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 .
Response to Amendment
Applicant’s remarks and amendments to the claims received 03/30/2026 have been acknowledged. Claims 105, 109, 118, 119, 122, 127, and 130 have been amended. Claims 107 and 116 have been canceled. In view of the claim amendments and upon further consideration of the record, the rejections under 35 USC 112(a) enablement previously set forth in the Non-Final Rejection of 12/29/2025 have been withdrawn.
Claim Rejections - 35 USC § 112
The following is a quotation of the first paragraph of 35 U.S.C. 112(a):
(a) IN GENERAL.—The specification shall contain a written description of the invention, and of the manner and process of making and using it, in such full, clear, concise, and exact terms as to enable any person skilled in the art to which it pertains, or with which it is most nearly connected, to make and use the same, and shall set forth the best mode contemplated by the inventor or joint inventor of carrying out the invention.
The following is a quotation of the first paragraph of pre-AIA 35 U.S.C. 112:
The specification shall contain a written description of the invention, and of the manner and process of making and using it, in such full, clear, concise, and exact terms as to enable any person skilled in the art to which it pertains, or with which it is most nearly connected, to make and use the same, and shall set forth the best mode contemplated by the inventor of carrying out his invention.
Written Description
Claims 105-106 and 117-119 are rejected under 35 U.S.C. 112(a) or 35 U.S.C. 112 (pre-AIA ), first paragraph, as failing to comply with the written description requirement. The claim(s) contains subject matter which was not described in the specification in such a way as to reasonably convey to one skilled in the relevant art that the inventor or a joint inventor, or for applications subject to pre-AIA 35 U.S.C. 112, the inventor(s), at the time the application was filed, had possession of the claimed invention.
Claims 105 (as amended) does not recite any specific amino acid mutations that can be made in an Fc molecule such that the resulting variant Fc molecule exhibits has the functional property of reducing autoreactive antibodies in a subject. Claims 106, 117, and 118 depend from claim 1 but do not cure the deficiencies of claim 1 and are thus also rejected.
Claim 119 also does not recite any specific amino acid substitutions that can be made in the Fc domain of the claimed anti-FcRn antibodies such that the resulting variant Fc molecule (or FcRn binding fragment thereof) exhibits increased binding to FcRn relative to wild-type IgG Fc region.
The guidelines for the Examination of Patent Applications Under the 35 U.S.C. 112, § 1 "Written Description" Requirement make clear that if a claimed genus does not show actual reduction to practice for a representative number of species, then the Requirement may be alternatively met by reduction to drawings, or by disclosure of relevant, identifying characteristics, i.e., structure or other physical and or chemical properties, by functional characteristics coupled with a known or disclosed correlation between function and structure, or by a combination of such identifying characteristics, sufficient to show the applicant was in possession of the genus (MPEP 2163).
In The Regents of the University of California v. Eli Lilly (43 USPQ2d 1398-1412) 19 F. 3d 1559, the court held that disclosure of a single member of a genus (rat insulin) did not provide adequate written support for the claimed genus (all mammalian insulins). In this same case, the court also noted:
“A definition by function, as we have previously indicated, does not suffice to define the genus because it is only an indication of what the gene does, rather than what it is. See Fiers, 984 F.2d at 1169-71, 25 USPQ2d at 1605-06 (discussing Amgen). It is only a definition of a useful result rather than a definition of what achieves that result. Many such genes may achieve that result. The description requirement of the patent statute requires a description of an invention, not an indication of a result that one might achieve if one made that invention. See In re Wilder, 736 F.2d 1516, 1521, 222 USPQ 369, 372-73 (Fed. Cir. 1984) (affirming rejection because the specification does “little more than outlin [e] goals appellants hope the claimed invention achieves and the problems the invention will hopefully ameliorate."). Accordingly, naming a type of material generally known to exist, in the absence of knowledge as to what that material consists of, is not a description of that material.”
The court has further stated that “Adequate written description requires a precise definition, such as by structure, formula, chemical name or physical properties, not a mere wish or plan for obtaining the claimed chemical invention.” Id. at 1566, 43 USPQ2d at 1404 (quoting at 1171, 25 USPQ2d at 1606). Also see (CAFC 2002). Enzo-Biochem v. Gen-Probe Fiers, 984 F.2d 01-1230.
