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 .
Response to Amendment
Applicant’s remarks and amendments filed 3/17/2026, in response to the non-final rejection mailed 12/17/2025, are acknowledged and have been fully considered.
Any previous rejection or objection not mentioned herein is withdrawn.
Applicant’s amendment to the claims is acknowledged. This listing of the claims replaces all prior versions and listings of the claims.
Applicant’s arguments regarding the rejections of the claims under 35 U.S.C. §§ 102 and 103 are persuasive, in view of the amendments to the claims to require at least three or all four of the requirement modification limits, as now recited in claim 1. None of the cited prior art explicitly teaches an HSA product having these specific features.
Claims 18, 20-5, and 27-28 remain withdrawn as being drawn to non-elected inventions, there being no allowable generic or linking claim.
Claims 1, 4-9, and 26 are pending and have been examined on the merits.
Terminal Disclaimer
The terminal disclaimer filed on 3/17/2026, disclaiming the terminal portion of any patent granted on this application which would extend beyond the expiration dates of App. No. 18/251,221 has been reviewed and is accepted. The terminal disclaimer has been recorded. Accordingly, the rejections on the grounds of non-statutory double patenting are moot.
Information Disclosure Statement
The information disclosure statement filed 3/17/2026 fails to comply with 37 CFR 1.98(a)(3)(i) because it does not include a concise explanation of the relevance, as it is presently understood by the individual designated in 37 CFR 1.56(c) most knowledgeable about the content of the information, of each reference listed that is not in the English language.
As explained in the rejection mailed 12/17/2025, there are no provided English language translations for the foreign language references: JP2019-528269; JP2023-534363; and “JP Application No. 2023-5511637, Office Action dated August 4, 2025”.
Further, the IDS filed 3/17/2026 lacks a timing statement as specified in 37 CFR 1.97(e), nor a timing fee as set forth in 37 CFR 1.17(p), and was filed after the non-final rejection mailed 12/17/2025. It has been placed in the application file, but the information referred to therein has not been considered.
Claim Interpretation
The following terms recited in the claims have been interpreted according to the definitions provided in the specification, in accordance with the level of ordinary skill in the art, as previously set forth in the rejection mailed 12/17/2025.
The specification states that the term "young and undamaged", as used in the preamble of claim 1, means that the HSA protein is in a fresh status and does not “have extensive damages as compared to a specific HSA preparation”, and the specification gives an example of “a HSA preparation obtained from an individual of 30 years old”.
Under the B.R.I. of the terms, in view of the specification, the element of “young and undamaged” HSA is being interpreted as rHSA, with minimal medication, and without exposure to oxidation or proteolytic chemicals (i.e. sources of “damage” to a protein). The specification also states: “A skilled artisan will understand that the term "young and undamaged" HSA does not strictly require that there is absolutely no damage. It is very difficult, if not totally impossible, to prepare such perfect preparations. For the purpose of the present invention, a HSA preparation comprising limited damages is still acceptable.” From the disclosure, under the B.R.I. of the claim, new recombinantly-produced HSA without oxidation meets this limitation.
In claim 26, the term "pharmaceutically acceptable carrier" is being interpreted as encompassing “any of the standard pharmaceutical carriers, buffers and excipients, including buffered saline solution, water, and emulsions (such as an oil/water or water/oil emulsion), and various types of wetting agents and/or adjuvants” (see specification, page 4).
Claim Objections
Claims 1 and 26 are objected to because of the following informalities:
Claim 1 recites “being greater than 50%” in line 4, where the word “being” is redundant. This is also the case for “being lower than 60” in line 6. It is recommended to remove the word “being” from these limitations for proper grammar.
Claim 1 recites “Ellman's method”, in line 5. Although this is a term of art that appears to be well recognized, as evidenced in the specification, for improved clarity and specificity, it is recommended that the claim be amended to recite that “measuring the absorbance increase at 412nm after addition of 5, 5'-dithio-bis-2(-nitrobenzoic acid) (DTNB)” is used for the detection (see pages 6 and 21 of the specification).
Claim 26 recites “in claim1” in line 3, which should say “in claim 1”.
Appropriate correction is required.
