DETAILED ACTION
The amendment and RCE filed on 03/11/2026 has been entered and fully considered. Claims 1-20 are pending, of which claims 51-10 are amended.
Response to Amendment
In response to amendment, the examiner maintains rejection over the prior art established in the previous Office action.
Notice of Pre-AIA or AIA Status
The present application, filed on or after March 16, 2013, is being examined under the first inventor to file provisions of the AIA .
Double Patenting
The nonstatutory double patenting rejection is based on a judicially created doctrine grounded in public policy (a policy reflected in the statute) so as to prevent the unjustified or improper timewise extension of the “right to exclude” granted by a patent and to prevent possible harassment by multiple assignees. A nonstatutory double patenting rejection is appropriate where the conflicting claims are not identical, but at least one examined application claim is not patentably distinct from the reference claim(s) because the examined application claim is either anticipated by, or would have been obvious over, the reference claim(s). See, e.g., In re Berg, 140 F.3d 1428, 46 USPQ2d 1226 (Fed. Cir. 1998); In re Goodman, 11 F.3d 1046, 29 USPQ2d 2010 (Fed. Cir. 1993); In re Longi, 759 F.2d 887, 225 USPQ 645 (Fed. Cir. 1985); In re Van Ornum, 686 F.2d 937, 214 USPQ 761 (CCPA 1982); In re Vogel, 422 F.2d 438, 164 USPQ 619 (CCPA 1970); In re Thorington, 418 F.2d 528, 163 USPQ 644 (CCPA 1969).
A timely filed terminal disclaimer in compliance with 37 CFR 1.321(c) or 1.321(d) may be used to overcome an actual or provisional rejection based on nonstatutory double patenting provided the reference application or patent either is shown to be commonly owned with the examined application, or claims an invention made as a result of activities undertaken within the scope of a joint research agreement. See MPEP § 717.02 for applications subject to examination under the first inventor to file provisions of the AIA as explained in MPEP § 2159. See MPEP § 2146 et seq. for applications not subject to examination under the first inventor to file provisions of the AIA . A terminal disclaimer must be signed in compliance with 37 CFR 1.321(b).
The filing of a terminal disclaimer by itself is not a complete reply to a nonstatutory double patenting (NSDP) rejection. A complete reply requires that the terminal disclaimer be accompanied by a reply requesting reconsideration of the prior Office action. Even where the NSDP rejection is provisional the reply must be complete. See MPEP § 804, subsection I.B.1. For a reply to a non-final Office action, see 37 CFR 1.111(a). For a reply to final Office action, see 37 CFR 1.113(c). A request for reconsideration while not provided for in 37 CFR 1.113(c) may be filed after final for consideration. See MPEP §§ 706.07(e) and 714.13.
The USPTO Internet website contains terminal disclaimer forms which may be used. Please visit www.uspto.gov/patent/patents-forms. The actual filing date of the application in which the form is filed determines what form (e.g., PTO/SB/25, PTO/SB/26, PTO/AIA /25, or PTO/AIA /26) should be used. A web-based eTerminal Disclaimer may be filled out completely online using web-screens. An eTerminal Disclaimer that meets all requirements is auto-processed and approved immediately upon submission. For more information about eTerminal Disclaimers, refer to www.uspto.gov/patents/apply/applying-online/eterminal-disclaimer.
Claim 1-20 are rejected on the ground of nonstatutory double patenting as being unpatentable over claim 1-20 of U.S. Patent No. 12,169,203. Although the claims at issue are not identical, they are not patentably distinct from each other because both the instant claims and the currently patented claims expressly recite the same subject matter, it would have been obvious to one of ordinary skill in the art at the time the invention was made to employ both device and methods, as recited in both sets of claims.
Claim Rejections - 35 USC § 103
The text of those sections of Title 35, U.S. Code not included in this action can be found in a prior Office action.
Claim(s) 1-3 and 6-9 is/are rejected under 35 U.S.C. 103 as being unpatentable over Haselberg et al. (Analytica Chimica Acta, 2018, IDS) (Haselberg) in view of Redman et al (Analytical Chemistry, 2016, IDS) (Redman), Francois et al. (Analytica Chimica Acta, 2016) (Francois), applicant admitted prior art and Chames et al. (mAbs, 2009, IDS) (Chames).
