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 .
DETAILED ACTION
Claims 1, 5-14, and 18 are pending. Claims 8-10 and 14 are withdrawn.
Response to Amendment
Applicant amended claim 1, deleted limitations S303D, S303G, S303M, S303N, S303V, and S303Y, and incorporated the limitation of now deleted claim 17. Applicant deleted claims 4 and 16-17.
The rejection of claims 1, 4-7, 11-13 and 16-18 under 35 U.S.C. 112(a) is withdrawn.
The rejection of claims 4 and 16-17 under 35 U.S.C. 112(d) is withdrawn in view of the amendment.
The rejection of claims 1, 4-7, 11-13 and 16-18 under 35 U.S.C. 102(a)(1) is withdrawn in view of the amendment.
The rejection of claims 1, 4-7, 11-13 and 16-18 under 35 U.S.C. 103 is withdrawn in view of the amendment.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.
Claims 1, 5-7, 11-13, and 18 are rejected under 35 U.S.C. 103 as being unpatentable over Carsten (WO 2006002643, published 01/2006, of record in Office Correspondence mailed on 09/24/2025) in view of Barnes (Bioinformatics for geneticists. John Wiley & Sons, 2003, of record in Office Correspondence mailed on 10/25/2024).
Regarding claims 1, 6-7, and 18, Carsten teaches a variant of an alpha-amylase with at least one substitution at position S303 (claim 1), and teaches the variant with S303Q, S303K or S303Y substitutions (claim 2, page 13 last para, page 51). Carsten teaches that the parent alpha-amylase is SP722 with SEQ ID NO: 4 (i.e., instant SEQ ID NO: 1) (claim 16). Since SEQ ID NO: 1 comprises 485 amino acids, a variant with a substitution at position S303 is 99.7% identical to SEQ ID NO: 1. Carsten teaches that the variant has an increase in specific activity (claim 19, page 48 last table, Table on page 51). Carsten teaches that substitutions along the putative substrate binding cleft, which includes S303, has shown to be beneficial for the activity of the enzyme (page 11 lines 31-32). Carsten does not teach S303C substitution.
However, Barnes teaches serine can be replaced by other polar or small amino acids, in particular threonine (T), and can also be substituted with cysteine (C) (page 307 para. 14.5.16.1 and 14.5.16.3).
It would have been prima facie obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to modify the alpha-amylase variant taught by Carsten by substituting threonine or cysteine for the serine at position 303 as suggested by Barnes. One of ordinary skill in the art would be motivated to do so in order to improve the properties of the enzyme such as stability and activity. Since Carsten teaches that glutamine (Q: polar amino acid), lysine (K: positively charged amino acid), and tyrosine (Y: hydrophobic amino acid) can be introduced at position 303 while preserving or improving the activity of the enzyme, and since Barnes teaches that threonine and/or cysteine can replace serine, there is a reasonable expectation of success to make substitutions with cysteine or tyrosine at the S303 position.
The limitation wherein said variant has increased specific activity in Model A detergent composition relative to said parent polypeptide, wherein said increased specific activity is measured as an Improvement Factor (IF) of >2.0 when compared to said parent polypeptide of SEQ ID NO: 1 having alpha-amylase activity” is a characteristic of the variant as disclosed by Applicant (page 145 Table 2 of the specification). Thus, this limitation would be found in Carsten’s variant in view of Barnes.
Regarding claim 5, Carsten teaches that the variant has a deletion at position R181+G182 and D183+G184 (SP722+R181*+G182* or SP722+D183*+G184*) (page 8 line 20).
Regarding claims 11-13, Carsten teaches the amylase is used in detergent composition which also comprises a glucoamylase, pullulanase, and other alpha-amylases (page 25 lines 5-10) and teaches that the detergent composition is formulated as a hand or machine laundry detergent composition and for hand or machine dishwashing operations (page 29 lines 28-32).
