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 .
Election/Restrictions
Claim 20 and 53 are withdrawn from further consideration pursuant to 37 CFR 1.142(b) as being drawn to a nonelected Group II and III, there being no allowable generic or linking claim. Election was made without traverse in the reply filed on 11/6/2023.
Status of Claims
Withdrawn: 20, 53
Cancelled: 10, 16, 21-52, 54
New: 55
Examined Herein: 1-9, 11-15, 17-19, 55
Priority
Priority to PRO 62/633,849 filed on 2/22/2018 and PCT/US2019/019090 filed on 2/22/2019 is
acknowledged.
Information Disclosure Statement
The information disclosure statement (IDS) submitted on 8/17/2020, 11/23/2021, 8/2/2022, and 7/17/2023 is in compliance with the provisions of 37 CFR 1.97. Accordingly, the information disclosure statement is being considered by the examiner.
Drawings
The drawings filed on 8/17/2020 are accepted.
Withdrawn Rejections
The rejection of claims 1-9, 11-15, and 17 under 35 U.S.C. 103 over Stefano are hereby withdrawn in view of the amendment to claim 1 and Applicant’s persuasive arguments that Stefano does not teach the claim limitations as amended. [Reply 11/17/2025, Page 6-7]
The rejection of claims 1-15 and 17 under 35 U.S.C. 103 over Stefano and Burnet are hereby withdrawn in view of the amendment to claim 1 and Applicant’s persuasive arguments that Stefano and Burnet do not teach the claim limitations as amended. [Reply 11/17/2025, Page 6-7]
The rejection of claims 1-5, 8, 9, 12, 13, 18, and 19 under 35 U.S.C. 103 over Mayers are hereby withdrawn in view of the amendment to claim 1 and Applicant’s persuasive arguments that Mayers does not teach the claim limitations as amended. [Reply 11/17/2025, Page 6-7]
Claim Rejections - 35 USC § 103
The following is a quotation of 35 U.S.C. 103 which forms the basis for all obviousness rejections set forth in this Office action:
A patent for a claimed invention may not be obtained, notwithstanding that the claimed invention is not identically disclosed as set forth in section 102, if the differences between the claimed invention and the prior art are such that the claimed invention as a whole would have been obvious before the effective filing date of the claimed invention to a person having ordinary skill in the art to which the claimed invention pertains. Patentability shall not be negated by the manner in which the invention was made.
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 1-5, 8, 9, 12-15, and 17-19 are rejected under 35 U.S.C. 103 as being unpatentable over Bossard (US 2011/0318322 A1, Published 12/29/2011), in view of Gengrinovitch (US 2009/0203879 A1, Published 8/13/2009).
With respect to claim 1, Bossard discloses a compound comprising:
a protecting group (amide); and
an enzyme (glucocerebrosidase or α-galactosidase [0089]);
wherein, the protecting group is covalently attached to the enzyme.
More specifically, Bossard discloses the compound is a lysosomal enzyme moiety covalently attached through a cleavable linkage to a non-peptidic water-soluble polymer having the following structure:
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[Bossard, Page 22, Table 2]
With respect to claim 2, Bossard discloses the protecting group is an amide. [Bossard, Page 22, Table 2] An amide group is enzymatically cleavable.
With respect to claim 3, Bossard discloses the protecting group is attached to the enzyme directly. [Bossard, Page 22, Table 2]
With respect to claim 4, Bossard discloses that the protecting group is an amide. [Bossard, Page 22, Table 2] An amide group protects an enzyme from enzymatic degradation.
With respect to claim 8, Bossard discloses the compound further comprises a linker, polyethylene glycol (PEG). [Bossard, Page 22, Table 2]
With respect to claim 9, Bossard discloses the protecting group comprises an amide. [Bossard, Page 22, Table 2]
With respect to claim 13, Bossard discloses the enzyme is α-Galactosidase or glucocerebrosidase. [Bossard, 0089 & Page 22, Table 2] α-Galactosidase and glucocerebrosidase are resistant to proteases.