Regarding claim 1, Haselberg teaches a method for characterizing a monospecific antibody in a mixture of a bispecific antibody and its monospecific antibody side products, in the context of post translational modification variants, charge variants and size variants of an antibody of interest (page 182, par 1) comprising:
separating a mixture of a bispecific antibody and its monospecific antibody side products by molecular weight and/or charge in one or more capillaries using capillary electrophoresis (page 183, par 4);
eluting the separated antibody and antibody side products from the one or more capillaries (page 183, par 4); and
determining the mass of the eluted antibody and antibody side products using mass spectrometer (page 183, par 4), thereby characterizing a charge variant of the monospecific antibody (Table 3, Fig. 5, page 185, 189);
wherein, the one or more capillaries are coupled to the mass spectrometer (CE-MS) (page 183, par 4); and
the charge variant of the monospecific antibody comprises a deamidation and glycosylation (page 183, par 1, page 184, par 3),
wherein the capillary electrophoresis is in an integrated microfluidic platform (CE-MS) (page 183, par 4),
Microfluidics refers to the behavior, precise control, and manipulation of fluids that are geometrically constrained to a small scale (typically sub-millimeter) at which surface forces dominate volumetric forces. In this case, capillary electrophoresis precisely control, and manipulate fluids that are geometrically constrained to a small scale (e.g. 30 μm i.d.) capillary channel at which surface forces dominate volumetric forces. Therefore, capillary electrophoresis is considered microfluidics. It is noted that claim 1 only requires capillary electrophoresis being in the microfluidic platform. Haselberg teaches that “Sheathless integrated capillary electrophoresis electrospray ionization was carried out on a Sciex CESI 8000 instrument.” (page 183, par 4). Thus, the microfluidic capillary electrophoresis is in the microfluidic platform of CE-ESI in Haselberg, Therefore, Haselberg meets the claim.
Haselberg does not specifically teach that the microfluidic capillary electrophoresis is integrated in a larger microfluidic platform. However, Redman teaches using a microfluidic capillary electrophoresis integrated in a larger microfluidic platform for detecting and/or discriminating between post-translational modification variants of an antibody of interest in a sample (abstract). Redman teaches that the larger integrated microfluidic platform uses very little sample preparation (page 2221, par 1). At time before the filing, it would have been obvious to one of ordinary skill in the art to integrate the microfluidic CE-ESI of Heaselberg into a larger microfluidic platform, in order to use less sample.
Haselberg describes intact monoclonal antibody separation by CE followed by MS for identification of clipped species and glycoforms without denaturation, demonstrating that native antibody forms and their variants can be separated and identified using CE-MS (page 186, par 1).
“CE-MS for the detection and assignment of native and clipped mAb forms and their glycoforms” (page 186, par 1).
Haselberg does not expressly teach that the microfluidic capillary electrophoresis is under native conditions. However, Francois teaches that microfluidic capillary electrophoresis is under native conditions (page 170, par 6). Francois teaches that the native condition enables the MS analysis under native state and allow precise middle-up characterization of Fc/2 variant of antibody (abstract). Francois expressly demonstrates maintaining non-covalent protein complexes during CE-MS analysis by using 25 mM ammonium acetate, a well-established native buffer:
“a last study consisted to infuse the same sample in condition classically described… as native conditions… 25 mM ammonium acetate at pH 6.8 was selected… This confirms the presence of Fc/2 dimers in native conditions….” (page 175, par 0).
Here, Francois shows preservation of noncovalent Fc/2 dimer interactions under CZE buffer conditions, Maintaining noncovalent subunit association during CE-MS. Constitutes “maintaining the antibody in native conditions,” as claimed.
Thus, it would have been obvious to one of ordinary skill in the art to carry out microfluidic capillary electrophoresis under native conditions, in order to do the MS analysis under native state and allow precise middle-up characterization of Fc/2 variant of antibody.
Applicant admits that integrated microfluidic CE-MS chip running in native condition is well-known in the art. In particular, the instant specification admits that “The intact mass analysis of antibody and its charge variants was conducted using Zipchip CE interface (908 Devices) coupled to Exactive Plus EMR Obitrap mass spectrometer (Thermo Scientific). Antibody charge variants were separated on Native microfluidic HRN chip (22 cm separation channel, 908 Devices) with Native background electrolyte (BGE), pH -5.5 (908 Devices).” (par [00108]). Device. 908 Device is a commercial company. It would have been obvious to one of ordinary skill in the art to use integrated microfluidic CE-MS chip in Haselberg’s method and run CE under native condition, in order to save sample and obtain more accurate result.
