DETAILED 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 .
Priority
This application claims benefit of priority to Foreign Application No. EP20184997.3 filed on 07/09/2020. Receipt is acknowledged of certified copies of papers required by 37 CFR 1.55. This application is also a 371 of PCT/EP2021/069090 filed on 07/09/2021. For the purposes of applying prior art, the effective filing date of the claimed invention is 07/09/2020.
Amendment and Claim Status
In the reply filed on 03/11/2026, Applicant amended claims 41-42, 49, 54 and 61 and added new claims 104-121. Claims 2-40, 43-48, 50-51, 53, 55-60, 62-93 are canceled. Claims 1, 94 and 101 are withdrawn by the Examiner as they are not encompassed by the elected group.
Claims 1, 41-42, 49, 52, 54, 61, 94, 101 and 104-121 are currently pending.
Claims 1, 94 and 101 are withdrawn.
Claims 41-42, 49, 52, 54, 61 and 104-121 are under examination.
Maintained Rejections (with modification as necessitated by amendment)
Claim Rejections - 35 USC § 103
The following is a quotation of 35 U.S.C. 103 which forms the basis for all obviousness rejections set forth in this Office action:
A patent for a claimed invention may not be obtained, notwithstanding that the claimed invention is not identically disclosed as set forth in section 102, if the differences between the claimed invention and the prior art are such that the claimed invention as a whole would have been obvious before the effective filing date of the claimed invention to a person having ordinary skill in the art to which the claimed invention pertains. Patentability shall not be negated by the manner in which the invention was made.
The factual inquiries for establishing a background for determining obviousness under 35 U.S.C. 103 are summarized as follows:
1. Determining the scope and contents of the prior art.
2. Ascertaining the differences between the prior art and the claims at issue.
3. Resolving the level of ordinary skill in the pertinent art.
4. Considering objective evidence present in the application indicating obviousness or nonobviousness.
This application currently names joint inventors. In considering patentability of the claims the examiner presumes that the subject matter of the various claims was commonly owned as of the effective filing date of the claimed invention(s) absent any evidence to the contrary. Applicant is advised of the obligation under 37 CFR 1.56 to point out the inventor and effective filing dates of each claim that was not commonly owned as of the effective filing date of the later invention in order for the examiner to consider the applicability of 35 U.S.C. 102(b)(2)(C) for any potential 35 U.S.C. 102(a)(2) prior art against the later invention.
Claims 41-42, 49, 52, 54, 104-107, 108, 110-114, 116 and 120 are rejected under 35 U.S.C. 103 as being unpatentable over Chorny et al. (WO 2005055949 A2, 06/23/2005) (IDS Reference of 03/03/2023, 1 Page, Abstract Only) in view of Liang et al. (Electrophoresis, 2006) and Baehner et al. (US 8268314 B2, 09/18/2012).
Regarding claim 41-42, 49, 54, 105-107 Chorny et al. disclose sustained release preparations composed of biocompatible complex microparticles (See entire document, Title). More specifically, Chorny et al. disclose a particle comprising a complex formed by a bioactive agent and a complexing agent (Claim 1 of Chorny et al.), wherein the bioactive agent taught includes a protein (Claim 8 of Chorny et al.) and the complexing agent is dextran or dextran sulfate (Claim 15 of Chorny et al.) wherein the molecular weight of dextran or dextran sulfate is 5 KDa to 500 KDa (Claim 16 of Chorny et al.). Sustained release preparations containing peptides and proteins have a broad field of use in medicine, for example, in cancer therapy (Page 3, Lines 24-25). Similarly, depending on the choice of the bioactive agent, the particle of the invention has a therapeutic activity for a desired application, such as cancer therapy (Page 10, Lines 14-17).
Chorny et al. further disclose a method of making particles wherein dextran sulfate is dissolved in water forming solution A, Platelet-Derived Growth Factor (PDGF) is dissolved in an aqueous solution of glucose, reading on an excipient, with a pH of 6.0 adjusted by acetate buffer or MES buffer, reading on the suspension comprising a buffer solution, forming solution B and then solution A is added to solution B. The obtained particle suspension, reading on the composition being a suspension, is then filtered to remove aggregates (Page 14, Lines 14-20, Example 1).