Claim 105 (as amended) is broadly drawn to a method of reducing autoreactive antibodies in a pregnant individual comprising administering an FcRn inhibitor to the individual thereby reducing the autoreactive antibodies in the pregnant individual, wherein the FcRn inhibitor is a polypeptide that comprises a variant Fc molecule.
Claim 119 also does not recite any specific amino acid substitutions that can be made in the Fc domain of the claimed anti-FcRn antibodies such that the resulting variant Fc molecule (or FcRn binding fragment thereof) exhibits increased binding to FcRn relative to wild-type IgG Fc region.
The specification teaches that administration of Abdegs – FcRn antagonists comprising variant IgG Fc regions with increased FcRn binding affinity relative to wild-type IgG Fc—reduces maternal autoreactive antibodies targeting LDHA, LDHB, CRMP1, and STIP1 in MAR (maternal-autoantibody related)-ASD positive rodents generated by immunization with these antigens (Example 3). The FcRn antagonists exemplified for use in the example included an ABDEG (a variant Fc molecule having increased FcRn binding relative to wildtype IgG, such as SEQ ID NOs: 1-3). There is no guidance provided in the specification for the identification of specific amino acid mutations across different IgG isotypes suitable for producing a variant Fc molecule that effectively reduces pathogenic IgG (i.e. autoreactive antibodies) in an individual commensurate in scope of claim 105.
The prior art teaches that FcRn normally recycles IgG and extends its half-life by preventing lysosomal degradation. FcRn inhibitors such as ABDEGs bind to FcRn with higher affinity than endogenous IgG, blocking IgG recycling and causing increased degradation and faster clearance of pathogenic IgG autoantibodies (see Fox-Edmiston, Section 2.2: In Vivo Antibody Competition and Removal, of record). Some Fc mutations increase FcRn binding affinity, while others decrease it. For example, YTE (M252Y, S254T, T256E), QL (T250Q/M428L), AAA (T307A, E380A, N434A ), and LS (M428L/N434S) mutations enhance IgG1 binding to FcRn (see Kuo et al, Table 1), whereas I253A/H310A/H435A (IHH) mutations disable IgG1 binding to murine and human FcRn binding (Qiao et al, see “FcRn Enhances Ag Presentation of Murine DC Both in Vitro and in Vivo” section). As presently written, the claimed genus of variant Fc molecules encompasses Fc mutations that can made across different IgG isotypes, including mutations that can potentially reduce binding to FcRn. A variant Fc molecule having mutations that reduce FcRn binding as encompassed by the claim scope would not be expected to reduce pathogenic IgG autoantibodies in an individual. Without further guidance, artisans would have to engage in additional unpredictable experimentation to identify mutations that can be made in an Fc molecule such that the resulting variant Fc molecule possesses the claimed functional properties. Claims 106, 117, and 118 depend from claim 1 but do not cure the deficiencies of claim 1 and are thus also rejected.
Similarly, claim 119 does not does not recite any specific amino acid substitutions that can be made in the Fc domain of the claimed anti-FcRn antibodies such that the resulting variant Fc molecule (or FcRn binding fragment thereof) exhibits increased binding to FcRn relative to wild-type IgG Fc region. The specification appears to only disclose Fc variants containing YTEKF substitutions (see, e.g. Para. 0010), and the working examples are limited to antibodies comprising these particular Fc mutations (Example 3). YTEKF mutations are not representative of the diversity of Fc substitutions that can be made in order to yield a variant Fc having increased affinity for FcRn relative to wild-type IgG. Artisans would not be able to readily determine without further testing which specific amino acid alterations can be made Fc domain or an FcRn binding fragment thereof to yield a variant Fc molecule that binds to FcRn with increased affinity relative to wild-type IgG Fc domain.
Thus, one of ordinary skill in the art would reasonably conclude that the applicant was not in possession of the full breadth of the claimed genus of variant Fc molecules at the time the instant application was filed.
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.