Double Patenting
The nonstatutory double patenting rejection is based on a judicially created doctrine grounded in public policy (a policy reflected in the statute) so as to prevent the unjustified or improper timewise extension of the “right to exclude” granted by a patent and to prevent possible harassment by multiple assignees. A nonstatutory double patenting rejection is appropriate where the conflicting claims are not identical, but at least one examined application claim is not patentably distinct from the reference claim(s) because the examined application claim is either anticipated by, or would have been obvious over, the reference claim(s). See, e.g., In re Berg, 140 F.3d 1428, 46 USPQ2d 1226 (Fed. Cir. 1998); In re Goodman, 11 F.3d 1046, 29 USPQ2d 2010 (Fed. Cir. 1993); In re Longi, 759 F.2d 887, 225 USPQ 645 (Fed. Cir. 1985); In re Van Ornum, 686 F.2d 937, 214 USPQ 761 (CCPA 1982); In re Vogel, 422 F.2d 438, 164 USPQ 619 (CCPA 1970); In re Thorington, 418 F.2d 528, 163 USPQ 644 (CCPA 1969).
A timely filed terminal disclaimer in compliance with 37 CFR 1.321(c) or 1.321(d) may be used to overcome an actual or provisional rejection based on nonstatutory double patenting provided the reference application or patent either is shown to be commonly owned with the examined application, or claims an invention made as a result of activities undertaken within the scope of a joint research agreement. See MPEP § 717.02 for applications subject to examination under the first inventor to file provisions of the AIA as explained in MPEP § 2159. See MPEP § 2146 et seq. for applications not subject to examination under the first inventor to file provisions of the AIA . A terminal disclaimer must be signed in compliance with 37 CFR 1.321(b).
The filing of a terminal disclaimer by itself is not a complete reply to a nonstatutory double patenting (NSDP) rejection. A complete reply requires that the terminal disclaimer be accompanied by a reply requesting reconsideration of the prior Office action. Even where the NSDP rejection is provisional the reply must be complete. See MPEP § 804, subsection I.B.1. For a reply to a non-final Office action, see 37 CFR 1.111(a). For a reply to final Office action, see 37 CFR 1.113(c). A request for reconsideration while not provided for in 37 CFR 1.113(c) may be filed after final for consideration. See MPEP §§ 706.07(e) and 714.13.
The USPTO Internet website contains terminal disclaimer forms which may be used. Please visit www.uspto.gov/patent/patents-forms. The actual filing date of the application in which the form is filed determines what form (e.g., PTO/SB/25, PTO/SB/26, PTO/AIA /25, or PTO/AIA /26) should be used. A web-based eTerminal Disclaimer may be filled out completely online using web-screens. An eTerminal Disclaimer that meets all requirements is auto-processed and approved immediately upon submission. For more information about eTerminal Disclaimers, refer to www.uspto.gov/patents/apply/applying-online/eterminal-disclaimer
Claims 1, 5-7, 11-13 and 18 remain rejected on the ground of nonstatutory double patenting as being unpatentable over claim 14 of US 9,434,932 in view of Carsten and Barnes.
Regarding instant claims 1, 5-7 and 18, patent claim 14 recites an isolated variant of a parent alpha-amylase, comprising at least two substitutions at positions corresponding to 140 and 206 of the polypeptide of SEQ ID NO: 1, wherein the variant has at least 90% sequence identity with the polypeptide of SEQ ID NO: 1, and has alpha-amylase activity, and wherein the substitution at position 206 is V206Y, which comprises alterations in the positions corresponding to D183*+G184*+W140Y +N195F+ V206Y + Y243F+E260G+S303G. Patent claim 14 does not recite S303C or S303T.
However, Carsten teaches a variant of an alpha-amylase with S303Q, S303K and S303Y substitutions, and teaches S303Q has an increase in specific activity (claims 1-2, and 19, page 48 last table, Table on page 51). Carsten teaches that the parent alpha-amylase is SEQ ID NO: 4 (i.e., instant SEQ ID NO: 1) (claim 16). Carsten teaches that substitutions along the putative substrate binding cleft, which includes S303, has shown to be beneficial for the activity of the enzyme (page 11 lines 31-32).
Furthermore, Barnes teaches serine can be replaced by other polar or small amino acids in particular threonine and can also be substituted with cysteine (page 307 para. 14.5.16.1 and 14.5.16.3).