Chorny et al. do not explicitly disclose the dextran sulfate has an average molecular weight ranging from 30 kDa to 50 kDa nor do Chorny et al. disclose the protein is the bispecific antibody anti-VEGF/Ang2.
However, as discussed above, Chorny et al. do disclose the molecular weight of dextran or dextran sulfate is 5KDa to 500 KDa. 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 utilized dextran sulfate with a molecular weight ranging anywhere from 5 KDa to 500 KDa in the composition of Chorny et al. In the case where the claimed ranges “overlap or lie inside ranges disclosed by the prior art” a prima facie case of obviousness exists. See MPEP 2144.05(I). See also In re Wertheim, 541 F.2d 257, 191 USPQ 90 (CCPA 1976); In re Woodruff, 919 F.2d 1575, 16 USPQ2d 1934 (Fed. Cir. 1990).
Moreover, Liang et al. disclose interactions between granulocyte colony-stimulating factor (G-CSF) and dextran sulfate are dependent on the chain lengths and sulfate contents of the saccharides (See entire document, Abstract). It is noted G-CSF is a protein. Further, Liang et al. disclose dextran sulfate with a molecular mass of 40 kDa had a binding affinity to G-CSF with the binding constant being 1.01 x 106 M-1 while dextran sulfate with a molecular mass of 8 kDa had no affinity to G-CSF.
Thus, based upon the disclosure of Chorny et al., it would have been obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to have utilized dextran sulfate with a molecular weight ranging from 5 KDa to 500 KDa with a reasonable expectation of success in the composition of Chorny et al. Additionally, it would have been obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to have utilized dextran sulfate with a molecular mass of 40 kDa in the composition of Chorny et al. because Liang et al. disclose dextran sulfate interactions between the growth factor protein G-CSF and dextran sulfate are dependent upon chain lengths and sulfate contents and therefore, it would be obvious that interactions between other proteins, such as anti-VEGF/Ang-2, would also be dependent on chain lengths and sulfate contents. Thus, it would be obvious to utilize dextran sulfate with a molecular weight of 40 kDa in the composition of Chorny et al. because it falls within the given range disclosed by Chorny et al. and because Liang et al. disclose dextran sulfate with a molecular mass 40 kDa has an affinity to G-CSF, while other molecular masses do not, and it would be obvious to utilize the same molecular mass dextran sulfate with another protein.
Regarding the elected species of protein being the bispecific antibody anti-VEGF/Ang2, as discussed above, Chorny et al. disclose the bioactive agent can be a protein. Antibodies are proteins. Additionally, Baehner et al. disclose bispecific antibodies against human VEGF and against human ANG-2 (See entire document, Abstract). Anti-VEGF neutralizing antibodies suppress the growth of a variety of human tumor cell lines in mice (Column 2, Lines 7-8). Further, it has been found that the bispecific antibodies against human VEGF and human ANG-2, reading on an anti-VEGF/Ang2 antibody, according to the current invention have improved characteristics such as biological or pharmacological activity, pharmacokinetic properties or toxicity as well as increased in vivo tumor growth inhibition and/or inhibition of tumor angiogenesis when compared to the monospecific parent antibodies against VEGF and ANG-2 (Column 28, Lines 43-49).
Thus, it would have been obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to have utilized any protein as the bioactive agent in the composition of Chorny et al. because Chorny et al. specifically disclose the bioactive agent can be a protein. Additionally, it would have been obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to have utilized the bispecific antibody anti-VEGF/Ang2 in the composition of Chorny et al. as antibodies are proteins and the bispecific antibody anti-VEGF/Ang2 was a known antibody for treating cancer as taught by Baehner et al. Thus, it would have been obvious to utilize a known antibody for treating cancer in the composition of Chorny et al. as Chorny et al. specifically state their composition is useful for treating cancer based upon the bioactive agent utilized.