Claims 105-106, 113, 114, and 117-119 are rejected under 35 U.S.C. 103 as being unpatentable over Fox-Edmiston et al (Fox-Edmiston, Elizabeth, and Judy Van de Water. “Maternal Anti-Fetal Brain IgG Autoantibodies and Autism Spectrum Disorder: Current Knowledge and its Implications for Potential Therapeutics.” CNS drugs vol. 29,9 (2015): 715-24. doi:10.1007/s40263-015-0279-2/0137713A1, of record), hereinafter Edmiston.
Edmiston teaches that prenatal exposure to maternal autoantibodies directed against fetal brain proteins is a viable risk factor for the development of autism spectrum disorder (ASD) in the exposed offspring. Seven fetal brain proteins critical for neurodevelopment were identified as specific targets of maternal autoantibodies associated with maternal autoantibody-related autism, including Y-box binding protein (YBX1), lactate dehydrogenase (LDH) A and B, stress-induced phosphoprotein 1 (STIP1), collapsing response mediator proteins (CRMPs) 1 and 2, and cypin. Maternal IgG—including those that target these fetal brain proteins—cross the placenta via the neonatal Fc receptor (FcRn) during the third trimester (Abstract’ 1st, 2nd, and last paragraphs of Introduction; and Key Points); thus, it is suggested that FcRn inhibitors such as Abdegs (recombinant antibodies with engineered Fc regions having increased affinity for FcRn compared to wild-type IgG Fc) and anti-FcRn antibodies can be used to prevent the transfer of maternal anti-brain autoantibodies during critical periods of neurodevelopment, thereby preventing ASD in the offspring (see 1st paragraph under Section 2: Mechanisms to prevent of pathogenic autoantibodies; 1st and 3rd paragraphs of Section 2.2: In Vivo Antibody Competition and Removal, and Figures 2 and 3 captions). It is noted that Abdegs necessarily comprise a variant Fc region with one or more substitutions that increase affinity for FcRn relative to wildtype Fc region per claim 119. It is further stated that development of an autoantibody-based screening assay would enable identification of candidates in need of medical intervention (Section 3: Conclusions). Although the paper refers generally to “candidates for medical intervention”, the therapeutic strategies described are uniformly directed toward reducing or preventing the transfer of maternal autoantibodies to the developing fetus during gestation, necessarily limiting such candidates to pregnant women. Therefore, it would have been obvious for artisans to identify pregnant women who harbor autoantibodies against fetal brain proteins such as YBX1 by assaying a biological sample from the pregnant women and select those women for therapeutic intervention with FcRn-targeted therapies in order to prevent placental transfer of these pathogenic IgG, thereby preventing or reducing symptoms associated with autism or ASD in the offspring.
Claims 109-112 are rejected under 35 U.S.C. 103 as being unpatentable over Edmiston, as applied to claims 105-106, 113, 114, and 117-119 above, and further in view of Ling et al (Ling, Leona E et al. “M281, an Anti-FcRn Antibody: Pharmacodynamics, Pharmacokinetics, and Safety Across the Full Range of IgG Reduction in a First-in-Human Study.” Clinical pharmacology and therapeutics vol. 105,4 (2019): 1031-1039. doi:10.1002/cpt.1276. EPUB: 2018 Dec 4, of record), hereinafter Ling.
The teachings of Edmiston have been discussed above and differ from the instantly claimed invention in that it is not specifically taught that the anti-FcRn antibody therapy is nipocalimab (or M281).
However, Ling teaches that M281 (nipocalimab) is a high affinity, fully human, effectorles monoclonal IgG anti-FcRn antibody that inhibits FcRn-mediated IgG recycling to decrease pathogenic IgG while preserving IgG production. A consistent and close relationship has been observed between FcRn receptor occupancy, serum IgG reduction, and M281 pharmacokinetics. This, together with initial safety and tolerability data, supports further clinical evaluation of M281 in autoimmune and alloimmune diseases driven by pathogenic IgG autoantibodies (see Abstract, Study Highlights, and last paragraph of Introduction on Page 1032 prior to “Results” section).