It would have been prima facie obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to modify the recited alpha-amylase variant by substituting cysteine or threonine for Serine at position 303, as suggested by Carsten and Barnes. One of ordinary skill in the art would be motivated to do so in order to form a variant with improved stability or activity.
Regarding instant claims 11-12, Carsten teaches a composition comprising the variant and comprises additional enzymes (page 25 lines 4-10).
Regarding instant claim 13, Carsten teaches that the composition is liquid dishwashing composition (page 36 first line).
Claims 1, 5-7, 11-13 and 18 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1, 11, 13 and 17 of US 9856437 in view of Carsten and Barnes.
Regarding instant claims 1, 5-7 and 18, patent claim 1 recites an isolated variant alpha-amylase, comprising an alteration at one or more positions selected from the group consisting of: R28, R118, N174; R181, G182, W189, N195, Y298, N299, K302, S303, N306, R310, N314; R320, H324, E345, Y396, R400, W439, R444, N445, K446, Q449, R458, N471, and N484, wherein (a) the alteration(s) are independently (i) an insertion of an amino acid downstream of the amino acid which occupies the position; (ii) a deletion of the amino acid which occupies the position; or (iii) a substitution of the amino acid which occupies the position with a different amino acid; (b) the variant has alpha-amylase activity. Patent claim 11 recites wherein the parent Termamyl-like alpha-amylase has an amino acid sequence of SEQ ID NOS: 4 (i.e., instant SEQ ID NO: 1).
Patent claim 1 does not recite S303C or S303T.
However, Carsten teaches a variant of an alpha-amylase with S303Q, S303K and S303Y substitutions, and teaches S303Q has an increase in specific activity (claims 1-2, and 19, page 48 last table, Table on page 51). Carsten teaches that the parent alpha-amylase is SEQ ID NO: 4 (i.e., instant SEQ ID NO: 1) (claim 16). Carsten teaches that substitutions along the putative substrate binding cleft, which includes S303, has shown to be beneficial for the activity of the enzyme (page 11 lines 31-32).
Furthermore, Barnes teaches serine can be replaced by other polar or small amino acids in particular threonine and can also be substituted with cysteine (page 307 para. 14.5.16.1 and 14.5.16.3).
It would have been prima facie obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to modify the recited alpha-amylase variant by substituting other amino acids for Serine at position 303, as suggested by Carsten and Barnes. One of ordinary skill in the art would be motivated to do so in order to form a variant with improved stability or activity.
Regarding instant claims 11-12, patent claim 13 recites a composition comprising the isolated variant. Patent claim 17 recites a detergent composition. Carsten teaches that the composition is a detergent composition and comprises the variant and additional enzymes (i.e., additional active component) (page 25 lines 4-10).
Regarding instant claim 13, Carsten teaches that the composition is liquid dishwashing composition (page 36 first line).
Claims 1, 5-7, 11-13 and 18 remain rejected on the ground of nonstatutory double patenting as being unpatentable over claim 24 of US 10,167,458 in view of Carsten and Barnes.
Regarding instant claims 1, 5-7 and 18, patent claim 24 recites an isolated variant of a parent alpha-amylase, comprising at least two substitutions at positions corresponding to positions 206 and 476 of the polypeptide of SEQ ID NO: 1, wherein the variant has at least 90%, but less than 100% sequence identity with the polypeptide of SEQ ID NO 1 (i.e., instant SEQ ID NO: 1), and wherein the variant has alpha-amylase activity, which comprises alterations in the positions, corresponding to the positions of D183*+G184*+W140Y +N195F+ V206Y + Y243F+ E260G+S303G. Patent claim 24 does not recite S303C or S303T.
However, Carsten teaches a variant of an alpha-amylase with S303Q, S303K and S303Y substitutions, and teaches S303Q has an increase in specific activity (claims 1-2, and 19, page 48 last table, Table on page 51). Carsten teaches that the parent alpha-amylase is SEQ ID NO: 4 (i.e., instant SEQ ID NO: 1) (claim 16). Carsten teaches that substitutions along the putative substrate binding cleft, which includes S303, has shown to be beneficial for the activity of the enzyme (page 11 lines 31-32).