It is noted claim 41 and amended claim 54 are drawn to a product-by-process. "[E]ven though product-by-process claims are limited by and defined by the process, determination of patentability is based on the product itself. The patentability of a product does not depend on its method of production. If the product in the product-by-process claim is the same as or obvious from a product of the prior art, the claim is unpatentable even though the prior product was made by a different process." In re Thorpe, 777 F.2d 695, 698, 227 USPQ 964, 966 (Fed. Cir. 1985). To that end, under the broadest reasonable interpretation, the process of claims 41 and 54 result in a reversible protein complex comprising dextran sulfate with an average molecular weight ranging from 30 kDa to 50 kDa and a protein in a suspension. Thus, the instant composition of claims 41 and 54 is obvious over the combination of Chorny et al., Liang et al. and Baehner et al. for the reasons discussed above.
Regarding claim 52, it is noted the instant Specification states “it was surprisingly found by the inventors that RPCs comprising dextran sulfate and/or chondroitin sulfate as the complexing agents dissociate at physiological pH and ionic strength” (Specification, Page 57, Last Paragraph). Thus, as Chorny et al. utilize dextran sulfate as the complexing agent in their composition, it appears, absent evidence to the contrary, that their composition, comprising a protein and dextran sulfate, would inherently dissociate at physiological pH and ionic strength because dextran sulfate is the complexing agent utilized.
Regarding claim 104, Chorny et al. disclose the cationic agent, reading on positively charged, is a protein (Page 5, Lines 26-27).
Regarding claim 108, Chorny et al. disclose the complexing agent is negatively charged (Page 11, Line 6).
Regarding claim 110, this limitation does not change the structure of the composition, just indicates what the composition does. Thus, as the prior art teaches the complex, it would inherently have the same properties, being a higher melting temperature compared to the uncomplexed protein.
Regarding claim 111, Chorny et al. do not disclose the protein concentration in the suspension ranges from 50-250 mg/mL or 100-200 mg/mL.
However, Chorny et al. disclose the dextran sulfate solution was added to the protein solution at a volume of 100-150 µl:10 ml (Page 14, Example 1). Chorny et al. disclose the protein-polysaccharide ratio is an important factor regarding the stability of the complex (Page 3, Lines 10-11).
Thus, it would have been obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to have utilized an amount of protein in the suspension that would allow for the stability of the complex as the protein-polysaccharide ratio was known to effect the stability as taught by Chorny et al. Therefore, one of ordinary skill in the art would select an amount of protein, including 50-250 mg/mL or 100-200 mg/mL, that would provide an appropriate ratio of protein to polysaccharide motivated by the desire to create a stable complex of the two.
Regarding claim 112, Chorny et al. disclose subjecting the complexed particles to a release medium to facility disassociation (Page 15, Lines 17-19). Thus, as the particles disassociate, there will be uncomplexed complexing agent in the suspension.
Regarding claim 113, Chorny et al. disclose the mixture spontaneously associates into electrostatically stabilized ion-pair particles sized from about 1 nm to about 1000 microns, forming a particle suspension (Page 13, Lines 19-21).
In the case where the claimed ranges "overlap or lie inside ranges disclosed by the prior art" a prima facie case of obviousness exists. See MPEP 2144.05(I). Thus, it would have been obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to have utilized any particle size between 1 nm to about 1000 microns, which fully encompasses the claimed range, because this was a known and effective range as taught by Chorny et al.
Regarding claim 114, Chorny et al. disclose the particles can be stored freeze-dried and stored for later use (Page 13, Line 28-29).
Regarding claim 116, as Chorny et al. teach the complex, it would inherently have the same properties, including being stable for at least 4 weeks at 4°C.
Regarding claim 120, Chorny et al. disclose the pH of the aqueous solution is about 1 to about 13 (Page 13, Lines 16-18).
In the case where the claimed ranges "overlap or lie inside ranges disclosed by the prior art" a prima facie case of obviousness exists. See MPEP 2144.05(I). Thus, it would have been obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to have utilized any pH between 1 to about 13, which fully encompasses the claimed range, because this was a known and effective pH range as taught by Chorny et al.
