DETAILED ACTION
Claims 1, 3, 5-13, and 15 are pending.
Status of Claims
Claims 1, 3, 5-13, and 15 are pending. Claims 1, 3, 6, and 9 have been amended. Claim 15 has been newly added.
Claims 1, 3, 5-13, and 15 are under examination.
Information Disclosure Statement
The information disclosure statement (IDS) filed on 11/04/2025 has been considered by the examiner.
Withdrawn Claim Objections and/or Rejections
The arguments filed on 11/04/2025 have been considered by the examiner.
The claim interpretations 112(f) of claims 6 and 9 as set forth on pp. 3-5 of the previous office action (mailed on 06/27/205) has been withdrawn in view of the amended claims (filed on 11/04/2025).
The rejection of claims 2-3, 6, 9, 11, and 13 under 35 USC 112(b) for being indefinite as set forth on pp. 5-6 of the previous office action (mailed on 06/27/205) has been withdrawn in view of the amended and cancelled claims (filed on 11/04/2025).
The rejection of claims 1-7 and 10-12 under 35 USC 102(a)(1) as being anticipated by Meschendoerfer et al., as set forth on pp. 7-16 of the previous office action (mailed on 06/27/205) has been withdrawn in view of the amended and cancelled claims (filed on 11/04/2025).
The rejection of claims 13-14 under 35 USC 103 as being unpatentable over Meschendoerfer et al., as set forth on pp. 17-19 of the previous office action (mailed on 06/27/205) has been withdrawn in view of the amended and cancelled claims (filed on 11/04/2025).
The rejection of claims 8-9 under 35 USC 103 as being unpatentable over Meschendoerfer and Duerr et al., as set forth on pp. 19-22 of the previous office action (mailed on 06/27/205) has been withdrawn in view of the amended and cancelled claims (filed on 11/04/2025).
Claim Rejections - 35 USC § 103
New 103 rejection Necessitated by Amendment
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.
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, 3, 5-7, 10-13, and 15 are rejected under 35 U.S.C. 103 as being unpatentable over Meschendoerfer, W et al. “SPR-based assays enable the full functional analysis of bispecific molecules.” Journal of pharmaceutical and biomedical analysis vol. 132 (2017): 141-147. doi:10.1016/j.jpba.2016.09.028 (IDS filed on 04/17/2023), in view of Nicoya Lifesciences “Reducing Non-Specific Binding in Surface Plasmon Resonance Experiments”. SPR Tips- 4 Ways to Reduce Non-Specific Binding in Surface Plasmon Resonance Experiments. 23. Nov. 2015.
Instant claim 1 recites “A method for determining the binding of an antibody, which comprises a first binding site specifically binding to a first antigen and a second binding site specifically binding to a second antigen, to said first and said second antigen, wherein the method comprises the following steps: a) capturing the antibody on a solid phase using a capture reagent specifically binding to a constant domain of the antibody, b) incubating the captured antibody with the first or the second antigen in a buffer comprising 1 mM KH2PO4, 10 mM Na2HPO4, 137 mM NaCl, 2.7 mM KCl pH 7.4, and 0.05% Tween-20 (PBS-T) and 300 mM NaCl to form a captured antibody-antigen complex and determining a first binding signal, c) either incubating the captured antibody-antigen complex with the antigen not used for the formation of the captured antibody-antigen complex to form a captured antibody-antigen-antigen complex and determining a second binding signal, or regenerating the surface, capturing the antibody on a solid phase using a capture reagent specifically binding to a constant domain of the antibody, incubating the captured antibody with the antigen not used for the formation of the captured antibody-antigen complex in step b) to form a captured antibody-antigen complex and determining a third binding signal, and d) determining the overall binding of the antibody or individual binding of each binding site of the antibody to the first and the second antigen from the first binding signal and the second or third binding signal, wherein the solid phase is a surface plasmon resonance chip, the first binding signal is a surface plasmon resonance response, and the second binding signal is a surface plasmon resonance response”.
