Notice of Pre-AIA or AIA Status
The present application, filed on or after March 16, 2013, is being examined under the first inventor to file provisions of the AIA .
Claims Status
The amendments and remarks filed 04/08/2026 are acknowledged.
Claim 1 is amended.
Claim 26 is new.
Claims 2-8, 11-13, 15-17, 19-21, and 24-25 are canceled.
Claims 1, 9-10, 14, 18, 22-23, and 26 are pending and under examination.
Withdrawn
The rejections of claims 1, 9-10, 14, 18, and 22-23 under 35 U.S.C. 112(b) are withdrawn. Applicant has amended claim 1 to overcome the rejections.
Maintained Rejections
Claim Rejections - 35 USC § 103
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.
This rejection has been modified solely to address the addition of new claim 26. The limitations set forth in instant claim 26 were previous limitations of claim 1 that were rejected under the maintained rejection as set forth below.
Claims 1, 9-10, 14, 18, 22, and 26 are rejected under 35 U.S.C. 103 as being unpatentable over Fujino (WO 2015099175; 02/23/2024 PTO-892), Gillies (WO200279415; 08/14/2024 PTO-892), Presta (US 5,869,046; 08/14/2024 PTO-892), Janeway et al., 2001 (08/14/2024 PTO-892), Goklen (US 20170174721; 01/12/2026 PTO-892), Qi et al., 2008 (02/23/2024 PTO-892) and Lam (US 6,171,586; 02/23/2024 PTO-892).
Regarding claims 1, 9-10, 14, 18, 22, and 26, Fujino teaches human anti-IL-33 neutralizing monoclonal antibodies [0001] and teaches a specific antibody clone named A10-1C04, which is disclosed as having the CDRs of C1 [0124], and C1 is disclosed as having an LCDR1 of SEQ ID NO: 1, an LCDR2 of SEQ ID NO: 11, an LCDR3 of SEQ ID NO:22, an HCDR1 of SEQ ID NO: 43, an HCDR2 of SEQ ID NO: 51, and an HCDR1 of SEQ ID NO: 65 [0011, Table 1].
SEQ ID NOs: 1, 11, 22, 43, 51, and 65 of Fujino have 100% sequence identity to SEQ ID NOs: 14-16 and 11-13 of the instant claim, respectively.
Further, Fujino teaches that the heavy chain and light chain variable regions of clone A10-1C04 is V1 [0124], which is disclosed as having SEQ ID NO: 105 for the heavy chain variable region and SEQ ID NO: 79 for the light chain variable region [0011, Table 2].
SEQ ID NO: 105 has 100% sequence identity to SEQ ID NO: 38 of the instant specification, and SEQ ID NO: 79 has 100% sequence identity to SEQ ID NO: 39 of the instant specification.
Fujino also teaches a composition comprising a monoclonal antibody of the invention [0099] and that the monoclonal antibodies can be separated and purified by any separation and purification method used in conventional proteins [0070].
However, Fujino does not specifically teach that the antibody heavy chain comprises SEQ ID NO: 1 and the antibody light chain comprises SEQ ID NO: 2, and also does not explicitly teach a specific formulation of the pharmaceutical composition comprising the antibody wherein the composition contains no salt, specifically no sodium chloride, potassium chloride, magnesium chloride, calcium chloride, sodium sulfate, potassium sulfate, magnesium sulfate, and calcium sulfate, and contains specific concentrations of histidine, sorbitol, and polysorbate 80 at a specific pH.
It is noted that residues 1-116 of SEQ ID NO: 1 correspond to SEQ ID NO: 38 of the instant specification and residues 1-110 of SEQ ID NO: 2 correspond to SEQ ID NO: 39 of the instant invention. SEQ ID NOs: 38 and 39 are taught above by Fujino.
Gillies teaches SEQ ID NO: 1, which is disclosed as a human IgG1 heavy chain Fc region [see pages 1, and 50-51].
SEQ ID NO: 1 of Gillies has 100% sequence identity to residues 117-446 of SEQ ID NO: 1 of the instant claim.
