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
The amendment to the claims filed after non-final office action on July 31, 2025 is acknowledged. Claims 1-9, 16, 20 were amended, claims 10-15, 17-19 were canceled, claim 21 was newly added and claims 1-9, 16, 20-21 are pending in the instant application.
The restriction requirement was deemed proper and made FINAL previously. Due to amendment of the claims, the elected species is free of the art and claims 5-8 are hereby rejoined and examined. Claims 1-9, 16 and 20-21 are examined on the merits in this office action.
Withdrawn Rejections/Objections
The objections to claims 2, 12, 20 are withdrawn in view of amendment of the claims filed July 31, 2025.
The rejections of claims 10-11 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or a joint inventor (or for applications subject to pre-AIA 35 U.S.C. 112, the applicant), regards as the invention, is withdrawn in view of amendment of the claims filed July 31, 2025.
The rejection of claim(s) 1-4, 9-12 and 14-20 under 35 U.S.C. 102(a)(1) as being anticipated by Wu (US8293710) is withdrawn in view of amendment of the claims filed July 31, 2025.
The rejection of claims 1-4, 10-12 and 14-20 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-20 of U.S. Patent No. 9156904 B2 is withdrawn in view of amendment of the claims filed July 31, 2025. In particular, the claims now require the patient have a bone defect and bone loss due to amendment of claims 1-2.
The rejection of claims 1-4, 9-12 and 14-15, 17-19 on the ground of nonstatutory double patenting as being unpatentable over claims 1-16 of U.S. Patent No. 9730983 B2 is withdrawn in view of amendment of the claims filed July 31, 2025. In particular, the claims now require the patient have a bone defect and bone loss due to amendment of claims 1-2.
The rejection of claims 1-4, 9-12 and 14-20 on the ground of nonstatutory double patenting as being unpatentable over claims 1-17 of U.S. Patent No.8293710 B2 is withdrawn in view of amendment of the claims filed July 31, 2025. In particular, the claims now require the patient have a bone defect and bone loss due to amendment of claims 1-2.
Maintained/Revised Rejections
Claim Rejections - 35 USC § 112, first paragraph
The following is a quotation of the first paragraph of 35 U.S.C. 112(a):
(a) IN GENERAL.—The specification shall contain a written description of the invention, and of the manner and process of making and using it, in such full, clear, concise, and exact terms as to enable any person skilled in the art to which it pertains, or with which it is most nearly connected, to make and use the same, and shall set forth the best mode contemplated by the inventor or joint inventor of carrying out the invention.
The following is a quotation of the first paragraph of pre-AIA 35 U.S.C. 112:
The specification shall contain a written description of the invention, and of the manner and process of making and using it, in such full, clear, concise, and exact terms as to enable any person skilled in the art to which it pertains, or with which it is most nearly connected, to make and use the same, and shall set forth the best mode contemplated by the inventor of carrying out his invention.
Claims 1-7, 9, 16, 20-21 are/remain rejected under 35 U.S.C. 112(a) or 35 U.S.C. 112 (pre-AIA ), first paragraph, as failing to comply with the written description requirement. The claim(s) contains subject matter which was not described in the specification in such a way as to reasonably convey to one skilled in the relevant art that the inventor or a joint inventor, or for pre-AIA the inventor(s), at the time the application was filed, had possession of the claimed invention.
MPEP § 2163 states that the written description requirement for a claimed genus may be satisfied through sufficient description of a representative number of species by actual reduction to practice, or by disclosure of relevant, identifying characteristics, i.e., structure or other physical and/or chemical properties, by functional characteristics coupled with a known or disclosed correlation between function and structure, or by a combination of such identifying characteristics, sufficient to show the applicant was in possession of the claimed genus.
Scope of the claims
The claims are drawn to “A method for stimulating bone regeneration, bone augmentation, enhancing bone defect healing, and alleviating a bone loss comprising: administering to a subject in need thereof a therapeutically effective amount of a biologically active recombinant polypeptide comprising domains 2 and 3 of human thrombomodulin (TMD23), wherein the recombinant polypeptide is free of or lacking amino acid residues from domains 4 and 5 of the human thrombomodulin and has biological activity of promoting osteoblast proliferation and migration, enhancing osteoblast mineralization, bone regeneration and/or and osteoblast function” (claim 1). Claim 2 claims “A method for stimulating bone regeneration, bone augmentation, treating bone defect healing, and alleviating a bone loss comprising: administering to a subject in need thereof a therapeutically effective amount of an isolated polypeptide comprising recombinant domains 2 and 3 of human thrombomodulin (rTMD23) or a biologically active recombinant variant thereof, wherein the biologically active recombinant variant thereof comprises two mutations N364A andN391A, at asparagine 364 and asparagine 391 replaced by alanine in the domain 2 of the human thrombomodulin, and further wherein the isolated polypeptide or the recombinant variant thereof is free of or lacking amino acid residues from domains 4 and 5 of the human thrombomodulin and has biological activity of promoting osteoblast proliferation and migration, enhancing osteoblast mineralization, bone regeneration and/or osteoblast function” (claim 2).