Claim Rejections - 35 USC § 112(b) - New Rejection
The following is a quotation of 35 U.S.C. 112(b):
(b) CONCLUSION.—The specification shall conclude with one or more claims particularly pointing out and distinctly claiming the subject matter which the inventor or a joint inventor regards as the invention.
The following is a quotation of 35 U.S.C. 112 (pre-AIA ), second paragraph:
The specification shall conclude with one or more claims particularly pointing out and distinctly claiming the subject matter which the applicant regards as his invention.
Claims 1, 4-9, and 26 are rejected under 35 U.S.C. 112(b) or 35 U.S.C. 112 (pre-AIA ), second paragraph, as being indefinite for failing to particularly point out and distinctly claim the subject matter which the inventor or a joint inventor (or for applications subject to pre-AIA 35 U.S.C. 112, the applicant), regards as the invention.
Claim 1 contains the phrase “Protein Carbonyl Content Assay Kit” in reference to determining the level of protein carbonyl modification. There is no specific definition nor further information in the claim on the referenced Protein Carbonyl Content Assay Kit. From the specification, this appears to be in reference to a single commercial product sold by Abcam, having product identifier ab126287 (see pg. 7, lines 3-10 of the specification). “Protein Carbonyl Content Assay Kit” is not a trademarked term, however it appears to be in reference to a specific kit, the products and composition of which are not disclosed in the specification nor readily known in the art. There is no way to tell if the claim is inclusive of any and all generic protein carbonyl content assay kits or if only the one exemplified in the specification would be sufficient to achieve the desired result of the claim. Further, assays can be performed without a kit, given that all of the components are readily known and available to one skilled in the art. However, the claim as written appears to exclude such generic assays, and only can be performed with a kit. Because the metes and bounds of the limitation requiring the “Protein Carbonyl Content Assay Kit” are undefined, the resulting claim is indefinite.
All other claims depend directly or indirectly from the rejected claims and are, therefore, also rejected under 35 U.S.C. 112(b) or 35 U.S.C. 112 (pre-AIA ), second paragraph, for the reasons set forth above.
For compact prosecution, the claimed properties have been interpreted according to the B.R.I. of the claims as reciting inherent or innate properties of an HSA protein. The manner in which the properties are tested does not affect the presence or lack of the recited chemical modification on the claimed composition.
Claim Rejections - 35 USC § 101 - Rejection Maintained
(modified as necessitated by Applicant’s amendment)
35 U.S.C. 101 reads as follows:
Whoever invents or discovers any new and useful process, machine, manufacture, or composition of matter, or any new and useful improvement thereof, may obtain a patent therefor, subject to the conditions and requirements of this title.
Claims 1, 4-9, and 26 are rejected under 35 U.S.C. 101 because the claimed invention is directed to a natural phenomenon without significantly more.
For determining subject matter eligibility, the following analysis was considered, per MPEP § 2106.
Patent Eligibility Analysis Step 1: Step 1 of the eligibility analysis asks: is the claim to a process, machine, manufacture or composition of matter? Yes, the claims are directed to a composition. (Claims 1, 4-9 and 26, STEP 1: YES).
Patent Eligibility Analysis Step 2A Prong 1: Step 2A, prong 1 asks: does the claim recite an abstract idea, law of nature, or a natural phenomenon (a product of nature)?
Claim 1 recites a preparation, a composition, of human serum albumin comprising at least three or all of the following properties: (1) a ratio of free thiol greater than 50% (free thiol HSA compared to total HSA) at the Cys-34 residue, determined by Ellman’s method; (2) a level of advanced glycation end-product (AGE) that is lower than 60 µg/g protein, determined by an ELISA; (3) a level of carbonylation lower than 1.7 nmol/mg protein, determined by a protein carbonyl content assay (according to the interpretation described above), and (4) a level of homocysteinylation lower than 5 nmol/g protein, determined by ELISA, as compared to an endogenous HSA preparation obtained from a young individual of human.
Dependent claims 4-8 recite additional limitations regarding the properties of the HSA.
Claim 9 recites that the preparation is produced recombinantly or purified from plasma.
Claim 26 recites a pharmaceutical composition, comprising the preparation of young and undamaged human serum albumin as defined in claim 1 and a pharmaceutically acceptable carrier, which includes buffered saline solutions, water, and emulsions.