Presta teaches SEQ ID NO: 9, which is disclosed as the human lambda CL domain [see column 3, lines 51-52, and columns 57-58].
SEQ ID NO: 9 of Presta has 100% sequence identity to residues 111-215 of SEQ ID NO: 2 of the instant claim.
Janeway teaches that immunoglobulin heavy and light chains are composed of constant and variable regions [page 2, last paragraph – page 3, first-second paragraphs] and that the constant region determine the isotype, thus determining their functional properties [page 5, last paragraph – page 6, first paragraph].
Goklen teaches a multi component buffer system for the purification of proteins by a series of chromatography steps, comprising an organic acid, an alkaline metal or ammonium salt of the conjugate of the organic acid, and an organic base and wherein the modes of chromatography are performed using buffers that are made without the addition of NaCl [0003]. Goklen further teaches that this purification method using sodium acetate for the chromatography steps, along with acetic acid and tris base, offers advantages for monoclonal antibodies, including increasing ionic strength, maintaining constant pH through step changes, and avoiding pH transients that can lead to a loss of impurity clearance and step performance [0016]. Goklen also teaches that the elimination of sodium chloride ensures that the corrosive impact of high concentration chloride solutions on stainless steel processing equipment is managed and avoided all together [0016].
The purification method is described as using sodium acetate, acetic acid, and tris base, and therefore, meets the limitation of claim 1 in that the purified antibody contains no sodium chloride and meets the limitation of claim 26 in that the purified antibody contains none of the listed salts.
Qi teaches an antibody formulation comprising 100 mg/mL of an IgG protein (active ingredient) in a histidine, sorbitol (saccharide, sugar alcohol), and polysorbate 80 (nonionic surfactant), with a pH 5.5 solution [page 3120, left column, fifth paragraph].
The formulation is listed as not containing salt; therefore it meets the limitation of claim 1 in that the purified antibody contains no sodium chloride and meets the limitation of claim 26 in that the purified antibody contains none of the listed salts.
Lam teaches a stable aqueous pharmaceutical formulation comprising a therapeutically effective amount of an antibody, a buffer maintaining the pH in the range from about 4.5 to about 6.0, a surfactant, and a polyol [see Abstract]. Lam further teaches that the buffer can be histidine at a concentration of about 1 mM to about 50 mM, preferably from about 5 mM to about 30 mM [column 22, second paragraph], that the surfactant can be polysorbate 80, present in the formulation in an amount from about 0.001% to about 0.5% (w/v) [column 22, fourth paragraph], and the polyol can be sorbitol [column 6, sixth paragraph] with a suitable concentration of about 1% to about 15% w/v [column 22, third paragraph]. Lam further teaches that the therapeutically effective amount of antibody present in the formulation is determined by taking into account the desired dose volumes and dose of administration, with an exemplary antibody concentration in the formulation being from about 0.1 mg/mL to about 50 mg/mL [column 22, first paragraph], but that the appropriate dosage will depend on the condition to be treated, the severity and course of the condition, why the antibody is being administered, the patient’s clinical history, and response to the antibody, and other dosage regimens can be useful [column 23, fifth paragraph – sixth paragraph]. Lam also teaches that the formulation is prepared comprising the antibody in a pH-buffered solution, where the pH can range from about 4.5 to about 6.0, and histidine can control the pH within this range [column 22, second paragraph]. Lam further teaches that the formulation can be administered by way of known methods, inclusive of subcutaneous and intravenous administration [column 23, fourth paragraph] and also teaches that the formulation does not contain a tonicifying amount of a salt, such as sodium chloride, as it may cause the antibody to precipitate and/or may result in oxidation at a low pH [column 22, third paragraph].