Furthermore, Barnes teaches serine can be replaced by other polar or small amino acids in particular threonine and can also be substituted with cysteine (page 307 para. 14.5.16.1 and 14.5.16.3).
It would have been prima facie obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to modify the recited alpha-amylase variant by substituting other amino acids for Serine at position 303, as suggested by Carsten and Barnes. One of ordinary skill in the art would be motivated to do so in order to form a variant with improved stability or activity.
Regarding instant claims 11-12, Carsten teaches a detergent composition comprising the variant and comprises additional enzymes (page 25 lines 4-10). One of ordinary skill in the art would be motivated to add the variant to a detergent composition in order to form an effective cleaning composition.
Regarding instant claim 13, Carsten teaches that the composition is liquid dishwashing composition (page 36 first line).
Claims 1, 5-7, 11-13 and 18 remain rejected on the ground of nonstatutory double patenting as being unpatentable over claim 14 of US 10,752,889 in view of Carsten and Barnes.
Regarding claims 1, 5-7 and 18, patent claim 14 recites an isolated variant of a parent alpha-amylase, comprising at least three substitutions at positions corresponding to positions 13, 206 and 260 of the polypeptide of SEQ ID NO: 1, wherein the variant has at least 90%, but less than 100% sequence identity with the polypeptide of SEQ ID NO 1 (i.e., instant SEQ ID NO:1), and wherein the variant has alpha-amylase activity, which comprises alterations in the positions, corresponding to the positions of D183*+G184*+W140Y +N195F+ V206Y + Y243F+ E260G+S303G. Patent claim 14 does not recite S303C or S303T.
However, Carsten teaches a variant of an alpha-amylase with S303Q, S303K and S303Y substitutions, and teaches S303Q has an increase in specific activity (claims 1-2, and 19, page 48 last table, Table on page 51). Carsten teaches that the parent alpha-amylase is SEQ ID NO: 4 (i.e., instant SEQ ID NO: 1) (claim 16). Carsten teaches that substitutions along the putative substrate binding cleft, which includes S303, has shown to be beneficial for the activity of the enzyme (page 11 lines 31-32).
Furthermore, Barnes teaches serine can be replaced by other polar or small amino acids in particular threonine and can also be substituted with cysteine (page 307 para. 14.5.16.1 and 14.5.16.3).
It would have been prima facie obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to modify the recited alpha-amylase variant by substituting other amino acids for Serine at position 303, as suggested by Carsten and Barnes. One of ordinary skill in the art would be motivated to do so in order to form a variant with improved stability or activity.
Regarding instant claims 11-12, Carsten teaches a detergent composition comprising the variant and comprises additional enzymes (page 25 lines 4-10). One of ordinary skill in the art would be motivated to add the variant to a detergent composition in order to form an effective cleaning composition.
Regarding instant claim 13, Carsten teaches that the composition is liquid dishwashing composition (page 36 first line).
Claims 1, 5-7, 11-13 and 18 remain rejected on the ground of nonstatutory double patenting as being unpatentable over claim 8 of US 11,091,748 in view of Carsten and Barnes.
Regarding claims 1, 5-7 and 18, patent claim 1 recites an isolated variant of a parent alpha-amylase, comprising at least two substitutions V206 and 304 of the polypeptide of SEQ ID NO: 1, wherein the variant has at least 80%, but less than 100% sequence identity with the polypeptide of SEQ ID NO 1 (i.e., instant SEQ ID NO: 1), and wherein the variant has alpha-amylase activity. Patent claim 8 recites variant further comprising one or more substitutions selected from the group consisting of Nl 95F, Y243F, G109A, G273DV, G337N, K72R, R181H, S303G and Y100I. Patent claim 15 recites the variant which consists of the following substitutions in the positions, corresponding to the positions of the polypeptide of SEQ ID NO: 1: D183*+G184*+W140Y +N195F+ V206Y + Y243F+E260G+G304R+G476K. Patent claims 1 and 8 do not recite S303C or S303T.