The negative limitation (bolded above) sets a clear structural boundary: the claimed polypeptide must lack all or part of domains 4 and 5 (amino acids to full sequence domain), which are c-terminal to domains 2 and 3 and typically begin around residue 498 in human (e.g. SEQ ID NO:1). Domain 4 is amino acids 492-521 of SEQ ID NO:1 and domain 5 is 522-557 of SEQ ID NO:1. In total, this is 492-557 (66 mer sequence) of which any amino acids can be missing/lacking (one to all of them). Furthermore, claim 7 recites “further comprises amino acid residues of domain 1..”. Similarly to above, Applicants do not provide guidance or description regarding what amino acids of domain 1 would be required to retain the same desired functional property or can be included without negatively impacting the desired function.
Therefore, to meet the written description requirement of 35 U.S.C. § 112, first paragraph, the specification must disclose a representative number of species that meet both the structural and functional limitations of the genus or the specification and/or the prior art must identify the structural elements that correlate to the claimed function in a manner that demonstrates to one of ordinary skill in the art that Applicant was in possession of the claimed genus at the time the application was filed. In the instant case, the specification must establish which of the thrombomodulin peptides encompassed by the claims that satisfy the structural limitations of the claim are also stimulate bone regeneration, bone augmentation, enhancing bone defect healing and alleviating bone loss.
Actual Reduction to Practice
MPEP § 2163 states that the written description requirement for a claimed genus may be satisfied through sufficient description of a representative number of species by actual reduction to practice. A “representative number of species” means that the species which are adequately described are representative of the entire genus. Thus, when there is substantial variation within the genus, one must describe a sufficient variety of species to reflect the variation within the genus. Applicants utilize rTMD23 (domains 2-3 of TM) and rTMD123 (domains 1-3 of TM) for treating bone defects in a diabetic model (see paragraph 0087). Applicant’s conclude “In conclusion, thrombomodulin domain 23-containing proteins, including TMD23, TMD123, and bioactive variants thereof, can inhibit osteoclastogenesis and promote osteoblastogenesis” (see paragraph 0092). rTMD23NA (a variant of rTMD23 with N364A and N391A) were reduced to practice. The figures show that these recombinant polypeptides promote osteoblast proliferation, enhance mineralization, inhibit RANKL-induced osteoclast formation and accelerate bone healing in mouse calvarial defect models. However, no construct including domains 4 and/or 5 (or amino acid portions thereof) are tested, described or directly contrasted against rTMD23 or rTMD12 constructs. There is no statement with regards to what amino acids of domains 4/5 could be included or excluded and still have the desired function. Applicants have support for lacking the full domains 4 and 5 however, the claim also includes lacking only amino acids from those domains without any guidance as to which amino acids could be included and till preserve the function.
Therefore, the instant specification has failed to meet the written description requirement by actual reduction to practice of a representative number of species alone.
Sufficient relevant identifying characteristic
MPEP § 2163 states that the written description requirement for a claimed genus may be satisfied through sufficient description of a representative number of species by actual reduction to practice, or by disclosure of relevant, identifying characteristics, i.e., structure or other physical and/or chemical properties, by functional characteristics coupled with a known or disclosed correlation between function and structure, or by a combination thereof.
The specification does not define: the amino acid boundaries or structural features of domains 4 and 5, which residues within those domains, if any, could be tolerated or retained, or how partial inclusion would affect protein folding, stability and activity desired. There is no discussion regarding permissible truncations with regards to domains 4-5. Without structural or functional benchmarks, one of ordinary skill in the art would not understand what variants fall within the claimed genus or which would exhibit the desired biological effects.
Physical and/or chemical properties:
The specification fails to disclose any physical or chemical properties of the claimed genus that would allow one to identify or distinguish operative embodiments from non-operative ones. In particular, there is no description of truncated constructs with regards to domains 4/5 or how retaining portions of domains 4-5 affects proteins structure and function. The specification contains no predictive correlation between these physical or chemical parameters and biological activity (osteoblast stimulation, osteoclast inhibition). Without disclosure of such properties, a skilled artisan lacks sufficient information to recognize which partially truncated variants might possess comparable structural integrity or functional effects to the exemplified rTMD23 and rTMD123 constructs.