With respect to claim 14, Bossard discloses the compound further comprises a degradation shielding moieties. [Bossard, Page 22, Table 2]
With respect to claim 15, Bossard discloses the compound the degradation shielding moiety is PEG. [Bossard, Page 22, Table 2]
With respect to claim 17, Bossard discloses the enzyme is α-Galactosidase or glucocerebrosidase. [Bossard, 0089 & Page 22, Table 2] α-Galactosidase and glucocerebrosidase have activity toward a substrate that is not native in a cell.
With respect to claim 18-19, Bossard discloses the enzyme is α-Galactosidase or glucocerebrosidase. [Bossard, 0089 & Page 22, Table 2] α-Galactosidase and glucocerebrosidase lack activity toward native substrates in a cell and is heterologous to the said cell.
Bossard further discloses the polymer has an alkoxy “end-capping moiety” that represents the terminal or endpoint of the water-soluble polymer. Bossard discloses the end-capping group may be coupled to a detectable label, so that the amount or location of the polymer and/or the moiety (e.g., active agent) polymer is coupled, can be determined by using a suitable detector. Bossard discloses the labels include, without limitation, fluorescers, chemiluminescers, moieties used in enzyme labeling, colorimetric (e.g., dyes), metal ions, radioactive moieties, and the like. [Bossard, 0046]
Bossard does not disclose the compound comprises a cancer cell targeting moiety or a cross-linking moiety comprising indoxyl.
However, with respect to claim 1, Gengrinovitch discloses labeling (L) molecules that upon activation are able to bind to a biomolecule including proteins, peptides, nucleotides, nucleic acids, lipids and sugars. [Gengrinovitch, 0021] Gengrinovitch further discloses said labelling molecules include biotin or a substrate of a reporter enzyme such as BCIP (5-bromo-4-chloro-3-indoxyl phosphate). [Gengrinovitch, 0024, 0094]
Modifying the compound disclose by Bossard by conjugating BCIP to one end-capping moiety and biotin to the other end-capping moiety results in the compound of claim 1 and comprises:
a cancer cell targeting agent (biotin);
a protecting group (amide and phosphate of BCIP);
a cross-linking moiety that comprises indoxyl (indoxyl of BCIP); and
an enzyme (α-Galactosidase or glucocerebrosidase);
wherein, the cross-linking moiety, cancer cell targeting agent, and protecting group are covalently attached to the enzyme.
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[Illustration drawn by the Examiner & depicts the addition of BCIP and biotin to the end-capping moieties]
In which case, with respect to claim 5, Bossard and Gengrinovitch disclose the protecting group (phosphate of BCIP) is attached to the cross-linking moiety.
With respect to claim 12, Bossard and Gengrinovitch disclose the cell targeting agent is biotin. Biotin binds to and targets and endocytosing receptor on a cell.
With respect to claim 55, Bossard and Gengrinovitch disclose the crosslinking moiety is between the protecting group and the enzyme.
It would be obvious to one of ordinary skill in the art to modify the compound disclosed by Bossard by adding BCIP and biotin to the end-capped moieties of the water-soluble polymers and have a reasonable expectation of success. Bossard discloses a compound comprising a water-soluble polymer comorising alkoxy end-capping moieties. Bossard discloses “end-capped” refers to a terminal or endpoint of a polymer. Bossard further discloses the end-capping group can advantageously comprise a detectable label such as moieties used in enzyme labeling. Gengrinovitch discloses biotin and BCIP are both detectable labels that upon activation are able to bind to a biomolecule including, a protein, a peptide, a nucleic acid molecule, a sugar and a lipid. So, Gengrinovitch establishes that biotin and BCIP are both detectable labels used in peptide labeling. Thus, the combined teachings of Bossard and Gengrinovitch suggest that biotin and BCIP may function as the detectable labels coupled to the end-capping moieties on the water-soluble polymer disclosed by Bossard. Therefore, it is reasonable to expect the compound disclosed by Bossard may be modified by adding BCIP and biotin to the end-capped moieties of the water-soluble polymer. One would have been motivated to do so because it is prima facie obvious to combine references when some advantage or expected beneficial result would have been produced by their combination. MPEP 2144(II) In the instant case, Bossard discloses when the polymer has an end-capping group comprising a detectable label, the amount or location of the polymer and/or the moiety (e.g., active agent) to which the polymer is coupled, can be determined by using a suitable detector. [Bossard, 0046] Thus, one would have been motivated by the expectation that the aforementioned modification could enable the amount or location of the compound disclosed by Bossard to be detected.