Haselberg clearly teaches analytical workflows for antibody heterogeneity (title, abstract), which would have been recognized by a POSITA as applicable to any antibody product, including bsAbs and their monoclonal side products.
Haselberg does not specifically teach that wherein the antibody of interest comprises a bispecific antibody. Chames teaches bispecific antibodies for cancer therapy (title). Chames teaches that bispecific antibodies (bsAbs) had become an important therapeutic modality, noting that clinical trials “are finally providing exciting results, with the most impressive ones being delivered by triomab and BiTE molecules,” and that bsAbs represent “a real leap in terms of therapeutic efficiency. For the first time, the possibility of actually curing patients using antibodies seems within reach.” (page 545, par 2).
Therefore, Chames not only discloses the existence of bispecific antibodies, but explicitly emphasizes their growing therapeutic importance and success in clinical development, thereby providing a clear motivation to apply known intact-protein CE-MS analytical methods to ensure bsAb structural integrity and to distinguish correctly assembled products from monospecific antibody side-products, as required for clinical quality control.
Such recognition in the art would have strongly motivated a person of ordinary skill to apply established analytical techniques for monoclonal antibody quality assessment, such as the CE-MS workflows taught by Haselberg and Francois, to bispecific antibody products — including the identification of mispaired monospecific side products that can arise during bsAb manufacturing.
At time before the filing it would have been obvious to one of ordinary skill in the art to apply Haselberg’s method for analyzing bispecific antibodies for cancer therapy, in order to have a quality control for the antibody drugs.
Regarding claim 2, Haselberg teaches that the method further comprising determining a relative or absolute amount of the charge variant of the monospecific antibody in the mixture (Fig. 5, page 187, par 1).
Regarding claim 3, Haselberg does not specifically teach that wherein the mixture includes an internal standard. However, using an internal standard for quantity calibration in MS is a well-known conventional method.
Regarding claim 6, Haselberg teaches that wherein the monospecific antibody is of isotype IgG 1, IgG2, IgG3, IgG4, or mixed isotype (page 185, par 0-2).
Regarding claim 7, it is conventional to further comprising characterizing a second monospecific antibody in the mixture.
Regarding claim 8-9, it would have been obvious to one of ordinary skill in the art to optimize the injection volume in the one or more capillaries by routine experimentation.
Claim 4-5 is/are rejected under 35 U.S.C. 103 as being unpatentable over Haselberg in view of Redman, Francois, applicant admitted prior art and Chames as applied to claims 1-3 and 6-9 above, and further in view of Dolnik (US 2010/0187113, IDS).
Regarding claim 4, Haselberg does not specifically teach that wherein the one or more capillaries comprise a separation matrix. Dolnik teaches capillaries comprise a separation matrix for separation of monoclonal antibodies (par [0128]). Dolnik teaches that “The sieving matrix enables size separation of proteins. It provides obstacles in the migration path and makes proteins complexed with cationic surfactants to electrophoretically migrate according to their size” (par [0105]). At time before the filing it would have been obvious to one of ordinary skill in the art to include a separation matrix in the capillary electrophoresis, in order to enable size separation
Regarding claim 5, Dolnik teaches that wherein the separating comprises a sieving matrix configured to separate proteins by molecular weight (par [0105]).
Claim(s) 10-14 and 16 is/are rejected under 35 U.S.C. 103 as being unpatentable over Haselberg et al. (Analytica Chimica Acta, 2018, IDS) (Haselberg) in view of Francois et al. (Analytica Chimica Acta, 2016) (Francois).