Instant claim 3 recites “A method for determining overall and individual binding of an antibody, which comprises a first binding site specifically binding to a first antigen and a second binding site specifically binding to a second antigen, to said first and said second antigen, wherein the method comprises the following steps:- capturing the antibody on a solid phase using a capture reagent specifically binding to a constant region of the antibody,- incubating the captured antibody with the first or second antigen in a buffer comprising 1 mM KH2PO4, 10 mM Na2HPO4, 137 mM NaCl, 2.7 mM KCl pH 7.4, and 0.05% Tween-20 (PBS-T) and 300 mM NaCl to form an immobilized antibody-antigen complex,- incubating the captured antibody-antigen complex with the antigen not used for the formation of the captured antibody-antigen complex in a buffer comprising PBS-T and 300 mM NaCl to form a captured antibody-antigen-antigen complex, and - determining the individual binding of each binding site of the antibody to the first and the second antigen, and based on this, also the overall binding of the antibody to the first and the second antigen based on the individual binding of each binding site, if the formation of the captured antibody-antigen complex results in a first binding signal and the formation of the captured antibody-antigen-antigen complex results in a second binding signal that is increased with respect to the first binding signal, wherein the solid phase is a surface plasmon resonance chip, the first binding signal is a surface plasmon resonance response, and the second binding signal is a surface plasmon resonance response.”.
Instant claim 15 recites “A method for determining the binding of an antibody, which comprises a first binding site specifically binding to a first antigen and a second binding site specifically binding to a second antigen, to said first and said second antigen, wherein the method comprises the following steps:a) capturing the antibody on a solid phase using a capture reagent specifically binding to a constant domain of the antibody,b) incubating the captured antibody with the first or the second antigen in a buffer comprising 1 mM KH2PO4, 10 mM Na2HPO4, 137 mM NaCl, 2.7 mM KCl pH 7.4, and 0.05% Tween-20 (PBS-T) and 300 mM NaCl to form a captured antibody-antigen complex and determining a first binding signal,c) either incubating the captured antibody-antigen complex with the antigen not used for the formation of the captured antibody-antigen complex to form a captured antibody-antigen-antigen complex and determining a second binding signal,o r regenerating the surface, capturing the antibody on a solid phase using a capture reagent specifically binding to a constant domain of the antibody, incubating the captured antibody with the antigen not used for the formation of the captured antibody-antigen complex in step b) to form a captured antibody-antigen complex and determining a third binding signal, and d) determining the overall binding of the antibody or individual binding of each binding site of the antibody to the first and the second antigen from the first binding signal and the second or third binding signal if, i) the formation of the captured antibody-antigen complex results in a first binding signal and ii) the formation of the captured antibody-antigen-antigen complex or the formation of the captured antibody-antigen complex after regeneration results in a second or third binding signal that is increased with respect to the first binding signal, wherein the solid phase is a surface plasmon resonance chip, the first binding signal is a surface plasmon resonance response, and the second binding signal is a surface plasmon resonance response”.