Claims 1-5, 8, 9, 11, 12, 17-19, and 55 are rejected under 35 U.S.C. 103 as being unpatentable over Mayers (US 2006/0018908 A1, Published 1/26/2006), in view of Malcolm (US 2003/0228324 A1, Published 12/11/2003).
With respect to claim 1, Mayers discloses a compound comprising:
A cell targeting moiety (transferrin);
A protecting group (glucoside); and
A crosslinking moiety that comprises indoxyl (indoxyl conjugated to amide);
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[Mayers, Figure 13B, 5224]
With respect to claim 2, Mayers discloses the protecting group is a glucoside group. [Mayers, Figure 13B, 5224] A glucoside is enzymatically cleavable.
With respect to claim 5, Mayers discloses the protecting group is attached to the cross-linking moiety. [Mayers, Figure 13B, 5224]
With respect to claim 8, Mayers discloses the compound further comprises a carbon chain linker. [Mayers, Figure 13B, 5224]
With respect to claim 9, Mayers discloses the protecting group comprises a glucoside. [Mayers, Figure 13B, 5224]
With respect to claim 11, Mayers discloses the compound comprises two protecting groups and two cross-linking moieties. [Mayers, Figure 13B, 5224]
With respect to claim 12, Mayers discloses the cancer cell targeting agent is transferrin. [Mayers, Figure 13B, 5224] Transferrin binds to and targets an endocytosis receptor on a cell.
Mayers discloses the compound further comprises a carrier protein, albumin. [Mayers, Figure 13B, 5224] Additionally, Mayers discloses any substance that (a) is biologically compatible, (b) has a number of functional groups (e.g., amino groups, carboxyl groups, thiol groups, and the like) to which multiple platform building materials are attached, and (c) has a place for linking a cell targeting agent, is useful as a carrier moiety. Mayers discloses a carrier moiety includes for example, proteins. [Mayers, 0104]
Mayers does not disclose the compound comprises an enzyme.
However, with respect to claim 1, Malcolm discloses diphtheria toxoid/toxin and serum albumin are both carriers that may be coupled to a peptide/antibody. [Malcolm, 0060]
Modifying the compound disclosed by Mayers by replacing the carrier moiety with diphtheria toxoid/toxin results in the compound of claim 1 and comprises:
A cell targeting moiety (transferrin);
A protecting group (glucoside); and
A crosslinking moiety that comprises indoxyl (indoxyl conjugated to amide);
An enzyme (diphtheria toxoid/toxin)
Wherein, the cell targeting moiety, protecting group, and crosslinking moiety are covalently attached to the enzyme.
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[Illustration drawn by the Examiner & depicts the replacement of albumin with diphtheria toxoid/toxin]
In which case, with respect to claim 3, Mayers and Malcolm disclose the protecting group is attached to the enzyme through a linker.
With respect to claim 4, Mayers and Malcolm disclose the protecting group is glucoside. Glucoside protects an enzyme from enzymatic degradation.
With respect to claim 17, Mayers and Malcolm disclose the enzyme is diphtheria toxin. Diphtheria toxin has activity toward a substrate that is not native in a cell.
With respect to claim 18, Mayers and Malcolm disclose the enzyme is diphtheria toxin. Diphtheria toxin lacks activity toward native substrates in a cell and is heterologous to said cell.
With respect to claim 19, Mayers and Malcolm disclose the enzyme is diphtheria toxin. Diphtheria toxoid/toxin lack activity toward a native substrate in a cell.