Regarding claim 10, Haselberg teaches a method for characterizing an antibody of interest in a co-formulated drug (antibody-based pharmaceuticals) (abstract), the method comprising:
separating antibodies within the co-formulated drug in one or more capillaries using capillary electrophoresis to form a separated antibody mixture, wherein the antibodies within the co-formulated drug are separated based on mass and/or charge (page 183, par 4);
eluting the separated antibody mixture from the one or more capillaries (page 183, par 4); and
determining a mass of a charge variant of the antibody of interest using a mass spectrometer coupled to the one or more capillaries (CE-MS) (Table 3, Fig. 5, page 183, par 4, page 185, 189);
wherein the charge variant comprises a deamidation, an oxidation, a glycation, a disulfide formation, a high mannose glycosylation, or an O-glycosylation (page 183, par 1, page 184, par 3)
Microfluidics refers to the behavior, precise control, and manipulation of fluids that are geometrically constrained to a small scale (typically sub-millimeter) at which surface forces dominate volumetric forces. In this case, capillary electrophoresis precisely control, and manipulate fluids that are geometrically constrained to a small scale (e.g. 30 μm i.d.) capillary channel at which surface forces dominate volumetric forces. Therefore, capillary electrophoresis is considered microfluidics. It is noted that claim 1 only requires capillary electrophoresis being in the microfluidic platform. Haselberg teaches that “Sheathless integrated capillary electrophoresis electrospray ionization was carried out on a Sciex CESI 8000 instrument.” (page 183, par 4). Thus, the microfluidic capillary electrophoresis is in the microfluidic platform of CE-ESI in Haselberg, Therefore, Haselberg meets the claim.
Haselberg describes intact monoclonal antibody separation by CE followed by MS for identification of clipped species and glycoforms without denaturation, demonstrating that native antibody forms and their variants can be separated and identified using CE-MS (page 186, par 1).
“CE-MS for the detection and assignment of native and clipped mAb forms and their glycoforms” (page 186, par 1).
Haselberg does not expressly teach that the microfluidic capillary electrophoresis is under native conditions. However, Francois teaches that microfluidic capillary electrophoresis is under native conditions (page 170, par 6). Francois teaches that the native condition enables the MS analysis under native state and allow precise middle-up characterization of Fc/2 variant of antibody (abstract). Francois expressly demonstrates maintaining non-covalent protein complexes during CE-MS analysis by using 25 mM ammonium acetate, a well-established native buffer:
“a last study consisted to infuse the same sample in condition classically described… as native conditions… 25 mM ammonium acetate at pH 6.8 was selected… This confirms the presence of Fc/2 dimers in native conditions….” (page 175, par 0).
Here, Francois shows preservation of noncovalent Fc/2 dimer interactions under CZE buffer conditions, Maintaining noncovalent subunit association during CE-MS. Constitutes “maintaining the antibody in native conditions,” as claimed.
Thus, it would have been obvious to one of ordinary skill in the art to carry out microfluidic capillary electrophoresis under native conditions, in order to do the MS analysis under native state and allow precise middle-up characterization of Fc/2 variant of antibody.
Regarding claim 11, Haselberg teaches that the method further comprising determining a relative or absolute amount of the antibody of interest in the co-formulated drug (Fig. 6, page 189, par 2).
Regarding claim 12, Haselberg teaches that wherein the antibody of interest is a first antibody of interest, the co-formulated drug includes a second antibody of interest, and the method further comprises determining a relative or absolute amount of the first antibody of interest in the coformulated drug and determining a relative or absolute amount of the second antibody of interest in to the co-formulated drug (Fig. 6, page 189, par 2).
Regarding claim 13, Haselberg teaches that wherein the antibody of interest is a contaminant of the co-formulated drug (page 184-185).
Haselberg analyzes intact antibodies and product-related impurities (page 185), including:
clipped heavy-chain species
truncated light chains
glycoform variants
charge variants
low-abundance contaminants in antibody preparations
These species are “contaminants” relative to the primary therapeutic antibody, directly corresponding to the limitation in claim 13.
A POSITA would recognize that the same CE–MS workflow used by Haselberg to identify mAb contaminants would be equally applicable to contaminants in a co-formulated antibody drug.
Regarding claim 14, Haselberg teaches that wherein the antibody of interest is a monoclonal antibody (page 185, par 2).
Regarding claim 16, Haselberg teaches that wherein the antibody of interest is conjugated to a cytotoxic agent, a chemotherapeutic drug, an immunosuppressant, or a radioisotope (e.g. trastuzumab) (page 183, par 2).
Claim(s) 15 and 19-20 is/are rejected under 35 U.S.C. 103 as being unpatentable over Haselberg in view of Francois as applied to claims 10-14 and 16 above, and further in view of Chames et al. (mAbs, 2009, IDS) (Chames).
Regarding claim 15, Haselberg clearly teaches analytical workflows for antibody heterogeneity (title, abstract), which would have been recognized by a POSITA as applicable to any antibody product, including bsAbs and their monoclonal side products.