Meschendoerfer teaches a method for determining the binding of an antibody, which comprises a first binding site specifically binding to a first antigen and a second binding site specifically binding to a second antigen, to said first and said second antigen (see abstract “The increasing complexity of novel biotherapeutics such as bispecific antibodies or fusion proteins raises new challenges for functional characterization. When compared to standard antibodies, two individual interactions and the inter-dependency of binding events need to be considered for bispecific antibodies. We have previously described an SPR-based assay setup, which enables us to assess the binding activity of a bivalent-bispecific molecule to both targets simultaneously and − in addition to one individual target− in a single setup…Comparison of data between the assays showed that simultaneous binding can be calculated based on both individual readouts, and revealed a good correlation. Hence, both SPR-based assay principles allow a “full” functional analysis of a bispecific. CrossMab in only one assay. The assay principles can be qualified and enable an efficient drug development”, see figure 1), wherein the method comprises the following steps:
a) capturing the antibody on a solid phase using a capture reagent specifically binding to a constant domain of the antibody (see figure 1 showing capturing the antibody (crossmab: bivalent antibody) on a solid phase (CM5 biosensor chip) using a capture reagent (capturing anti-human Fab antibody) specifically binding to the constant domain (Fc) of the antibody, see page 142 ““Capturing anti-human Fab antibody (Human Fab Capture Kit, GE Healthcare) was immobilized on the surface of a CM5 biosensor chip using the provided amine coupling chemistry from GE Healthcare. Flow cells were activated with a 1:1 mixture of 0.4 M1-ethyl-3-(3-dimethylaminopropyl)-carbodiimide (EDC) and 0.1MN- hydroxysuccinimide (NHS) at a flow rate of 5 µl/min. Anti-human Fab antibody was injected in sodium acetate, pH 5.0 at15 µg/ml for 420 s, which resulted in a surface density of approximately 6000 RU.”);
b) incubating the captured antibody with the first or the second antigen in a buffer comprising 1 mM KH2PO4, 10 mM Na2HPO4, 137 mM NaCl, 2.7 mM KCl pH 7.4, and 0.05% Tween-20 (PBS-T) to form a captured antibody-antigen complex and determining a first binding signal (see figure 6, see page 145 “To demonstrate that the assay is specific and loss-of-function indicating, an isotype control and two differently stressed Cross-Mabs were measured as shown in Fig. 5. In order to assess the loss-of-function properties of the assay, CrossMab samples were incubated for moderate or accelerated stress… Fig. 6 shows data that correspond to six different samples(A–F). A decrease of binding for CrossMabs incubated at various stress conditions was detected in both assays. The SPR-based dual-binding assay measures the interaction of both individual targets (VEGFA-121 and Ang2), whereas the SPR-based bridging assays addresses binding to both targets (overall), and in addition, one individual interaction (VEGFA-121). In case of independent damage, the third not directly measured interaction from each assay principle can be derived from the two analyzed interactions as shown in Eq. (1) allowing the Ang2 signal calculation for the bridging assay, and Eq. (2) enabling overall signal calculation for the dual-binding assay”, see page 142 “The bispecific antibodies were diluted in PBS-T (1 mM KH2PO4, 10 mMNa2HPO4, 137 mM NaCl, 2.7 mM KCl pH 7.4, 0.05% Tween20, Roche Diagnostics GmbH) and injected on the second flow cell at various concentrations for 90 s at a flow rate of 10 µl/min.”);
c) incubating the captured antibody-antigen complex with the antigen not used for the formation of the captured antibody-antigen complex to form a captured antibody-antigen-antigen complex and determining a second binding signal (see figure 1. Figure 1 shows incubating the capture antibody antigen complex with the antigen not used (VEGF) for formation of the captured antigen-antibody complex, and determining the second binding signal (Biacore will determine the binding signal throughout the assay; see figure 2A), See page 145: Fig. 6 shows data that correspond to six different samples(A–F). A decrease of binding for Cross Mabs incubated at various stress conditions was detected in both assays. The SPR-based dual-binding assay measures the interaction of both individual targets (VEGFA-121 and Ang2), whereas the SPR-based bridging assays addresses binding to both targets (overall), and in addition, one individual interaction (VEGFA-121).”);
d) determining the overall binding of the antibody or individual binding of each binding site of the antibody to the first and the second antigen from the first binding signal and the second or third binding signal, wherein the solid phase is a surface plasmon resonance chip, the first binding signal is a surface plasmon resonance response, and the second binding signal is a surface plasmon resonance response (see figure 1. Figure 1 shows determining the second binding signal (Biacore will determine the binding signal throughout the assay; see figure 2A), See figure 2A, See figure 4, See page 142: “The comparison of assay results should allow us to understand the
contributions of individual activities to the overall signal in both assays”) (instant claims 1, 3, and 15).