With respect to claim 55, Mayers and Malcolm disclose the cross-linking moiety is between the protecting group and the enzyme.
It would be obvious to one of ordinary skill in the art to modify the compound disclosed by Mayers by replacing the carrier moiety with diphtheria toxoid/toxin and have a reasonable expectation of success. Mayers discloses a compound comprising a carrier moiety, albumin, coupled to a cell targeting agent, transferrin. Mayers discloses a cell targeting moiety includes polypeptides, viral proteins, cell surface ligands, peptides, or small molecules. Mayers further discloses the carrier moiety may include a protein or any substance that (a) is biologically compatible, (b) has a number of functional groups, and (c) has a place for linking a cell targeting agent, is useful as a carrier moiety. Malcolm discloses a carrier moiety, including albumin or diphtheria toxoid/toxin, coupled to a peptide. Malcolm discloses the diphtheria toxoid/toxin is biologically compatible and has a place for linking a peptide (or “cell targeting agent”). Moreover, it is known in the art that diphtheria toxoid/toxin is a peptide and has a number of functional groups. Thus, Malcom establishes that albumin and diphtheria toxoid/toxin both function as a carrier moiety for a cell targeting agent and that diphtheria toxoid/toxid is useful as a carrier moiety according to the aforementioned criteria disclosed by Mayers. Accordingly, the combined teachings of Mayers and Malcolm suggest that diphtheria toxoid/toxin may function as the carrier moiety in the compound disclosed by Mayers. Therefore, it is reasonable to expect the compound disclosed by Mayers may be modified by replacing the carrier moiety with diphtheria toxoid/toxin. One would have been motivated to do so because it is prima facie obvious to substitute equivalents known for the same purpose when the equivalency is recognized in the prior art. MPEP 2144.06(II) In the instant case, Malcolm recognizes albumin and diphtheria toxoid/toxin as carrier moieties suitable for coupling a targeting agent. [Malcolm, 0060] Therefore, it is obvious to substitute one known carrier moiety for the other in the art of targeting constructs. Moreover, the selection of a known material based on its suitability for its intended use is prima facie obvious. MPEP 2144.07 In the instant case, Mayers discloses any compound that meets the criteria defined above is useful as a carrier moiety. [Mayers, 0104] Malcolm discloses the diphtheria toxoid/toxin is biologically compatible and has a place for linking a peptide (or “cell targeting agent”). Furthermore, it is known in the art that diphtheria toxoid/toxin is a peptide and has a number of functional groups. Therefore, the selection of diphtheria toxoid/toxin as carrier moiety based on its suitability as a carrier moiety, as defined by Mayers, is prima facie obvious.
Claims 1-9, 11, 17-19, and 55 are rejected under 35 U.S.C. 103 as being unpatentable over Mayers, in view of Malcolm and Karaboga (US 2017/0119784 A1, Published 5/4/2017)
With respect to claim 1, Mayers discloses a compound comprising:
A protecting group (glucoside); and
A crosslinking moiety that comprises indoxyl (indoxyl conjugated to amide);
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[Mayers, Figure 13, 5220]
With respect to claim 2, Mayers discloses the protecting group is a glucoside group. [Mayers, Figure 13, 5220] A glucoside is enzymatically cleavable.
With respect to claim 5, Mayers discloses the protecting group is attached to the cross-linking moiety. [Mayers, Figure 13, 5220]
With respect to claim 8, Mayers discloses the compound further comprises a carbon chain linker. [Mayers, Figure 13, 5220]
With respect to claim 9, Mayers discloses the protecting group comprises a glucoside. [Mayers, Figure 13, 5220]
With respect to claim 11, Mayers discloses the compound comprises two protecting groups and two cross-linking moieties. [Mayers, Figure 13, 5220]
Mayers discloses the compound further comprises a carrier protein, albumin and loracarbef. [Mayers, Figure 13, 5220]
Additionally, Mayers discloses any substance that (a) is biologically compatible, (b) has a number of functional groups (e.g., amino groups, carboxyl groups, thiol groups, and the like) to which multiple platform building materials are attached, and (c) has a place for linking a cell targeting agent, is useful as a carrier moiety. Mayers discloses a carrier moiety includes for example, proteins. [Mayers, 0104]
Mayers further disclose loracarbef functions as an additional molecular structure. [Mayers, 0011, 0177] Mayers further discloses the additional molecular structure may be another carbacephem analog. [Mayers, 0011]
Mayers does not disclose the compound comprises an enzyme or a cancer cell targeting agent.