Haselberg does not specifically teach that wherein the antibody of interest comprises a bispecific antibody. Chames teaches bispecific antibodies for cancer therapy (title). Chames teaches that bispecific antibodies (bsAbs) had become an important therapeutic modality, noting that clinical trials “are finally providing exciting results, with the most impressive ones being delivered by triomab and BiTE molecules,” and that bsAbs represent “a real leap in terms of therapeutic efficiency. For the first time, the possibility of actually curing patients using antibodies seems within reach.” (page 545, par 2).
Therefore, Chames not only discloses the existence of bispecific antibodies, but explicitly emphasizes their growing therapeutic importance and success in clinical development, thereby providing a clear motivation to apply known intact-protein CE-MS analytical methods to ensure bsAb structural integrity and to distinguish correctly assembled products from monospecific antibody side-products, as required for clinical quality control.
Such recognition in the art would have strongly motivated a person of ordinary skill to apply established analytical techniques for monoclonal antibody quality assessment, such as the CE-MS workflows taught by Haselberg and Francois, to bispecific antibody products — including the identification of mispaired monospecific side products that can arise during bsAb manufacturing.
At time before the filing, it would have been obvious to one of ordinary skill in the art to apply Haselberg’s method for analyzing bispecific antibodies for cancer therapy, in order to have a quality control for the antibody drugs.
Regarding claim 19, Haselberg-Chames teaches that wherein the co-formulated drug includes a plurality of bispecific antibodies and a plurality of monoclonal antibodies, and the target antibody is one of the plurality of bispecific antibodies or one of the plurality of monoclonal antibodies (Haselberg, Fig. 6, page 189) (Chames, page 545).
Haselberg demonstrates CE–MS separation of multiple coexisting antibody species in a single sample (par 184-185), including:
clipped or truncated chains
glycoform variants
charge variants
antibody-derived impurities
These species already vary in mass, charge, and structure—just as monoclonal antibodies and bispecific antibodies do.
A POSITA would understand that CE–MS does not depend on therapeutic purpose or antibody lineage.
It simply separates whatever antibody species are present by mass and/or charge.
Thus, applying CE–MS to a mixture containing pluralities of bispecific and monoclonal antibodies is a predictable, routine extension of Haselberg’s method.
Chames recognizes:
the clinical growth of bispecific antibodies,
the importance of correctly defining product purity, and
the inherent mixing and mispairing events associated with bsAb production.
Importantly, Chames also explains that bispecifics and monoclonals are often developed in parallel therapeutic strategies, reinforcing that drug products may contain multiple antibody modalities.
Given this teaching, a POSITA would have been strongly motivated to apply the intact/native CE–MS workflows of Haselberg and Francois to any formulation containing:
multiple bispecific antibodies,
multiple monoclonal antibodies, or
combinations thereof.
Nothing in claim 19 requires any analytical capability beyond what CE–MS already provides.
Regarding claim 20, Haselberg-Chames teaches that wherein the antibody of interest is a first antibody of interest and a monoclonal antibody, the co-formulated drug includes a second antibody of interest, and the second antibody of interest is a bispecific antibody (Haselberg, Fig. 6, page 189) (Chames, page 545).
Haselberg demonstrates that CE–MS can resolve multiple intact antibodies, including:
distinct glycoforms,
clipped variants,
truncation products,
charge variants, and
co-existing impurity species.
This is analytically no different from resolving:
a monoclonal antibody and
a bispecific antibody
present together in a single mixture.
A POSITA would understand that CE–MS separation depends solely on mass and charge, not on whether the antibody is monoclonal or bispecific.
Thus, applying Haselberg’s method to a co-formulated mixture of a mAb and a bsAb is a predictable and routine extension of the reference.
Chames describes:
the importance of therapeutic bispecific antibodies,
their increasing clinical relevance,
their structural diversity, and
the critical need for analytical characterization of bsAbs for product quality.
Chames also teaches that bispecific antibodies frequently coexist with other antibody species (including monoclonal antibodies) in development and formulation contexts.
As Chames notes:
“clinical trials of bsAbs… are finally providing exciting results… a real leap in therapeutic efficiency…” (page 545, par 2).