It would have been obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to have modified the heavy chain (i.e. residues 1-116 of instant SEQ ID NO: 1) and light chain variable regions (i.e. residues 1-110 of instant SEQ ID NO: 2) of clone A10-1C04 is V1, as taught by Fujino, to further comprise the human IgG1 heavy chain Fc region (i.e. residues 117-446 of instant SEQ ID NO: 1), as taught by Gillies, and the human lambda CL domain (i.e. residues 111-215 of instant SEQ ID NO: 2), as taught by Presta, to arrive at the heavy chain of SEQ ID NO: 1 and the light chain of SEQ ID NO: 2 as instantly claimed. One would have been motivated to make this modification because Janeway taches that immunoglobulin heavy and light chains are composed of both constant and variable regions, and the constant regions determine the antibodies functional properties. Thus, this is a known structure for an antibody.
Further, it would have been obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to have specifically purified the antibody of Fujino using the purification process taught by Goklen, thereby obtaining a purified antibody without sodium chloride or any of the salts listed in instant claim 26. One would have been motivated to have purified the antibody of Fujino with the process of Goklen because Fujino teaches that the monoclonal antibodies can be separated and purified by any separation and purification method used in conventional proteins, and Goklen teaches that the purification method using sodium acetate for the chromatography steps, along with acetic acid and tris base, offers advantages for monoclonal antibodies, including increasing ionic strength, maintaining constant pH through step changes, and avoiding pH transients that can lead to a loss of impurity clearance and step performance, and that the elimination of sodium chloride ensures that the corrosive impact of high concentration chloride solutions on stainless steel processing equipment is managed and avoided all together.
Additionally, it would have been obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to formulate the antibody as taught by Fujino, Gillies, Presta, Janeway, and Goklen in the pharmaceutical composition of Qi. One would have been motivated to use the pharmaceutical composition of Qi to have formulated a composition comprising the antibody taught by Fujino, Gillies, Presta, Janeway, and Goklen because Qi teaches that this formulation protects IgG antibodies from fragmentation with or without light exposure [page 3125, right column, first paragraph] and that the formulation was stable under normal light exposure encountered during manufacturing and handling [page 3129, left column, second-third paragraphs]. One of skill in the art would have a reasonable expectation that formulating the antibody taught by Fujino, Gillies, Presta, Janeway, and Goklen in the composition of Qi would produce a composition with superior stabilization properties.
It further would have been obvious to optimize the concentrations of the antibody, histidine, sorbitol, and polysorbate 80 of the composition of Qi using the teachings of Lam as a guide. One would have been motivated to optimize the composition to comprise 150 mg/mL of antibody (active ingredient), 10mM histidine, 4% (w/v) sorbitol, 0.02% (w/v) polysorbate 80, and has a pH adjusted to 5.5 to 6.5, because Lam teaches that these formulations are stable for antibody compositions. Further, MPEP 2144.05 (I) states “in the case where the claimed ranges ‘overlap or lie inside ranges disclosed by the prior art’ a prima facia case of obviousness exists.”
Specifically regarding the concentration of the antibody at 150 mg/mL, as encompassed by claims 1, 10, and 18, it would have been obvious to formulate the composition at this concentration of antibody because Qi teaches a composition with an antibody at 100 mg/mL and Lam teaches that the composition can comprise the antibody in an exemplary range of 0.1 mg/mL to about 50 mg/mL but that the appropriate dosage will depend on the condition to be treated, the severity and course of the condition, why the antibody is being administered, the patient’s clinical history, and response to the antibody, and that other dosage regimens can be useful [column 23, fifth paragraph – sixth paragraph]. A prima facie case of obviousness exists where the claimed ranges do not overlap with the prior art but are merely close (see MPEP 2144.05(I). Therefore, this is recognized as a result effective variable and one of skill in the art would engage in routine optimization to find the best antibody concentration for creating compositions that allow for desired dosing, while also retaining composition stability.