Meschendoerfer teaches determining the overall binding of the antibody or individual binding of each binding site of the antibody to the first and the second antigen from the first binding signal and the second or third binding signal if, i) the formation of the captured antibody-antigen complex results in a first binding signal and ii) the formation of the captured antibody-antigen-antigen complex or the formation of the captured antibody-antigen complex after regeneration results in a second or third binding signal that is increased with respect to the first binding signal, wherein the solid phase is a surface plasmon resonance chip, the first binding signal is a surface plasmon resonance response, and the second binding signal is a surface plasmon resonance response (see figure 1 showing determining the second binding signal (Biacore will determine the binding signal throughout the assay. See figure 2A, see figure 4, see page 142 “The comparison of assay results should allow us to understand the
contributions of individual activities to the overall signal in both assays”) (instant claim 15).
Meschendoerfer teaches wherein the antibody is a bispecific antibody that is bispecific IgG antibody comprising a first Fab fragment and a second Fab fragment, or an antibody comprising two non-overlapping paratopes in a complimentary pair of a VH and a VL domain (see abstract “Hence, both SPR-based assay principles allow a “full” functional analysis of a bispecific CrossMab in only one assay.”, see figure 1 showing capturing the antibody (crossmab; bivalent antibody) on a solid phase (CM5 biosensor chip) using a capture reagent (capturing anti -human Fab antibody) specifically binding to the constant domain (Fc) of the antibody, see page 142 “All SPR experiments were performed on a BIAcore©T200 instrument (GE Healthcare) at 25◦C. VEGFA-121, Ang2, both CrossMabs and all used control antibodies were manufactured in house (RocheDiagnostics GmbH).”. It is known in the art that a CrossMab is a bispecific IgG antibody that contains two Fab fragments”) (instant claims 5-6). Meschendoerfer teaches the capture reagent is an anti-Fab antibody (see figure 1, see page 143 “Capturing anti-human Fab antibody (Human Fab Capture Kit, GE Healthcare) was immobilized on the surface of a CM5 biosensor chip using the provided amine coupling chemistry from GEHealthcare.”) (instant claim 7). Meschendoerfer teaches wherein the capturing is by injecting the antibody for about 60 seconds at a flow rate of about 5 µL/min, and at a concentration of 0.6 µg/mL to 10 µg/mL (see page 142 “Capturing anti-human Fab antibody (Human Fab Capture Kit, GE Healthcare) was immobilized on the surface of a CM5 biosensor chip using the provided amine coupling chemistry from GE Healthcare. Flow cells were activated with a 1:1 mixture of 0.4 M1-ethyl-3-(3-dimethylaminopropyl)-carbodiimide (EDC) and 0.1MN-hydroxysuccinimide (NHS) at a flow rate of 5 µl/min… Ang2 was injected for 60 s with a concentration of 1.1 µg/ml followed by an injection of 1.4 µg/ml VEGFA-121 for 60 s over both flow cells.”) (instant claims 10-11).
Meschendoerfer teaches wherein the incubating is by an injection of the respective antigen at a concentration of 2 µg/mL for about 60 seconds (see “Ang2 was injected for 60 s with a concentration of 1.1 µg/ml followed by an injection of 1.4 µg/ml VEGFA-121 for 60 s over both flow cells.”.) (instant claims 12-13). Meschendoerfer does not explicitly teach a concentration of 2 µg/mL. Meschendoerfer teaches an injection concentration that is substantially similar and on the same order of magnitude to that which is claimed. The art is therefore supporting this is an appropriate concentration, one suitable for this type of assay. Absent evidence of unexpected results, it would have been prima facie obvious to have arrived at the claimed concentration (2 µg/mL) as an obvious matter of routine optimization, namely performing routine experimentation to determine the optimum or workable
concentration for the assay. In general, differences in concentration or temperature will not support the patentability of subject matter encompassed by the prior art unless there is evidence indicating such concentration or temperature is critical. "[W]here the general conditions of a claim are disclosed in the prior art, it is not inventive to discover the optimum or workable ranges by routine experimentation." In re Aller, 220 F.2d 454, 456, 105 USPQ 233, 235 (CCPA 1955). See also MPEP §2144.05.