It would have been obvious to one of ordinary skill in the art to use nipocalimab (or M281) as the FcRn antagonist in the method for prevention of autism spectrum disorder in the offspring of pregnant mothers as taught by Edmiston. One of ordinary skill in the art would have been motivated to do so since FcRn inhibitors such as anti-FcRn antibodies can be used to prevent the transfer of maternal anti-brain autoantibodies during critical periods of neurodevelopment, thereby preventing ASD in the offspring as taught by Edmiston; and nipocalimab (M281) is an anti-FcRn antibody that inhibits FcRn-mediated IgG recycling to decrease pathogenic IgG while preserving IgG production. Therefore, one of ordinary skill in the art would reasonably expect that administration of nipocalimab (M281) to pregnant mothers can prevent the transfer of maternal anti-brain autoantibodies- such as those targeting YBX1- in order to prevent or the reduce the risk of ASD in the offspring.
Claims 105-106, 109-114, and 117-119 are rejected under 35 U.S.C. 103 as being unpatentable over Van de Water et al (WO2011019929A1, of record), hereinafter Van de Water, in view of Fox-Edmiston et al (Fox-Edmiston, Elizabeth, and Judy Van de Water. “Maternal Anti-Fetal Brain IgG Autoantibodies and Autism Spectrum Disorder: Current Knowledge and its Implications for Potential Therapeutics.” CNS drugs vol. 29,9 (2015): 715-24. doi:10.1007/s40263-015-0279-2/0137713A1, of record), hereinafter Edmiston, and Ling et al (Ling, Leona E et al. “M281, an Anti-FcRn Antibody: Pharmacodynamics, Pharmacokinetics, and Safety Across the Full Range of IgG Reduction in a First-in-Human Study.” Clinical pharmacology and therapeutics vol. 105,4 (2019): 1031-1039. doi:10.1002/cpt.1276. EPUB: 2018 Dec 4, of record), hereinafter Ling.
Van de Water teaches methods for determining the risk of developing an autism spectrum disorder (ASD) in a fetus or child by detecting in a biological sample from the mother antibodies that bind to one or more biomarkers selected from the group consisting of Y Box Binding Protein 1 (YBX1), lactate dehydrogenase (LDH), guanine deaminase (GDA), collapsin response mediator protein 1 (CRMP1), stress-induced phosphoprotein 1 (STIP1), alpha subunit of the barbed-end actin binding protein Cap Z (CAPZA2), eukaryotic translation and elongation factor 1A1 (EEF1A1), microtubule-associated protein Tau (MAPT), dihydropyrimidinase-like protein 2 (DPYSL2), dynamin 1-like protein (DNM1L), radixin (RDX), moesin (MSN), and ezrin (EZR) (Abstract; Brief Summary of the Invention, in particular, Para. 0008). Further disclosed are methods of preventing or reducing the risk of a fetus or child developing an ASD by administering to the mother an agent that removes from the mother antibodies that bind to the one or more fetal biomarkers such as YBX1 (Abstract and Para. 0030). As such, the diagnostic and prevention and/or treatment methods are performed on a woman carry a fetus (i.e. who is pregnant) (Para. 0100).
Van de Water does not teach that the agent that facilitates removal of maternal autoantibodies targeting fetal biomarkers (e.g. YBX1) is an FcRn antagonists such as an Abdeg or the anti-FcRn antibody nipocalimab (M281).
However, Edmiston teaches that FcRn inhibitors such Abdegs (recombinant antibodies with engineered Fc regions having increased affinity for FcRn compared to wild-type IgG Fc) or anti-FcRn antibodies can be used to prevent the transfer of maternal anti-brain autoantibodies during critical periods of neurodevelopment, thereby preventing ASD in the offspring (see Abstract; last paragraph of Introduction prior to Section 2; 1st paragraph under Section 2: Mechanisms to prevent of pathogenic autoantibodies; 1st and 3rd paragraphs of Section 2.2: In Vivo Antibody Competition and Removal, and Figures 2 and 3 captions). It is noted that Abdegs necessarily comprise a variant Fc region with one or more substitutions that increase affinity for FcRn relative to wildtype Fc region per claim 119.