Functional characteristics when coupled with a known or disclosed correlation between function and structure:
Although rTMD23 and related constructs are show to enhance osteoblast activity and bone defect healing, there is no functional correlation presented for any constructs containing residues from domains 4 or 5. The disclosure does not identify which specific structural features are necessary or sufficient of for the observed biological effects. Consequently, applicants have not provided a basis for concluding that peptides retaining any portion of domains 4 or 5 would continue to exhibit the desired therapeutic activity.
Method of Making
The specification lacks adequate disclosure of methods by which a skilled artisan could make the full scope of recombinant thrombomodulin derived polypeptides encompassed by the claims, particularly those that are free of or lacking amino acid residues from domains 4 and 5, including variants with partial exclusion.
Conclusion
In conclusion, only specific TMD variants reduced to practice, satisfies the written description requirements of 35 U.S.C. 112, first paragraph.
Response to Applicant’s Arguments
Applicants argue “As amended, the scope of the claimed invention does not encompass a genus of “a polypeptide comprising an amino acid sequence that that is at least 80% identical to TMD23”.
(ii) The specification discloses recombinant polypeptides rTMD23, rTMD123, and variants thereof, rTMD23NA and rTMD123NA. The variant was reduced to practice. The data on osteoblast show that rTMD23 and rTMD123 promote migration of MG63 osteoblast-like cells (FIGs.1A-B), rTMD23 enhanced MG-63 cell mineralization (FIG. 3), and that the variant rTMD23NA enhanced MC3T3-E1 osteoblast-like cell proliferation (FIG. 2B; p.12, lines 3-11). MG-63 is a type of osteoblast cell line. MC3T3-E1 cells are osteoblast-like, exhibiting characteristics of osteoblasts, including mineralization and collagen production, and used for studying bone formation. The data on osteoclast show that rTMD123, rTMD23, and the variant rTMD23NAinhibit RANKL-induced osteoclast formation from RAW264.7 cells (FIGs. 4A-B, FIGs. 5A-D; p.12, lines 17-24), and that rTMD123 inhibits bone resorption activity of osteoclasts, leading to decreased resorption area (FIGs. 6A-B; p.12, lines 25-32). RAW264.7 cells can differentiate into osteoclast-like cells upon RANKL/MCSF stimulation and are used for osteoclastogenesis studies.
The data on bone defect healing/bone regeneration show that rTMD23 enhances calvarial bone defect healing (bone regeneration) in streptozotocin-induced diabetic models (FIGs. 7A-B; p.12, line 33 to p.13, line 6), and rTMD1 did not promote MG63 osteoblast-like cell migration (FIG. 8A), or proliferation (FIG. 8B), or mineralization (FIG. 8C), and that no significant difference in calvarial bone healing was found between TM wild-type TMwt/wt and TMD1-deleted TMLeD/LeD mice (FIG. 8D), and that DCI reduced bone regeneration of calvarial bone defect, which could be rescued by rTMD23 but not by rTMD1 (FIGs. 8E-F), indicating that rTMD23 but not rTMD1 has the capacity to promote osteoblastic functions and bone healing (p.13, lines 8-20). DCI (3,4-Dichloroisocoumarin), a rhomboid intramembrane serine protease inhibitor, was used to inhibit Rhomboid-like-2 (RHBDL2) and TM ectodomain shedding. RHBDL2 is an intramembrane serine protease, specifically cleaves TM at the transmembrane domain and causes the release of soluble TM. Accordingly, claims 1-9, 16, 20-21 satisfies the written description requirements of 35 U.S.C. 112, first paragraph.
Applicant’s arguments have been fully considered but not found persuasive. While Applicants have provided experimental data supporting specific constructs (rTMD23, rTMD123 and rTMD23NA), the written description requirement under 35 U.S.C 112(a) is not satisfied for the full structural scope of the claims. Specifically, the limitation “free of or lacking amino acid residues from domains 4 and 5” is drafted broadly and encompasses not only polypeptides that completely exclude domains 4 and 5, but also constructs that include portions of those domains. However, the specification provides no description of the amino acid boundaries or sequence characteristics of domains 4 or 5, whether partial inclusion (e.g. a few terminal residues beyond residue 497) would maintain or alter biological activity, and what structure-function relationships apply to the c-terminal region of thrombomodulin beyond domain 3. The working examples all terminate at residue 497 and no constructs extending into domain 4 were disclosed, tested, or structurally analyzed. The claims, by contrast, cover a genus of recombinant polypeptides with undefined structural boundaries, and the specification lacks sufficient identifying characteristics, structural variability, or physical/chemical property descriptions to show possession of the broader genus. While Applicants distinguish their claims from a broad sequence identity genus, this distinction does not resolve the structural written description issue for the negative limitation as claimed. The claim language is not restricted to rTMD23 or its variants, but rather encompasses a wide array of potentially functional constructs that the inventors did not show they had in their possession at the time of filing. Accordingly, although rTMD23 and rTMD123 were reduced to practice and show to possess osteogenic activity, the specification does not demonstrate possession of the broader genus of polypeptides lacking or partially lacking domains 4 and 5, as currently claimed.