Meschendoerfer does not teach the use of 300 mN NaCl.
Nicoya teaches the use of PBS-T (also referred to as tween 20 buffer) and 300 mM of NaCl (see page 2 under materials and equipment, see page 8 “Results are shown in Figure 12 and indicate a dramatic reduction at aII lgG concentrations tested, with essentially no non-specific binding observed. Similar results were demonstrated in an experiment performed at 300 mM NaCl”) (instant claims 1, 3, and 15).
It would have been obvious to one of ordinary skill in the art at the time of the instant application to combine the SPR-based method for determining the binding of an antibody of Meschendoerfer with the methods of reducing non-specific binding in surface plasmon resonance experiments with PBS-T and 300 mM of NaCl taught by Nicoya. Nicoya provides motivation by teaching that the use of PBS-T and 300 mM NaCl completely prevents non-specific binding (see table 1). Nicoya provides motivation by teaching that the prevention of non-specific binding is critical when performing any SPR experiment (see page 9). The artisan would have had reasonable expectation of success based on the cumulative disclosures of these prior art references.
Claims 8-9 are rejected under 35 U.S.C. 103 as being unpatentable over Meschendoerfer and Nicoya as applied to claims 1, 3, 5-7, 10-13, and 15 above, and in view of Duerr et al., (US20140017244) (IDS filed on 04/17/2023).
The teachings of Meschendoerfer and Nicoya as it pertains to claims 1, 3, 5-7, 10-13, and 15 is discussed in the 35 USC 103 rejection above.
Meschendoerfer teaches the solid phase is a surface plasmon resonance chip (See figure 1. Figure 1 shows capturing the antibody (crossmab; bivalent antibody) on a solid phase (CM5 biosensor chip) using a capture reagent (capturing anti -human Fab antibody) specifically binding to the constant domain (Fc) of the antibody),
the first binding signal is a surface plasmon resonance response and the second binding signal is a surface plasmon resonance response. (See page 141 “SPR (surface plasmon resonance) is a biosensor-based technology to measure real time protein-protein interaction. SPR technology has become a standard tool in biopharmaceutical research and development [4–8], and is commonly employed to determine binding constants for macromolecular interactions… we have described an SPR based assay principle enabling us to assess the binding activity of a bispecific Ang-2/VEGF antibody to both of its targets in parallel…we have developed another SPR-based assay principle, called dual-binding assay.”, see figure 2-4) (instant claim 9).
Meschendoerfer does not teach the antibody being an antibody that comprises two non-overlapping paratopes in a complementary pair of a VH and a VL domain, nor does Meschendoerfer teach the capture reagent being an anti-kappa-light chain antibody or an anti-lambda light chain antibody.
Duerr teaches the antibody being an antibody that comprises two non-overlapping paratopes in a complementary pair of a VH and a VL domain (see [0003]: “The present invention relates a method for the reduction of the viscosity of an antibody (including a bispecific antibody) of human IgG1 or human IgG4 subclass, to bispecific antibodies against human vascular endothelial growth factor (VEGF/VEGF-A) and against human angiopoietin-2 (ANG-2), methods for their production, pharmaceutical compositions containing said antibodies, and uses thereof.”, see [0014]), and the capture reagent being an anti-kappa-light chain antibody or an anti- lambda light chain antibody (see [0169] “In one embodiment the recovering step under c includes the use of a light chain constant domain specific capture reagent (which e.g. specific for the kappa or the lambda constant light chain, depending on whether a kappa or a lambda light chain in the bispecific antibody according to invention used). In one embodiment this light chain specific capture reagent is used in a bind-and-elute-mode). Examples of such light chain
constant domain specific capture reagents are e.g. KappaSelect™ and LambdaFabSelect™ from GE Healthcare/BAC, which are based on a highly rigid agarose base matrix that allows high flow rates and low back pressure at large scale. They feature a ligand that binds to the constant region of the kappa or the lambda light chain respectively (i.e. fragments lacking the constant region of the light chain will not bind; FIG. 1). Both are therefore capable of binding other target molecules containing the constant region of the light chain, for example, IgG, IgA and IgM. The ligands are attached to the matrix via a long hydrophilic spacer arm to make it easily available for binding to the target molecule. They are based on a single-chain antibody fragment that is screened for either human Ig kappa or lambda.”) (instant claims 8- 9).