Additionally, regarding the specific concentrations for all of the components of the composition (i.e. antibody, histidine, sorbitol, and polysorbate 80), these are art recognized variables and therefore, one would engage in routine optimization to obtain the desired result of a stable formulation for the composition, thus arriving at these specific concentrations as claimed. See MPEP 2144.05 (II). Further, it is the normal desire of scientists or artisans to improve upon what is already generally known. The MPEP states the following: generally, 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. “[Where 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) (Claimed process which was performed at a temperature between 40°C and 80°C and an acid concentration between 25% and 70% was held to be prima facie obvious over a reference process which differed from the claims only in that the reference process was performed at a temperature of 100°C and an acid concentration of 10%.); see also Peterson. 315 F.3d at 1330, 65 USPQ2d at 1382 (“The normal desire of scientists or artisans to improve upon what is already generally known provides the motivation to determine where in a disclosed set of percentage ranges is the optimum combination of percentages.”); In re Hoeschele, 406 F.2d 1403, 160 USPQ 809 (CCPA 1969) (Claimed elastomeric polyurethanes which fell within the broad scope of the references were held to be unpatentable thereover because, among other reasons, there was no evidence of the criticality of the claimed ranges of molecular weight or molar proportions.). For more recent cases applying this principle, see Merck & Co. Inc, v. Biocraft Laboratories Inc.. 874 F.2d 804, 10 USPQ2d 1843 (Fed. Cir.), cert, denied, 493 U.S. 975 (1989); In re Kulling. 897 F.2d 1147, 14 USPQ2d 1056 (Fed. Cir. 1990); and In re Geisler. 116 F.3d 1465, 43 USPQ2d 1362 (Fed. Cir. 1997). The determination of specific excipients at specific concentrations in the instant composition requires only routine experimentation for one of ordinary skill in the art. Therefore, given that the excipients and antibody are common to include in the formulation of antibody compositions, as taught in the art above, without specific evidence that the indicated concentrations are critical to the formulation, the identification of these properties will not render the subject matter patentable.
Claims 1, 9-10, 14, 18, 22, 23, and 26 are rejected under 35 U.S.C. 103 as being unpatentable over Fujino (WO 2015099175; 02/23/2024 PTO-892) in view of Gillies (WO200279415; 08/14/2024 PTO-892), Presta (US 5,869,046; 08/14/2024 PTO-892), Janeway et al., 2001 (08/14/2024 PTO-892), Goklen (US 20170174721; 01/12/2026 PTO-892), Qi et al., 2008 (02/23/2024 PTO-892) and Lam (US 6,171,586; 02/23/2024 PTO-892), as applied to claims 1, 9-10, 14, 18, 22, and 26 above, and further in view of Terra Universal, 2015 (02/23/2024 PTO-892).
The teachings of Fujino, Gillies, Presta, Janeway, Goklen, Qi, and Lam are above.
However, Fujino, Gillies, Presta, Janeway, Goklen, Qi, and Lam do not teach a lyophilized preparation of the pharmaceutical composition.
Regarding claim 23, Terra Universal teaches that lyophilization, also known as freeze-drying, prevents sample contamination and promotes sample stability [see page 1, first paragraph]. Further, Terra Universal teaches that lyophilization also reduces sample weight and volume, remove the need to store samples on dry ice, as the samples are more stable at room temperature, and that overall lyophilization increases sample stability, purity, and increased shelf life [page 2, fifth paragraph].
It would have been obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to have lyophilized the pharmaceutical composition, as taught by Fujino, Gillies, Presta, Janeway, Goklen, Qi, and Lam. One would have been motivated to lyophilize the pharmaceutical composition because Terra Universal teaches that lyophilization increases sample stability, purity, and increase shelf life. One of skill in the art would have a reasonable expectation that lyophilizing the antibody formulation of Fujino, Gillies, Presta, Janeway, Goklen, Qi, and Lam would produce a composition with superior stabilization, purity and shelf life. Additionally, KSR International Co. v. Teleflex Inc., 127 S. Ct. 1727, 1741 (2007), discloses that if a technique has been used to improve one method, and a person of ordinary skill would recognize that it would be used in similar methods in the same way, using the technique is obvious unless its application is beyond that person' s skill. It would be obvious to apply a known technique to a known product to be used in a known method that is ready for improvement to yield predictable results. Thus, the combination of prior art references as combined provided a prima facie case of obviousness, absent convincing evidence to the contrary.