Claims 41-42, 49, 52, 54, 61 and 104-121 are rejected under 35 U.S.C. 103 as being unpatentable over Chorny et al. (WO 2005055949 A2, 06/23/2005) (IDS Reference of 03/03/2023, 1 Page, Abstract Only) in view of Liang et al. (Electrophoresis, 2006) and Baehner et al. (US 8268314 B2, 09/18/2012) and further in view of Larson et al. (US 20180085463 A1, 03/29/2018).
Regarding amended claim 61 and new claim 117, Chorny et al. disclose the delivery route of the particles of the invention is preferably by a parenteral route, i.e., an injection, including intravenously and intramuscularly (Page 9, Lines 3-6).
Chorny et al. do not disclose the composition is injectable through a 26G needle nor do Chorny et al. disclose the suspension has a viscosity ranging from 2 to 20 cP when measured at 20°C.
However, Larson et al. disclose concentrated, low-viscosity, low-volume pharmaceutical formulations of proteins that can be rapidly and conveniently administered by subcutaneous or intramuscular injection instead of via lengthy intravenous infusion (See entire document, Abstract). Increased viscosity is one of the key challenges encountered in concentrated protein compositions affecting both production processes and the ability to readily deliver such compositions by conventional means (Paragraph [0006]). Highly viscous liquid formulations are difficult to manufacture, draw into a syringe and inject subcutaneously or intramuscularly (Paragraph [0007]). The use of force in manipulating the viscous formulations can lead to excessive frothing, which may further denature and inactive the therapeutically active protein (Paragraph [0007]). Highly viscosity solutions also require larger diameter needles for injection and produce more pain at the injection site (Paragraph [0007]). The viscosity of the formulations is less than 20 cP, less than 15 cP and even less than or about 10 cP at about 25°C (Paragraph [0024]). The reduced-viscosity formulations have improved injectability and can readily be injected through needles of about 18-32 gauge (Paragraph [0081]).
Thus, it would have been obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to have manipulated the viscosity of the composition of Chorny et al. into a low viscosity composition, including having a viscosity less than 20 cP, so that it would be readily injectable through a needle, including a gauge size from 18 to 32, and could be delivery intramuscularly or intravenously as that is the preferred delivery method of Chorny et al. and Larson et al. specifically teach low-viscosity protein compositions can be rapidly and conveniently administered by subcutaneous or intramuscular injection. One of ordinary skill in the art would be motivated to create a low-viscosity composition that is easily drawn into and injected out of a smaller needle because highly viscous liquid formulations require larger diameter needles that cause pain at the injection site and additionally require extra force which can lead to excessive frothing and the denaturing and inactivation of the therapeutically active protein as taught by Larson et al.
Claims 41-42, 49, 52, 54, 104-116 and 118-121 are rejected under 35 U.S.C. 103 as being unpatentable over Chorny et al. (WO 2005055949 A2, 06/23/2005) (IDS Reference of 03/03/2023, 1 Page, Abstract Only) in view of Liang et al. (Electrophoresis, 2006) and Baehner et al. (US 8268314 B2, 09/18/2012) and further in view of Ristroph et al. (Nanoscale Advances, 2019).
Regarding claim 109, Chorny et al. do not explicitly state their complexing agent comprise a hydrophobic moiety.
However, Ristroph et al. disclose hydrophobic ion pairing is a method to modulate the solubility of charged hydrophilic molecules ranging in class from small molecules to large enzymes (See entire document, Abstract). It is noted reversible protein complexes are also referred to a hydrophobic ion pairing complexes as evidenced by the instant Specification (Specification, Page 2, Paragraph 2). In hydrophobic ion pairing, charged hydrophilic molecules are ionically paired with oppositely-charged molecules that includes hydrophobic moieties (Abstract).
Thus, it would have been obvious to one of ordinary skill in the art before the effective filing date of the claimed invention for the complexing agent of Chorny et al. to have a hydrophobic moiety so it could ionically pair with the antibody, which is the hydrophilic molecule in the instant case, motivated by the desire to effectively pair the two components as taught by Ristroph et al.
