO: 282 is free of prior art.
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 nonprovisional extension fee (37 CFR 1.17(a)) 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 mailing date of this final action.
Any inquiry concerning this communication or earlier communications from the examiner should be directed to PHUONG HUYNH whose telephone number is (571)272-0846. The examiner can normally be reached on 9:00 a.m. to 6:30 p.m. The examiner can also be reached on alternate alternative Friday from 9:00 a.m. to 5:30 p.m.
If attempts to reach the examiner by telephone are unsuccessful, the examiner's supervisor, Misook Yu, can be reached at 571-270-3497. The fax phone number for the organization where this application or proceeding is assigned is 571-272-0839.
Information regarding the status of an application may be obtained from Patent Center. Status information for published applications may be obtained from Patent Center. Status information for unpublished applications is available through Patent Center for authorized users only. Should you have questions about access to Patent Center, contact the Electronic Business Center (EBC) at 866-217-9197 (toll-free).
Examiner interviews are available via telephone, in-person, and video conferencing using a USPTO supplied web-based collaboration tool. To schedule an interview, applicant is encouraged to use the USPTO Automated Interview Request (AIR) Form at https://www.uspto.gov/patents/uspto-automated- interview-request-air-form.
/PHUONG HUYNH/ Primary Examiner, Art Unit 1641