Response to Arguments
The rejections under 35 U.S.C. 103 over Fujino, Gillies, Presta, Janeway et al., Goklen, Qi et al., and Lam are maintained. On pages 5-7 of the remarks, Applicant argues the teachings of Qi as they relate to the conclusion of obviousness for a composition that is salt free and more specifically that contains no sodium chloride. However, these arguments as a whole are not persuasive because the rejection of record did not rely only on the teachings of Qi to arrive at a salt-free composition but also relied upon the teachings of Goklen. To reiterate, Goklen teaches a multi component buffer system for the purification of proteins by a series of chromatography steps comprising sodium acetate, acetic acid, and tris base without the addition of NaCl which offers advantages for monoclonal antibodies, including increasing ionic strength, maintaining constant pH through step changes, and avoiding pH transients that can lead to a loss of impurity clearance and step performance. Therefore, it would have been obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to have specifically purified the antibody of Fujino using the purification process taught by Goklen, thereby obtaining a purified antibody without any sodium chloride or any of the salts listed in instant claim 26, and that one would have been motivated to have purified the antibody of Fujino with the process of Goklen because Fujino teaches that the monoclonal antibodies can be separated and purified by any separation and purification method used in conventional proteins, and Goklen teaches that the purification method using sodium acetate for the chromatography steps, along with acetic acid and tris base, offers advantages for monoclonal antibodies, including increasing ionic strength, maintaining constant pH through step changes. See rejection above.
To address the specific arguments regarding the teachings of Qi applied in the rejection of record, on page 5 of the remarks, Applicant argues that Qi’s data reveals that omitting salt is insufficient to prevent aggregation even under ideal storage conditions, that according to the linear regression analysis of Figure 11, Qi's salt free formulation (comprising histidine, sorbitol, and polysorbate 80 at pH 5.5) exhibited a steady increase in aggregate formation over time even in the unexposed (dark) controls, specifically, the aggregate formation rate was reported as 0.075% per month during storage at 25°C, despite the absence of salt, which demonstrates that a salt-free composition, as taught by Qi, does not inherently prevent the progression of aggregation for a monoclonal antibody, and thus, there is no reasonable expectation that simply adopting a salt-free formulation based on Qi would yield superior stabilization and long-term clarity achieved by the claimed invention. This is not found persuasive because this is a misrepresentation of the teachings of Qi. The data presented in Figure 11 of Qi represents samples pre-exposed to light and is silent on any light conditions during storage [see page 3127, left column, third paragraph]. While the teachings of Qi as a whole are focused on photodegradation of the formulation after extensive light exposure, Qi does teach that the formulation of 100 mg/mL in a histidine, sorbitol, polysorbate 80 solution at pH 5.5, when it has no light exposure (i.e. a control), was colorless (i.e. no clouding) [see Figure 1, and Tables 3-4 of Qi]. Prior art is presumed enabled for all that it teaches. See MPEP 2121(I).
On page 6 of the remarks, Applicant argues that the inherent instability in Qi’s teaching serves as a teach-away from applying its composition to the human anti-IL-33 monoclonal antibody of the claimed invention and that there is no reasonable motivation to select a problematic formulation for a different, specific antibody. First, this is not found persuasive because a teaching away must be explicit, and Qi clearly teaches that the composition was colorless (i.e. had no clouding) when it was not exposed to light. Second, Applicant does not provide any rationale as to why one of ordinary skill in the art would only interpret the teachings of Qi to be limited to Figure 11 or why this example would undermine the rejection as a whole. Art is available for all that it teaches and is not limited to specific paragraphs and examples. Applicant is reminded that “arguments of counsel cannot take place of factually supported objective evidence” (see MPEP §2145). Applicant further argues the Examiner’s arguments presented in the previous office action relating to the teachings of Bickel and Arosio stating that as evidenced by these references, even subtle differences between IgG1 and IgG2 subclasses result in different aggregation conditions and therefore, the effect of salt on one protein cannot be generalized to the anti-IL-33 antibody of the claim invention. This is not found persuasive because Applicant does point to any specific teachings of Bickel and Arosio nor does Applicant provide any objective evidence to support this argument. Applicant is reminded that “arguments of counsel cannot take place of factually supported objective evidence” (see MPEP §2145).