The claims recite a natural product, the preparation of human serum albumin.
Thus, the B.R.I. of claims 1, 4-9 and 26 includes limitations encompassing natural products.
The disclosure discusses the use of freshly prepared recombinant serum albumin (see page 11 and Figure 12). The instant claims encompass a natural HSA protein having none of the recited modifications. MPEP § 2106.04(c)I. states that “if the nature-based product limitation is naturally occurring, there is no need to perform the markedly different characteristics analysis because the limitation is by definition directed to a naturally occurring product and thus falls under the product of nature exception”. In the instant case, a fully unmodified HSA with no exposure to oxidizing conditions and having no modifications will fall under this definition. However, even if the claimed preparation could be considered a nature-based product having some man-made intervention, affecting to some extent the claimed characteristics of the properties compared to the natural product, then the markedly different characteristics (MDC) analysis below has been applied.
When a claim recites a nature-based product limitation, the markedly different characteristics (MDC) analysis is used to determine whether the natural product has markedly different characteristics from its natural counterpart (MPEP 2106.04(c)).
The first step is to determine the appropriate natural counterpart for the claimed product to be compared against. In this case, the appropriate natural counterpart for the preparation of human serum albumin of claims 1 and 4-9 would be a natural HSA protein.
For claim 26, the proper comparison is to the HSA protein in a carrier within the limits of the claim, including water or a buffered solution (i.e. a naturally occurring buffered solution such as plasma). MPEP § 2106.04(c) explains “Where the claim is to a nature-based product produced by combining multiple components, the markedly different characteristics analysis should be applied to the resultant nature-based combination, rather than its component parts.”
The second step in the MDC analysis is to identify appropriate characteristics to compare. Appropriate characteristics can be expressed as the nature-based product’s structure, function, and/or other properties, and are evaluated on a case-by-case basis. In this case, the appropriate characteristics include: biological functions or activities, phenotypic characteristics which include functional and structural characteristics such as the shape, size, color, and behavior of an organism, and structure and form (chemical, genetic or physical) of the natural components. These include the sequence and structure of the HSA, which is unchanged from the natural product. The functional and chemical properties include, but are not solely limited to therapeutic effects, the amino acid sequence, molecular weight, the ratio of free thiol in Cys-34 residue, the amounts of glycation end-product (AGE), the lower level of carbonylation, and/or the levels of homocysteinylation, which are recited in the disclosure.
The final step in the markedly different characteristics analysis is to compare the characteristics of the claimed nature-based product to its naturally-occurring counterpart in its natural state, in order to determine whether the characteristics of the claimed product are markedly different. The courts have emphasized that to show a marked difference, a characteristic must be changed as compared to nature, and cannot be an inherent or innate characteristic of the naturally-occurring counterpart or an incidental change in a characteristic of the naturally occurring counterpart. Myriad, 569 U.S. at 580, 106 USPQ2d at 1974-75.
In order to be markedly different, the inventor must have caused the claimed product to possess at least one characteristic that is different from that of the counterpart (MPEP § 2106.04(c).II.C.). If there is no change in any characteristic, the claimed product lacks markedly different characteristics, and is a product of nature exception.
No characteristics of the naturally-derived product are markedly changed by a process of purification, nor is there any disclosure of a difference from the instantly claimed protein preparation and the “young and undamaged” HSA protein as it exists in nature, according to the interpretation described above. Detecting the presence or amount of a natural phenomenon is not patent eligible, see MPEP§2106.04(c).I.C: "the existence and location of cffDNA is a natural phenomenon [and thus] identifying its presence was merely claiming the natural phenomena itself." Rapid Litig. Mgmt., 827 F.3d at 1048, 119 USPQ2d at 1374, (explaining the holding in Ariosa Diagnostics, Inc. v. Sequenom, 788 F.3d 1371, 115 USPQ2d 1152 (Fed. Cir. 2015))”.
Turning to the literature, one can determine that HSA proteins with none (i.e. with free or reduced thiol) or varying amounts of oxidative modifications are found naturally.