However, Carsten teaches a variant of an alpha-amylase with S303Q, S303K and S303Y substitutions, and teaches S303Q has an increase in specific activity (claims 1-2, and 19, page 48 last table, Table on page 51). Carsten teaches that the parent alpha-amylase is SEQ ID NO: 4 (i.e., instant SEQ ID NO: 1) (claim 16). Carsten teaches that substitutions along the putative substrate binding cleft, which includes S303, has shown to be beneficial for the activity of the enzyme (page 11 lines 31-32).
Furthermore, Barnes teaches serine can be replaced by other polar or small amino acids in particular threonine and can also be substituted with cysteine (page 307 para. 14.5.16.1 and 14.5.16.3).
It would have been prima facie obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to modify the recited alpha-amylase variant by substituting other amino acids for Serine at position 303, as suggested by Carsten and Barnes. One of ordinary skill in the art would be motivated to do so in order to form a variant with improved stability or activity.
Regarding instant claims 11-12, Carsten teaches a detergent composition comprising the variant and comprises additional enzymes (page 25 lines 4-10). One of ordinary skill in the art would be motivated to add the variant to a detergent composition in order to form an effective cleaning composition.
Regarding instant claim 13, Carsten teaches that the composition is liquid dishwashing composition (page 36 first line).
Claims 1, 5-7, 11-13 and 18 remain rejected on the ground of nonstatutory double patenting as being unpatentable over claim 14 of US 12,012,623 in view of Carsten and Barnes.
Regarding claims 1, 5-7 and 18, patent claim 14 recites an isolated variant of a parent alpha-amylase, comprising at least three substitutions at positions corresponding to positions 140 and 260 of the polypeptide of SEQ ID NO: 1, wherein the variant has at least 80%, but less than 100% sequence identity with the polypeptide of SEQ ID NO: 1 (i.e., instant SEQ ID NO: 1), and wherein the variant has alpha-amylase activity, which comprises alterations in the positions, corresponding to the positions of D183*+G184*+W140Y +N195F+ V206Y + Y243F+ E260G+S303G. Patent claim 14 does not recite S303C or S303T.
However, Carsten teaches a variant of an alpha-amylase with S303Q, S303K and S303Y substitutions, and teaches S303Q has an increase in specific activity (claims 1-2, page 48 last table, Table on page 51). Carsten teaches that the parent alpha-amylase is SEQ ID NO: 4 (i.e., instant SEQ ID NO: 1) (claim 16). Carsten teaches that substitutions along the putative substrate binding cleft, which includes S303, has shown to be beneficial for the activity of the enzyme (page 11 lines 31-32).
Furthermore, Barnes teaches serine can be replaced by other polar or small amino acids in particular threonine and can also be substituted with cysteine (page 307 para. 14.5.16.1 and 14.5.16.3).
It would have been prima facie obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to modify the recited alpha-amylase variant by substituting other amino acids for Serine at position 303, as suggested by Carsten and Barnes. One of ordinary skill in the art would be motivated to do so in order to form a variant with improved stability or activity.
Regarding instant claims 11-12, Carsten teaches a detergent composition comprising the variant and comprises additional enzymes (page 25 lines 4-10). One of ordinary skill in the art would be motivated to add the variant to a detergent composition in order to form an effective cleaning composition.
Regarding instant claim 13, Carsten teaches that the composition is liquid dishwashing composition (page 36 first line).
Claims 1, 5-7, 11-13 and 18 remain provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claim 1, 9, and 14 of copending Application No. 18/601534 in view of Carsten and Barnes.
Regarding instant claims 1, 5-7 and 18, copending claim 1 recites an isolated variant of a parent alpha-amylase, comprising an alteration at two or more (several) positions corresponding to positions G304, W140, W189, D134, E260, F262, W284, W347, W439, W469, G476, and G477 of the mature polypeptide of SEQ ID NO: 1 wherein each alteration is independently a substitution, deletion or insertion, and wherein the variant has at least 80%, or at least 87%, but less than 100% sequence identity with the mature polypeptide of any of SEQ ID NOs 1,2,3,4,5, 6, 7, 8, 9, 10, 11 or 12, and wherein the variant has alpha-amylase activity. Copending claim 9 recites the variant of claim 1, further comprising one or more substitutions selected from the group consisting of N195F, V206Y, Y243F, G109A, G273DV, G337N, K72R, R181H, S303G and Y1001. Copending claim 9 does not recite the substitution S303C or S303T.