On pages 6-7 of the remarks, Applicant argues that the decision to omit salt while maintaining stability for this specific antibody [the claimed antibody] was not a mere routine optimization but non-obvious step required under 35 U.S.C. § 103 at the time when the present application was filed. This is not found persuasive because the Examiner did not rely upon routine optimization to support a conclusion of obviousness for a salt-free composition. Rather, the Examiner relied upon the teachings of Fujino, Gillies, Presta, Janeway, Goklen, and Qi to support a conclusion of obviousness for the composition being salt-free and the Examiner clearly articulated these teachings in the rejection. See above. Further, Applicant points to Examples 14 and 15 of the specification to support the argument that the claimed formulation exhibits superior long-term stability and remains clear, an effect neither disclosed nor suggested by the cited references. This is not found persuasive because these results are not commensurate in scope with the claims. Example 14 is explicitly at concentrations of 10 mg/mL antibody, 10 mM histidine, 0.02% w/v polysorbate 80, and 3.6% w/v sorbitol with a pH of 6, and Example 15 is explicitly at concentrations of 150 mg/mL antibody, 10mM histidine, 0.02% w/v polysorbate 80, 4.0% sorbitol with a pH of 6. While Applicant argues that very specific conditions exhibit superior long-term stability and remain clear (i.e. no clouding/aggregation), these examples are narrower than what is claimed. Further, Applicants test of stability for Examples 14 and 15 was storing the formulations in a sealed glass vial for 1, 2, and 3 years at a temperature of 2-8 degrees Celsius, and the presence or absence of aggregation was confirmed by visual examination for 5 seconds each under a 2000 to 3750 Lux fluorescent lamp, against white and black board backgrounds [see 0081, Examples 14 and 15 of the instant specification]. Thus, these were only exposed to light for 5 seconds, which would be comparable to the formulations of Qi that were controls and were not exposed to light, and thus, were colorless (i.e. no clouding/aggregation).
On pages 7-8 of the remarks, Applicant argues that the experimental data showing that “10 mM salt can also inhibit clouding” in the specification does not detract from the unexpected effect observed when no NaCl is present and that the unexpected result is observed when the salt concentration is lowered at 10 M or less and when the composition contains no salt. This is not found persuasive because Example 10 demonstrates that clouding was inhibited with 10 mM sodium chloride at pH 4 to 6 and clouding was only observed when sodium chloride exceeded 30 mM and Example 2 states that Kd value was negative (aggregation increased) with NaCl addition of 50 mM or greater, suggesting that NaCl addition of less than 50 mM is desirable in the formulation. Thus, the clouding does not appear to be due to the presence of salt (i.e. NaCl), which Applicant claims, but rather clouding is dependent on the specific concentration of NaCl. Applicant’s results explicitly state that there was no clouding when 10 mM NaCl at pH 4 to 6 was present in the formulation and only when sodium chloride exceeded 30 mM was clouding observed. Thus, Applicant’s Examples in the specification support that the concentration of NaCl is a condition to be optimized (i.e. in order to improve the composition) and establishes that these conditions, when adjusted, lead to improved results. Optimizing conditions to obtain improved results is not equivalent to unexpected or unpredictable results. Additionally, the results of the instant application that Applicant relies upon to demonstrate unexpected results are not commensurate in scope with the instant claims. See MPEP 716.02(d). Applicant further argues that the remaining rejected claims incorporate all the features of Claim 1 through their dependencies and therefore, the dependent claims are also patentable over the prior art for at least the same reasons that Claim 1 is patentable as well as for their own patentable features. This is not found persuasive for all the reasons set forth above.
Conclusion
No claims are allowed.
THIS ACTION IS MADE FINAL. 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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/B.E.D./Examiner, Art Unit 1675
/JEFFREY STUCKER/Supervisory Patent Examiner, Art Unit 1675
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