However, with respect to claim 1, Malcolm discloses diphtheria toxoid/toxin and serum albumin are both carriers that may be coupled to a peptide/antibody. [Malcolm, 0060]
Additionally, with respect to claim 1, Karaboga discloses ceftriaxone suppresses lung cancer growth by targeting Aurora B. Ceftriaxone is substituted by a sulfur-derived substituent at position 3 of the cephalosporin core and of formula (B):
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[Karaboga, 0005]
As evidenced by the structure disclosed by Karaboga, ceftriaxone is a carbacephem analog.
Modifying the compound disclosed by Mayers by replacing the carrier moiety with diphtheria toxoid/toxin and the additional molecular structure with ceftriaxone results in the compound of claim 1 and comprises:
A cell targeting moiety (ceftriaxone);
A protecting group (glucoside); and
A crosslinking moiety that comprises indoxyl (indoxyl conjugated to amide);
An enzyme (diphtheria toxoid/toxin)
Wherein, the cell targeting moiety, protecting group, and crosslinking moiety are covalently attached to the enzyme.
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[Illustration drawn by the Examiner & depicts the replacement of albumin with diphtheria toxoid/toxin and the additional molecular structure (loracarbef) with ceftriaxone]
In which case, with respect to claim 3, Mayers, Malcolm, and Karaboga disclose the protecting group is attached to the enzyme through a linker.
With respect to claim 4, Mayers, Malcolm, and Karaboga disclose the protecting group is glucoside. Glucoside protects an enzyme from enzymatic degradation.
With respect to claim 6, Mayers, Malcolm, and Karaboga the compound has a structure represented by Formula I, wherein:
CTA is the cancer cell targeting agent;
L are each an amide linking moiety;
PG is the protecting group;
X is the cross-linking moiety;
ENZ is the enzyme; and
n1, n2, n3, n4, and n7, is 1;
n5, n6, n8, and n9 is 0; and
the sum of n7, n8 and n9 is 1.
With respect to claim 7, Mayers, Malcolm, and Karaboga the compound has a structure represented by Formula II, wherein:
CTA is the cancer cell targeting agent;
L are each an amide linking moiety;
PG is the protecting group;
X is the cross-linking moiety;
ENZ is the enzyme; and
n1, n2, n3, n4, n5, and n6 is 1.
With respect to claim 17, Mayers, Malcolm, and Karaboga disclose the enzyme is diphtheria toxin. Diphtheria toxin has activity toward a substrate that is not native in a cell.
With respect to claim 18, Mayers, Malcolm, and Karaboga disclose the enzyme is diphtheria toxin. Diphtheria toxin lacks activity toward native substrates in a cell and is heterologous to said cell.
With respect to claim 19, Mayers, Malcolm, and Karaboga disclose the enzyme is diphtheria toxin. Diphtheria toxoid/toxin lack activity toward a native substrate in a cell.
With respect to claim 55, Mayers, Malcolm, and Karaboga disclose the cross-linking moiety is between the protecting group and the enzyme.