Ling further teaches that M281 (nipocalimab) is a high affinity, fully human, effectorles monoclonal IgG anti-FcRn antibody that inhibits FcRn-mediated IgG recycling to decrease pathogenic IgG while preserving IgG production. A consistent and close relationship has been observed between FcRn receptor occupancy, serum IgG reduction, and M281 pharmacokinetics. This, together with initial safety and tolerability data, supports further clinical evaluation of M281 in autoimmune and alloimmune diseases driven by pathogenic IgG autoantibodies (see Abstract, Study Highlights, and last paragraph of Introduction on Page 1032 prior to “Results” section).
It would have been obvious to one of ordinary skill in the art to use an FcRn antagonists such as an Abdeg or the anti-FcRn antibody nipocalimab (or M281) as the agent that facilitates removal of maternal autoantibodies against fetal biomarkers in the method for the prevention of autism spectrum disorder in the offspring of pregnant mothers as taught by Van de Water. One of ordinary skill in the art would have been motivated to do so since FcRn inhibitors such as Abdegs or anti-FcRn antibodies can be used to prevent the transfer of maternal anti-brain autoantibodies during critical periods of neurodevelopment, thereby preventing ASD in the offspring as taught by Edmiston; and nipocalimab (M281) is an anti-FcRn antibody that inhibits FcRn-mediated IgG recycling to decrease pathogenic IgG while preserving IgG production. Therefore, one of ordinary skill in the art would reasonably expect that administration of nipocalimab (M281) to pregnant mothers can prevent the transfer of maternal anti-brain autoantibodies- such as those targeting YBX1- in order to prevent or the reduce the risk of ASD in the offspring.
Response to Arguments
Applicant's arguments filed 03/30/2026 have been fully considered but they are not persuasive.
With respect to rejections made under 35 USC 112(a) written description, Applicant argues that as amended claim 105 details both the polypeptide that binds to an FcRn and six non-degenerate CDR sequences, thus satisfying the written description requirement.
In response to Applicant’s argument, the Examiner notes that claim 105 (as amended) further broadens the scope of a variant Fc molecule used as an FcRn antagonist. Claim 105 does not recite any specific amino acid mutations that can be made in an Fc molecule such that the resulting variant Fc molecule exhibits has the functional property of reducing autoreactive antibodies in a subject as discussed in the 35 USC 112(a) writhe description rejection above. Briefly, some Fc mutations increase FcRn binding affinity, while others decrease it. As presently written, the claimed genus of variant Fc molecules encompasses Fc mutations that can made across different IgG isotypes, including mutations that can potentially reduce binding to FcRn. A variant Fc molecule having mutations that reduce FcRn binding as encompassed by the claim scope would not be expected to reduce pathogenic IgG autoantibodies in an individual. Without further guidance, artisans would have to engage in additional testing and screening to identify mutations that can be made in an Fc molecule such that the resulting variant Fc molecule possesses the claimed functional properties. Claims 106, 117, and 118 depend from claim 1 but do not cure the deficiencies of claim 1 and are thus also rejected. The Examiner further notes that the particular deficiencies raised previously under 35 USC 112(a) written description regarding claim 119 were not addressed. For the reasons discussed previously, this rejection is thus maintained over claim 119.
With respect to the rejections made under 35 USC 103, Applicant argues that the skilled artisan reading Van de Water and Fox-Edmiston would not turn towards the claimed subject matter because Fox-Edmiston and Ling teach away from general FcRn inhibition alone. In particular, Applicant notes that among the various potential therapies discussed, Fox-Edmiston specifically disparages and highlights the significant potential drawbacks of general FcRn inhibition alone in its discussion on Abdegs and anti-FcRn antibodies. For example, Fox-Edmiston states that "[u]nfortunately, all of the above-mentioned treatments [Abdegs and anti-FcRn antibodies and peptides] could systematically induce the degradation of all IgGs because they are relatively non-specific." (Fox-Edmiston at Section 2.2; emphasis added). Further, Fox-Edmiston warns that "the aforementioned therapeutics [Abdegs and anti-FcRn antibodies and peptides] would potentially prevent the transfer of all maternal antibodies, which may increase the risk of immunodeficiency in the infant." (Fox-Edmiston at Section 2.2; emphasis added). Similarly, Ling also cautions the disadvantage of general FcRn inhibition alone in that "blockade of FcRn recycling is expected to reduce serum and tissue levels of all IgGs ...." (Ling at Page 1032, 3rd Paragraph). Thus, the skilled artisan reading Van de Water, Fox-Edmiston, and Ling would not turn towards the claimed subject matter because Fox-Edmiston teaches away from general FcRn inhibition for fear of its unfortunate drawbacks, including increased risk of immunodeficiency and infection to both mother and offspring.