Regarding claim 115, as discussed above, Chorny et al. disclose freeze-drying, or lyophilization.
Chorny et al. do not disclose spray drying.
However, Ristroph et al. disclose a means of formulating microparticles via spray drying.
Thus, it would have been obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to have spray dried the composition of Chorny et al. as an alternative to freeze-drying the composition as this was another known and effective means of formulating microparticles as taught by Ristroph et al.
Regarding claims 118-119, Chorny et al. disclose mixing aqueous solutions of the bioactive compound, which is positively charged, and the complexing agent, which is negatively charged, and it spontaneously associates into electrostatically stabilized ion-pair particles under a specific pH, preferably pH 5.5-6.0 (Page 13, Lines 16-20). Meaning at a pH of 5.5-6.0, the bioactive compound and the complexing agent still carry a charge. The isoelectric point is the pH at which one of the component has no net charge.
Chorny et al. do not disclose the pH of the suspension is lower than the isoelectric point of the protein, or more specifically, 1 to 3 pH units lower than the isoelectric point of the protein.
However, Ristroph et al. disclose the many uses of hydrophobic ion pairing (HIP) (See entire document, Abstract). Ristroph et al. teach counterions must be charged to ionically complex and sulfate anions are essentially always charged in aqueous environments (Page 4216, Right Column, Paragraph 3). Additionally, operating at a pH near one components pKa is not advised because charge ratios can be hard to predict and control (Page 4216, Right Column, Paragraph 3). However, with protein drugs, the isoelectric point is a straightforward parameter to use rather than trying to account for the pKa (Page 4222, Right Column). De-complexation is driven by counterion competition by salts or pH-driven charge negation. Salt competition occurs when salts in the medium are able to access the complex and outcompete the hydrophobic ion pair which leads to disassociation with a low chance of recomplexation due to the high ionic strength. The pH driven decomplexation occurs due to the protonating or deprotonating of one of the charged species (Page 4227, Left Column, Paragraph 3). Complexation formation, dissociation and release have all been found to be a function of bulk ionic strength with it being difficult to form complexes at a high ionic strength due to charge screening. (Page 4227, Right Column, Paragraph 4). Additionally, peptides and proteins are subject to degradation under basic conditions so shifting the pH to strongly acidic is likely preferable while also keeping in mind that the complexing counterions are subject to protonation or deprotonation under extreme pH conditions as well (Page 4214, Left Column, Paragraphs 2-3).
Thus, it would have been obvious to one of ordinary skill in the art for the pH of the suspension of Chorny et al. to not be equal to the isoelectric point of the protein because the complex would disassociate at the isoelectric point of the protein because the protein would no longer have a charge and the protein and complexing agent spontaneously associate into electrostatically stabilized ion-pair particles due to their respective charges as taught by Chorny et al. It would have been further obvious for the pH of the suspension of Chorny et al. to be lower than the isoelectric point of the protein so that the protein does not degrade because Ristroph et al. teach proteins are subject to degradation under basic conditions. As the pH of the suspension of Chorny et al. was 5.5 to 6.0 at the time of complexation, the pH would have to be lowered to remain acidic. Additionally, it would have been obvious for the pH to be any number of pH units lower than the isoelectric point of the protein, including 1 to 3, that would not push the pH to the extreme and results in protonation or deprotonation of the complexing counterion, being dextran sulfate in the instant case, motivated by the desire to keep the two components of the complex charged so they do not disassociate.
Regarding claim 121, Chorny et al. do not disclose the suspension has an ionic strength ranging from 20 to 50 mM.
However, as discussed above, Ristroph et al. disclose complexation formation, dissociation and release have all been found to be a function of bulk ionic strength with it being difficult to form complexes at a high ionic strength due to charge screening. (Page 4227, Right Column, Paragraph 4)
Thus, it would have been obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to have selected an ionic strength suitable for the desired outcome, being complexation, dissociation or release in the suspension of Chorny et al. because Ristroph et al. disclose all three are a function of ionic strength. Therefore, one of ordinary skill in the art would select an ionic strength, including from 20 to 50 mM, motivated by the desire to either effectively complex the protein and complexing agent or to dissociate the two because ionic strength was a known and effective means of achieving both.