It would have been obvious to one of ordinary skill in the art at the time of the instant
application to considerer combining Meschendoerfer’s methods of determining the binding of an antibody using SPR-based methods with Duerr’s teachings of anti-Fab antibody being an anti-kappa-light chain antibody or an anti-lambda-light-chain antibody and the use of a DutaFab (an antibody that comprises two non-overlapping paratopes in a complementary pair of a VH and a VL domain) because they both teach methods of SPR assays. Duerr provides motivation by teaching that these the bivalent antibodies (CrossMab) discussed above are known to bind to anti-kappa or anti-lambda (See [0169]). Thus, teaching that at the time of the instant application, it was known in the art that anti-lambda and/or anti-kappa will bind to CrossMab’s. One of ordinary skill in the art would have had reasonable expectation of success because they both teach detecting bispecific molecules with SPR-based methods. The artisan would have had reasonable expectation of success based on the cumulative disclosures of these prior art references.
Response to Arguments
Applicant's arguments filed on 11/04/2025 have been fully considered but they are not persuasive.
On pp. 11-12 applicant argues that Meschendoerfer doesn’t teach PBS-T and 300mnM NaCl. Applicant argues that Meschendoerfer only teaches the use of PBS-T to dilute bispecific antibodies, not in connection with the SPR assay in their experiment.
Meschendoerfer teaches the use of PBS-T and 137 mM of NaCl. In general, differences in concentration or temperature will not support the patentability of subject matter encompassed by the prior art unless there is evidence indicating such concentration or temperature is critical. "[W]here the general conditions of a claim are disclosed in the prior art, it is not inventive to discover the optimum or workable ranges by routine experimentation." In re Aller, 220 F.2d 454, 456, 105 USPQ 233, 235 (CCPA 1955). See also MPEP §2144.05. One of ordinary skill in the art would have considered optimizing the concentration of the antibody solution, in the method of Meschendoerfer, because concentrations of solutions to sensors are routinely optimized.
Meschendoerfer teaches the use of PBS-T and NaCl to dilute bispecific antibodies, but it is in connection with the SPR assay. Bispecific antibodies are diluted before SPR assays. The instant specification teaches that the PBS-T and NaCl are buffers that are used as dilutants (see pages 4 and 14 of specification, see example 1 on page 18 of the specification). Meschendoerfer teaches diluting the bispecific antibodies before doing the SPR assay (see page 142).
Further, Nicoya specifically teaches using PBS-T and 300 mM NaCl as SPR buffers (see page 2 under materials and equipment, see page 8 “Results are shown in Figure 12 and indicate a dramatic reduction at aII lgG concentrations tested, with essentially no non-specific binding observed. Similar results were demonstrated in an experiment performed at 300 mM NaCl”).
On p. 13 applicant argues that Duerr does not teach or suggest adding 300 mM NaCl (or anything similar) in the PBS solution used in connection with the surface plasmon resonance (SPR) experiments.
However, Meschendoerfer and Nicoya teach the use of PBS-T and NaCl in connection with SPR experiments. Duerr teaches the anti-Fab antibody being a anti- kapa-light-chain antibody or a anti- lambda-light-chain antibody and the antibody being an antibody that comprises two non-overlapping paratopes in a complementary pair of a VH and a VL domain.
Conclusion
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.
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/MCKENZIE A DUNN/Examiner, Art Unit 1678
/GREGORY S EMCH/Supervisory Patent Examiner, Art Unit 1678