Era et al. (“Age-related change in redox state of human serum albumin.” Biochimica et biophysica acta vol. 1247,1 (1995): 12-6, cited in the specification) demonstrates that in healthy, 20-yr old humans, HSA in the reduced form (termed therein human mercaptalbumin, or HMA) was found at a mean value of 0.76 + 0.04 (n = 54), and in older individuals at a fraction of 0.48 + 0.06 (n = 183) (Abstract). Era teaches that it is known that HSA/HMA has one free sulfhydryl residue in position 34 (Cys-34) (pg. 12, left col). Interestingly Era also demonstrates that time-dependent changes of f(HMA) values in HSA, depending on the temperature it is stored at (see Table 2). Thus, Era et al provides evidence that the relative amount of free thiol at Cys-34 of HSA is a natural and condition/environment dependent property of the protein.
Anguizola et al. ("Glycation of human serum albumin." Clinica chimica acta 425 (2013): 64-76.) discusses measurements of glycated albumin, with an interest in using glycation of albumin as an indicator for glycemic control in diabetic patients, and discuss the natural phenomena involving the formation of Advanced glycation end-product, or AGE (see Abstract, Figure 1). See also Table 1 of Anguizola, describing a number of modification sites and adducts that have been reported for glycated human serum albumin (HSA). Anguizola states that studies estimate that 6–13% of HSA is glycated in healthy individuals, with this amount increasing by up to 20–30% in diabetic patient (see pg 67, left col, 2nd para). Thus, naturally occurring HSA may be found with minimal glycation and with extensive modification including AGEs.
Jana et al. (“Specificity of age-related carbonylation of plasma proteins in the mouse and rat.” Archives of biochemistry and biophysics vol. 397,2 (2002): 433-9, cited in the instant specification) teaches that, at least in mice and Rhesus monkeys, the amount of carbonylation of plasma albumin increases with age (Abstract), and states that this is a natural selective phenomenon. Jana suggests that carbonylated albumin can be a possible marker of oxidative damage in the plasma (pg 438, final paragraph).
Colombo et al. (“Redox Albuminomics: Oxidized Albumin in Human Diseases.” Antioxid. Redox Sign. 17, (2012):1515-1527, cited in the instant specification) reviews the role of modified albumins in oxidative stress and suggests that the albumin redox state may serve as a global biomarker for the redox state in the body in various human diseases (Abstract). Colombo states: “In plasma of healthy young adults, 70%– 80% of total HSA contains the free sulfhydryl group of Cys34” (page 1518, left col). Colombo also discloses that carbonylated albumin (Alb-CO) is present in high levels in various human diseases and pathophysiological conditions (see Table 2, and pages 1519-1521).
Jakubowski (“Homocysteine is a protein amino acid in humans. Implications for homocysteine-linked disease”. J. Biol. Chem. 277, 30425-30428 (2002), cited in the instant specification) describes that homocysteine bound by amide or peptide linkages (Hcy-N-protein) is present in human serum albumin (Abstract, Table II). Jakubowski discloses that for human albumin homocysteine modified protein was up to 2.8 ± 0.7 µM (in 50mg/mL of albumin).
Regazzoni et al. (“Human serum albumin cysteinylation is increased in end stage renal disease patients and reduced by hemodialysis: mass spectrometry studies.” Free radical research. 2013 Mar 1;47(3):172-80. DOI: 10.3109/10715762.2012.756139), discloses covalent modifications of human serum albumin (HSA) in end stage renal diseases (ESRD) non-diabetic patients and age-matched healthy subjects (n = 10, 20–60 yr) (Abstract), including the natural occurrence of homocysteinylation (pg. 172, right col, and Figure 2). Regazzoni also states that “As a further confirmation, we found that HSA-Cys is significantly elevated in older subjects as compared to HSA-Cys in younger subjects” (pg. 178, right col).
The cited art and the instant disclosure provide substantial evidence that there are no markedly different characteristics of the claimed composition when compared to naturally-occurring HSA, as the levels of modification are variable in vivo, and the claims encompass newly produced, fully reduced HSA, having no oxidation or modification.
Thus, after consideration, the recited chemical properties and modifications (or lack thereof) amount to nothing more than naturally occurring phenomena, and the claimed HSA having low amounts of one or more of these is not markedly different than natural HSA, obtained from a young or healthy subject, or even to HSA obtained from an in vitro cultured cell.