USC § 103 - Response to Arguments
Applicant's arguments filed 03/11/2026 have been fully considered but they are not persuasive.
Applicant argued the broad range of Chorny et al. does not render obvious the narrower range as instantly claimed.
The Examiner disagrees. As stated in the Non-Final and above, a prima facie case of obviousness exists when the claimed ranges overlap or lie inside the ranges disclosed by the prior art absent evidence of unobviousness. The primary reference, Chorny et al., teaches a range of dextran sulfate from 5 KDa to 500 KDa. Therefore, it would be obvious to utilize a dextran sulfate at any weight within said range. See MPEP 2144.05(I).
Applicant further argued the arrival to the claimed range of dextran sulfate is based on impermissible hindsight.
In response to applicant's argument that the examiner's conclusion of obviousness is based upon improper hindsight reasoning, it must be recognized that any judgment on obviousness is in a sense necessarily a reconstruction based upon hindsight reasoning. But so long as it takes into account only knowledge which was within the level of ordinary skill at the time the claimed invention was made, and does not include knowledge gleaned only from the applicant's disclosure, such a reconstruction is proper. See In re McLaughlin, 443 F.2d 1392, 170 USPQ 209 (CCPA 1971). As stated above, Chorny et al. teach a range of dextran sulfate from 5 KDa to 500 KDa. Therefore, it would be obvious to utilize a dextran sulfate at any weight within said range. See MPEP 2144.05(I). Applicant has not met the burden of nonobviousness that would render the narrower range nonobvious.
Applicant argued Liang et al. teach away from the claimed range because the dextran sulfate has no nearly no effect on inhibiting the proliferation of the leukemia cells.
The Examiner disagrees. First, the range is obvious solely in view of Chorny et al. Second, Liang et al. was utilized to show this specific dextran sulfate was utilized in the prior art for interacting with other proteins, thus, it would have been obvious to utilize the same molecular mass dextran sulfate with another protein. Additionally, Liang et al. specifically state dextran sulfate 40 has more binding sites than dextran sulfate 50 while dextran sulfate 50 is bigger and sterically hinders binding between the protein. Therefore, Liang et al. do not teach away from dextran sulfate 40 regarding protein interactions. Even such, even without Liang et al., the claimed range is obvious in view of Chorny et al. for the reasons stated immediately above.
Applicant further argued unexpected results wherein nearly 100% complexation and dissociation efficiency at physiological pH with dextran sulfate 40 kDa and points to Paragraph [0130] and Figure 8.
Respectfully, it is unclear what the unexpected property is. Figure 8 is noted for the percent complexation and disassociation. However, the unexpected result is unclear because Chorny et al. also teach particles that complex and subsequently disassociate. The claims do not recite any parameters for disassociation that would distinguish the instant complex from the complex of the prior art. Additionally, the claims are not commensurate in scope with the showing. The broadest claims, being claim 41-42 and 54, are directed to any protein while Figure 8 shows complexation and disassociation of very specific antibodies. Thus, the unexpected result is unclear and the claims are not commensurate in scope with the showing.
Applicant argued the composition of Chorny wouldn’t necessarily meet the limitations of claim 52 and argued the Examiner did not provide evidence of such.
It is the Examiner’s position that Chorny et al. meet the limitations of claim 52 because they disclose a complex comprising a protein and dextran sulfate, including suggesting the claimed weight range of dextran sulfate, therefore, their complex would implicitly have the same properties, including disassociating at physiological pH. Additionally, there are two separate embodiments within claim 52. The second embodiment regarding disassociation when diluted to a specific concentration is an intended use. Thus, as the prior art suggests the same structure, it would necessarily be capable of performing the intended use.
Conclusion
Claims 41-42, 49, 52, 54, 61 and 104-121 are rejected.
No claims are 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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/A.T.W./Examiner, Art Unit 1653
/SHARMILA G LANDAU/Supervisory Patent Examiner, Art Unit 1653
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