This motivates a POSITA to apply standard intact/native CE–MS methods to any mixture containing bsAbs, including mixtures where the other component is a monoclonal antibody.
Claim(s) 17-18 is/are rejected under 35 U.S.C. 103 as being unpatentable over Haselberg in view of Francois as applied to claims 10-14 and 16 above, and further in view of Dolnik (US 2010/0187113, IDS).
Regarding claim 17, Haselberg does not specifically teach that wherein the one or more capillaries comprise a separation matrix. Dolnik teaches capillaries comprise a separation matrix for separation of monoclonal antibodies (par [0128]). Dolnik teaches that “The sieving matrix enables size separation of proteins. It provides obstacles in the migration path and makes proteins complexed with cationic surfactants to electrophoretically migrate according to their size” (par [0105]). At time before the filing it would have been obvious to one of ordinary skill in the art to include a separation matrix in the capillary electrophoresis, in order to enable size separation.
Regarding claim 18, Dolnik teaches that wherein the one or more capillaries comprise a sieving matrix configured to separate proteins by molecular weight (par [0105]).
Response to Arguments
Applicant's arguments filed 03/11/2026 have been fully considered but they are not persuasive.
1. Haselberg teaches CE directly coupled to mass spectrometry for intact antibody analysis
Haselberg discloses capillary electrophoresis directly coupled to electrospray mass spectrometry for the analysis of intact monoclonal antibodies and antibody variants. The reference explicitly describes separation of antibody species by charge and/or mass using CE followed by MS determination of mass, which corresponds to the core analytical steps recited in the pending claims.
While Haselberg performs the analysis under conditions described as denaturing, the reference nevertheless establishes that:
capillary electrophoresis can be directly coupled to a mass spectrometer, and
intact antibodies and their variants can be separated and characterized by CE-MS.
Thus, Haselberg clearly teaches the primary analytical platform recited in the claims.
2. Francois teaches antibody analysis under native conditions
Francois teaches the use of capillary electrophoresis methods under native conditions for antibody characterization. Francois further explains that antibody structural variants and charge variants may be analyzed while maintaining native antibody structure.
Although Applicant argues that Francois does not explicitly disclose CE directly coupled to MS, this distinction does not overcome the rejection. The coupling of CE to MS was already well established in Haselberg and other analytical literature. A person of ordinary skill in the art would have recognized that native-condition CE separations disclosed by Francois could be implemented in CE-MS systems such as those described in Haselberg.
Combining these teachings represents a routine application of known analytical instrumentation to achieve predictable analytical results.
3. The combination represents a predictable modification
Applicant argues that Haselberg provides no motivation to modify its denaturing CE-MS method to operate under native conditions. However, the motivation arises from the recognized advantages of native-condition analysis discussed in Francois and other literature, including preservation of higher-order structure and characterization of intact antibody complexes.
A person of ordinary skill in the art seeking to analyze intact antibodies under conditions preserving native structure would reasonably have been motivated to apply native CE conditions (Francois) within the CE-MS analytical framework already demonstrated by Haselberg.
Under KSR, applying a known technique to a known device for its established purpose is an obvious design choice where the result is predictable.
4. Statements in the references regarding analytical challenges do not teach away
Applicant also argues that Haselberg and Francois describe challenges in detecting certain charge variants such as deamidation or oxidation using intact mass spectrometry.
However, such statements merely recognize analytical limitations or difficulties associated with detecting small mass differences. A disclosure that a technique has limitations or may present analytical challenges does not constitute a teaching away, particularly where the reference nevertheless demonstrates successful antibody characterization using CE-MS.
The cited references therefore do not discourage the use of CE-MS for antibody characterization; rather, they confirm that such methods were actively used for this purpose.
5. The recited charge variants are known antibody modifications
claimed charge variants—including deamidation, oxidation, glycation, disulfide formation, and glycosylation—are well-known antibody modifications commonly characterized in therapeutic antibody analysis. The identification of these variants represents a routine analytical objective in antibody characterization workflows.
Accordingly, their recitation in the claims does not confer patentable distinction over the cited analytical techniques.
Conclusion
Any inquiry concerning this communication or earlier communications from the examiner should be directed to XIAOYUN R XU, Ph. D. whose telephone number is (571)270-5560. The examiner can normally be reached M-F 8am-5pm.
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/XIAOYUN R XU, Ph.D./ Primary Examiner, Art Unit 1797
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