Regarding a recombinantly-produced protein, if the protein is identical in characteristics to the naturally occurring product, then the manner in which it is produced is immaterial to the eligibility, unless there is substantial evidence of a changed property, compared to its natural counterpart, in this case naturally occurring HSA protein. See MPEP § 2106.04(c).I.B.
The claimed subject matter encompasses a HSA protein having none of the recited modifications. Such a protein, either produced recombinantly or purified would not have any markedly different characteristics or functional properties than the natural protein.
When considering the composition of claim 26, there is no evidence or suggestion that the claimed product has any markedly different characteristic than a combination of the individual naturally occurring products, i.e. the natural protein without any modifications in a natural aqueous solution, including but not limited to water or plasma.
Therefore, the claimed product lacks markedly different characteristics, and is a product of nature exception (Claims 1, 4-9, and 26, Step 2A, Prong 1: YES).
Patent Eligibility Analysis Step 2A Prong 2: Step 2A, prong 2 asks: does the claim recite additional elements that integrate the judicial exception into a practical application?
Claims 1 and 4-8 do not recite any additional elements other than the product of nature exception and intrinsic properties thereof, as set forth above. These claims do not integrate the judicial exception into a practical application because the functional limitations merely reflects innate capabilities of the natural product, as determined from comparison to another natural product. The modifications are in fact themselves drawn to naturally occurring phenomena, and there exists evidence of naturally occurring HSA having none or low amounts of these modifications. Further, these elements do not require a particular or directed application.
Claim 9 recites that the protein is produced recombinantly or is purified, but this doesn’t differentiate the claims from the natural product, nor does it recite a practical application thereof.
Claim 26 recites a pharmaceutical composition having a suitable carrier, but this does not apply the judicial selection in any specific and practical application. There is no practical application or implementation of the natural product recited.
Therefore, the judicial exception is not integrated into a practical application because the claims do not recite any additional elements other than the naturally-occurring product(s) and innate functional characteristics thereof (Claims 1, 4-9 and 26, Step 2A, Prong 2: NO).
Patent Eligibility Analysis Step 2B: Does the claim recite additional elements that amount to significantly more than the judicial exception?
The recitation of an innate property or characteristic of a natural product does not result in significantly more than the judicial exception. In this case, the B.R.I. of the claims, even in view of the additional elements, encompasses a recombinant HSA protein preparation with only free thiol at Cys-34 (i.e. no oxidation), with no AGE, no carbonylation, and no homocysteinylation. In other words, the fully natural HSA protein, having none of the recited modifications, would still be a natural product, as this is a naturally occurring protein.
Further, the art cited above together with the evidence from the specification indicates that naturally occurring human protein can have varying levels of these four chemical modifications, depending on the age and health status of the individual. These chemical modifications are also naturally occurring. Therefore, regardless of the amounts of reduced Cys-34, AGE, carbonylation, and/or homocysteinylation present, the claims continue to be directed to an ineligible natural product, and not to significantly more.
None of the additional elements recited in claims 4-9 amount to significantly more than the ineligible natural product when the claim is considered as a whole. These limitations do not practically limit the claims to transformed structures, or anything other than the natural product, instead these merely recite specific elements or functional properties of the product.
Regarding claim 26, the B.R.I. of the pharmaceutical carrier encompasses solutions, i.e. water, phosphate buffers, emulsions, which are themselves natural products, and thus these cannot be considered an additional element that amounts to significantly more than the ineligible natural product. As a whole, the claimed product would not be significantly different from naturally occurring HSA found in plasma or in an aqueous buffer.
When considered individual or in combination, the claims do not amount to more than the judicial exception.
Thus, the claims do not include additional elements that are sufficient to amount to significantly more than the judicial exception (Claims 1, 4-9 and 26, Step 2B: NO).
As such, the claims do not qualify as eligible subject matter. For these reasons the claims are rejected under section 101 as being directed to non-statutory subject matter.
Response to Arguments
Applicant's arguments on pages 3-5 of the remarks filed 3/17/2026 have been fully considered but they are not persuasive.