However, Carsten teaches a variant of an alpha-amylase with S303Q, S303K and S303Y substitutions, and teaches S303Q has an increase in specific activity (claims 1-2, page 48 last table, Table on page 51). Carsten teaches that the parent alpha-amylase is SEQ ID NO: 4 (i.e., instant SEQ ID NO: 1) (claim 16). Carsten teaches that substitutions along the putative substrate binding cleft, which includes S303, has shown to be beneficial for the activity of the enzyme (page 11 lines 31-32).
Furthermore, Barnes teaches serine can be replaced by other polar or small amino acids in particular threonine and can also be substituted with cysteine (page 307 para. 14.5.16.1 and 14.5.16.3).
Regarding instant claim 5, copending claim 14 recites the variant of claim 1, which further comprises deletions at positions corresponding to positions G182*+D183* or D183*+G184* of SEQ ID NO:1
Regarding instant claims 11-13, copending claim 1 does not recite a composition comprising the variant and at least one additional active component, wherein the composition is a detergent composition, where in the composition is a liquid laundry. However, Carsten teaches a detergent composition comprising the variant and comprises additional enzymes (page 25 lines 4-10). Carsten teaches that the composition is liquid dishwashing composition (page 36 first line). One of ordinary skill in the art would be motivated to add the variant to a detergent composition in order to form an effective cleaning composition.
This is a provisional nonstatutory double patenting rejection.
Response to Arguments
Applicant's arguments filed 01/19/2026 have been fully considered but they are not persuasive.
Applicant argues a variant comprising S303C or S303T is not taught nor suggested by Carsten and/or Barnes, and argues a person of skill in the art would not be motivated to mutate S303 to S303C or S303T, as these are conservative substitutions and therefore not expected to greatly change the function or stability of the amylase. Applicant argues the variants had an unexpected improvement factor greater than 2 and the other substitutions did not perform as well.
In response to the argument, Carsten teaches alpha-amylase variant SEQ ID NO: 1 with S303Q, S303K and S303Y substitutions, and teaches the variant has an alteration in the specific activity relative to the parent alpha-amylase (claim 19). Carsten teaches S303Q has an increase in specific activity (page 48 last table, Table on page 51). Carsten teaches that substitutions along the putative substrate binding cleft, which includes S303, has shown to be beneficial for the activity of the enzyme (page 11 lines 31-32). This is also shown in Applicant’s disclosure in Table 2 where substitutions of Ser at position 303 increases the specific activity of the amylase. Carsten teaches that the S303 residue of SEQ ID NO: 1 can be substituted with different amino acids: polar (Q), positively charged (K), and hydrophobic (Y) amino acids. Barnes teaches serine can be replaced by other polar or small amino acids, in particular threonine (T), and can also be substituted with cysteine (C). Since the prior art teaches several substitutions at S303 position do not abolish the enzyme’s activity and teaches an important role of the region comprising S303 on the activity of the enzyme, one of ordinary skill in the art would be motivated to mutate this residue to other amino acids and test their effect on the enzyme’s function and/or structure. In response to applicant's argument that the variants had an unexpected improvement factor greater than 2, the fact that the inventor has recognized another advantage which would flow naturally from following the suggestion of the prior art cannot be the basis for patentability when the differences would otherwise be obvious. See Ex parte Obiaya, 227 USPQ 58, 60 (Bd. Pat. App. & Inter. 1985).
Conclusion
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.
Any inquiry concerning this communication or earlier communications from the examiner should be directed to MARY A CRUM whose telephone number is (571)272-1661. The examiner can normally be reached M-F 8:00-5:00 CT with alternate Fridays off.
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/MARY A CRUM/Examiner, Art Unit 1657
/THANE UNDERDAHL/Primary Examiner, Art Unit 1699