It would be obvious to one of ordinary skill in the art to modify the compound disclosed by Mayers by replacing the carrier moiety with diphtheria toxoid/toxin and have a reasonable expectation of success. Mayers discloses a compound comprising a carrier moiety, albumin, coupled to a cell targeting agent, transferrin. Mayers discloses a cell targeting moiety includes polypeptides, viral proteins, cell surface ligands, peptides, or small molecules. Mayers further discloses the carrier moiety may include a protein or any substance that (a) is biologically compatible, (b) has a number of functional groups, and (c) has a place for linking a cell targeting agent, is useful as a carrier moiety. Malcolm discloses a carrier moiety, including albumin or diphtheria toxoid/toxin, coupled to a peptide. Malcolm discloses the diphtheria toxoid/toxin is biologically compatible and has a place for linking a peptide (or “cell targeting agent”). Moreover, it is known in the art that diphtheria toxoid/toxin is a peptide and has a number of functional groups. Thus, Malcom establishes that albumin and diphtheria toxoid/toxin both function as a carrier moiety for a cell targeting agent and that diphtheria toxoid/toxid is useful as a carrier moiety according to the aforementioned criteria disclosed by Mayers. Accordingly, the combined teachings of Mayers and Malcolm suggest that diphtheria toxoid/toxin may function as the carrier moiety in the compound disclosed by Mayers. Therefore, it is reasonable to expect the compound disclosed by Mayers may be modified by replacing the carrier moiety with diphtheria toxoid/toxin. One would have been motivated to do so because it is prima facie obvious to substitute equivalents known for the same purpose when the equivalency is recognized in the prior art. MPEP 2144.06(II) In the instant case, Malcolm recognizes albumin and diphtheria toxoid/toxin as carrier moieties suitable for coupling a targeting agent. [Malcolm, 0060] Therefore, it is obvious to substitute one known carrier moiety for the other in the art of targeting constructs. Moreover, the selection of a known material based on its suitability for its intended use is prima facie obvious. MPEP 2144.07 In the instant case, Mayers discloses any compound that meets the criteria defined above is useful as a carrier moiety. [Mayers, 0104] Malcolm discloses the diphtheria toxoid/toxin is biologically compatible and has a place for linking a peptide (or “cell targeting agent”). Furthermore, it is known in the art that diphtheria toxoid/toxin is a peptide and has a number of functional groups. Therefore, the selection of diphtheria toxoid/toxin as carrier moiety based on its suitability as a carrier moiety, as defined by Mayers, is prima facie obvious.
It would be obvious to one of ordinary skill in the art to modify the compound disclosed by Mayers by replacing the additional molecular structure (loracarbef) with ceftriaxone and have a reasonable expectation of success. Mayers discloses a compound comprising an additional molecular structure, loracarbef. Mayers discloses loracarbef is a carbacephem analog but the additional molecular structure may be another carbacephem analog. Karaboga discloses ceftriaxone is a carbacephem analog. Thus, the combined teachings of Mayers and Karaboga suggest ceftriaxone may function as the additional molecular structure in the compound disclosed by Mayers. Therefore, it is reasonable to expect the compound disclosed by Mayers may be modified by replacing the additional molecular structure with ceftriaxone. One would have been motivated to do so because the selection of a known material based on its suitability for its intended use is prima facie obvious. MPEP 2144.07 In the instant case, Mayers discloses the additional molecular structure may be another carbacephem analog. Karaboga discloses ceftriaxone is a carbacephem analog. Thus, the selection of ceftriaxone based on its suitability as a carbacephem analog for its intended use as an additional molecular structure in the compound disclosed by Mayers, is prima facie obvious.
Response to Arguments
Applicant’s arguments, filed 11/17/2025, with respect to the rejection of claims 1-5, 8, 9, 12, 13, 18, and 19 over Stefano and claims 1-15 and 17 over Mayers under 35 U.S.C. § 103 have been fully considered and are persuasive. Applicant’s arguments essentially state that the prior art does not teach the limitations of the claims as amended. Therefore, the rejection has been withdrawn. However, upon further consideration, a new ground of rejection is made in view of the references cited above
Conclusion
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 KAILA A CRAIG whose telephone number is (703)756-4540. The examiner can normally be reached Monday-Friday 0800-1600.
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/K.A.C./Examiner, Art Unit 1618
/Michael G. Hartley/Supervisory Patent Examiner, Art Unit 1618