However, Applicant contends that FcRn antagonists surprisingly reduce pathogenic IgG (Figures 6A-D) without systemically reducing the amount of total IgG, noting in paragraph [0254] that “interestingly, an apparent reduction in total IgG was not discernable”. Thus, Applicant asserts that the claimed subject matter produces results that are unexpected and non-obvious in view of the cited prior art.
In response to Applicant’s arguments, first the Examiner notes that while Fox-Edmiston and Ling acknowledge that FcRn antagonists can reduce total IgG and/or lead to certain risks (e.g. immunodeficiency as noted in the latter), neither expressly criticize, discredit, or otherwise discourage the use of FcRn antagonists for achieving the intended purpose of the claimed invention (i.e. reducing pathogenic IgG, or autoreactive antibodies). In fact, the passage in Fox-Edmiston cited by Applicant goes on to say that “[d]etermining the precise time point during which the blood-brain barrier (BBB) becomes impermeable to circulating maternal factors may allow these treatments [Abdegs and anti-FcRn antibodies and peptides] to be utilized in a way that prevents anti-brain antibodies from entering the fetal compartment before BBB formation but permits the transfer of protective antibodies after early steps in fetal brain development have been completed (Emphasis Added). Thus, far from teaching away, Fox-Edmiston acknowledges the technical hurdle of FcRn antagonists to be mitigated and further provides a proposed solution to the problem, namely, optimizing the timing of administration to achieve a safer clinical result. Therefore, Fox-Edmiston presents the use of FcRn antagonists as a viable therapeutic option that can be optimized to reduce the transfer of maternal autoreactive antibodies while permitting the transfer of protective antibodies; the reference does not disparage their use to achieve this effect contrary to applicant’s assertion.
Second, in regards to the alleged unexpected results, the Examiner notes that the graphical representation of total IgG levels over time (Figure 6E) is not accompanied with any statistical analyses or quantitative comparison between groups; and thus it is unclear how Applicant has reached the conclusion that “an apparent reduction in total IgG levels was not discernable”. The prior art (see, e.g. Ling) demonstrates that recovery of IgG levels toward baseline levels after treatment with an FcRn antagonist is due to loss of receptor occupancy as the drug clears from the system over time, allowing normal IgG recycling to resume. In particular, a single administration of M281 (nipocalimab) resulted in rapid FcRn saturation as measured by receptor occupancy concomitant with a decrease in serum IgG. The recovery of IgG is initiated upon loss of receptor occupancy and returns toward baseline levels in an asymptotic manner (see Figure 1). Applicant’s data (Figure 6E) appears to show a reduction (~ 2-fold) in total IgG levels after administration of an FcRn antagonist to MAR rat 1 and MAR rat 2, particularly at the 48-hour and 72-hour timepoints, respectively, followed by a gradual return towards baseline levels consistent with known mechanism of action of FcRn antagonists. Thus, the observed changes in total IgG after administration of an FcRn antagonist do not appear to be unexpected.
Third, it is well-known that there is a dose-dependent clearance of IgG by FcRn antagonists. For example, as noted in Ling, intravenous infusion of single ascending doses of M281 (nipocalimab) up to 60 mg/kg induced dose-dependent serum IgG reductions (Abstract). Thus, even if, for the sake of argument, the FcRn antagonist used by Applicant at 5 mg per dose (per Example 3) reduced maternal autoreactive antibodies without systemically lowering total IgG, this observation does not appear to take into account potential dose-dependent effects of FcRn antagonism on serum IgG levels (e.g. whether similar effects are observed at different doses) and may not fully support a conclusion of unexpected results.
Therefore, in view of the foregoing, the 35 USC 103 rejections are maintained.
Conclusion
No claims are allowable.
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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/LIA E TAYLOR/Examiner, Art Unit 1641
/MISOOK YU/Supervisory Patent Examiner, Art Unit 1641
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