Applicant argues that “The preparation of young and undamaged HSA exhibits at least three or all of (1) a ratio of free thiol in Cys-34 residue being greater than 50%; (2) a level of advanced glycation end-product (AGE) being lower than 60 µg/g protein; (3) a level of carbonyl lower than 1.7 nmol/mg protein; and (4) a level of homocysteinylation lower than 5 nmol/g protein. The combination of at least three of these properties makes the young and undamaged HSA of the present invention markedly different from naturally occurring HSA.”
Applicant argues that the cited references provide that the levels of the ratio of free thiol in Cys-34 residue, advanced glycation end-products, carbonylation, and homocysteinylation vary upon age and with various diseases, but do not show a naturally occurring HSA having three or more of the required limitations.
In response to Applicant’s argument that none of the referenced art demonstrates a protein preparation having all of the claimed features (i.e. regarding the allowable amounts of modifications to the HSA), it is noted that subject matter eligibility is distinct from the requirements of an invention to be novel and non-obvious (see MPEP 2106.05: "As made clear by the courts, the '"novelty' of any element or steps in a process, or even of the process itself, is of no relevance in determining whether the subject matter of a claim falls within the§ 101 categories of possibly patentable subject matter." Intellectual Ventures Iv. Symantec Corp., 838 F.3d 1307, 1315, 120 USPQ2d 1353, 1358 (Fed. Cir. 2016) (quoting Diamond v. Diehr, 450 U.S. at 188-89, 209 USPQ at 9). See also Synopsys, Inc. v. Mentor Graphics Corp., 839 F.3d 1138, 1151, 120 USPQ2d 1473, 1483 (Fed. Cir. 2016)" ). In this case, the art is provided as evidence to the natural variation in these factors, and the relevance of these factors in human physiology natural aging, and disease pathology.
The presence or lack of the assayed modifications, including each of oxidized or reduced Cys34, formation of AGEs, protein side chain carbonylation, and homocysteines attached to Cys or Lys residues, are all natural phenomenon. The claimed preparation is no different than a naturally occurring human serum albumin having no modifications. The presence or lack of any of these natural phenomenon does not result in a patent eligible composition which amounts to significantly more than a natural product. Determining how much of a natural modification is present does not amount to more than measuring a natural product.
Further, the instant specification describes how such assays for determining the level of the modifications are well-known in the art, as further evidenced by the availability of commercial kits and products to detect the modifications.
There is no change or transformation caused by the inventors to the naturally occurring subject matter. The claims encompass naturally-produced HSA isolated from plasma (see e.g. claim 9). The steps discussed by the Applicant include means for isolating the natural human protein or producing the recombinant HSA which is material the same as the endogenous protein, for all of the reasons highlighted by the authors (i.e. having favorable properties or being “undamaged”). However, the material has no markedly changed characteristics compared to the natural counterparts for all of the reasons discussed above.
Further, there is no supporting evidence on the record that any of the argued properties are significantly more than the discovery of properties of the natural product. See MPEP § 2106.04.I., “The Supreme Court’s cited rationale for considering even "just discovered" judicial exceptions as exceptions stems from the concern that "without this exception, there would be considerable danger that the grant of patents would ‘tie up’ the use of such tools and thereby ‘inhibit future innovation premised upon them.’" Myriad, 569 U.S. at 589, 106 USPQ2d at 1978-79 (quoting Mayo, 566 U.S. at 86, 101 USPQ2d at 1971). See also Myriad, 569 U.S. at 591, 106 USPQ2d at 1979 ("Groundbreaking, innovative, or even brilliant discovery does not by itself satisfy the §101 inquiry.")”.
Applicant also argues that the product can be used to provide increase longevity, enhanced skeletal function, and improved cognitive ability, however these amount only to intended uses of the product, and are benefits derived from properties of the natural product. An isolated undamaged natural HSA is indistinguishable from the claimed product and would intrinsically have all of these benefits. This is not an implementation of the claimed product in a practical application that amounts to significantly more than the ineligible natural product.
Thus, the arguments are not persuasive. The rejection is maintained, as modified above in response to the Applicant’s amendments.
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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/A.T.M./Examiner, Art Unit 1655
/ANAND U DESAI/Supervisory Patent Examiner, Art Unit 1655
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