Claims 1-9, 16, 20-21 are/remain rejected under 35 U.S.C. 112(a) or 35 U.S.C. 112 (pre-AIA ), first paragraph, because the specification, while being enabling for treating patients with specific bone defects (i.e. diabetic mice with local bone defects) does not reasonably provide enablement for treating bone loss in any patient population encompassed by the claims. The specification does not enable any person skilled in the art to which it pertains, or with which it is most nearly connected, to use the invention commensurate in scope with these claims.
To comply with the enablement requirements of 35 U.S.C. §112, first paragraph, a specification must adequately teach how to make and how to use a claimed invention throughout its scope, without undue experimentation. Plant Genetic Systems N.V. v. DeKalb Genetics Corp., 315 F.3d 1335, 1339, 65 USPQ2d 1452, 1455 (Fed. Cir. 2003). There are a variety of factors which may be considered in determining whether a disclosure would require undue experimentation. These factors include: (1) the quantity of experimentation necessary, (2) the amount of direction or guidance presented, (3) the presence or absence of working examples, (4) the nature of the invention, (5) the state of the prior art, (6) the relative skill of those in the art, (7) the predictability or unpredictability of the art, and (8) the breadth of the claims. In re Wands, 858 F.2d 731, 737, 8 USPQ2d 1400, 1404 (Fed. Cir. 1988).
The Nature of the Invention/ The breadth of the claims
The claims are drawn to “A method for stimulating bone regeneration, bone augmentation, enhancing bone defect healing, and alleviating a bone loss, comprising: administering to a subject in need thereof a therapeutically effective amount of a biologically active recombinant polypeptide comprising domains 2 and 3 of human thrombomodulin (TMD23), wherein the recombinant polypeptide is free of or lacking amino acid residues from domains 4 and 5 of the human thrombomodulin and has biological activity of promoting osteoblast proliferation and migration, enhancing osteoblast mineralization, bone regeneration and osteoblast function.”
The claims are broad with regards to the patient population. The claim covers any cause of bone loss or healing impairment, in any subject using any polypeptide lacking or free of amino acid residues from domains 4 and 5 of human thrombomodulin. The invention relates to protein based modulation of bone remodeling and process that is dependent on local and systemic signaling and involves both osteoblast and osteoclast dynamics which vary by disease state. Different causes of bone loss require different therapeutic mechanisms. For example, estrogen loss involves upregulation of osteoclastogenesis via RANKL, inflammation activates NF-kB and TNF-a pathways, disuse induced bone loss suppresses Wnt/B-catenin signaling. A single human thrombomodulin effective in diabetic mice cannot be presumed effective in all contexts.
The State of the Prior Art
There is no established precedent in the prior art for using thrombomodulin derived peptides to treat bone conditions. Thrombomodulin is known for anticoagulant and endothelial protective properties and there is no known role for skeletal signaling or mineral metabolism.
Cheng (Scientific Reports volume 6, Article number: 28340 (2016), cited in Applicant’s IDS), teaches that “the inhibiting effects of recombinant TM lectin-like domain (rTMD1) on bone resorption in vitro and bone loss in both the ovariectomized model and collagen antibody-induced arthritis model has been detected. These findings suggested that the myeloid TM lectin-like domain may inhibit osteoclastogenesis by reducing HMGB1 signaling and rTMD1 may hold therapeutic potential for inflammatory bone loss” (see abstract).
Kuo (Cardiovascular Research (2015) 105, 107–117) teaches rTMD23 induced angiogenesis via FGFR1, a process that is independent of the APC pathway (see abstract). Thus, the art teaches domain 1 of TMD has anti-bone loss activity and domains 2-3 have angiogenic activity. However, there is nothing in the art that discloses variants of TMD (other than domain 1) and mutations of TMD domains and how they affect bone. Thus, there is unpredictability with regards to TMD peptide variants and treating bone defects and bone loss. Without any prior functional link, a skilled artisan would not expect broad osteogenic or anti-resorptive activity across diverse disease states.
The Predictability or Unpredictability of the Art/ The Relative Skill of Those in the Art
While a skilled researcher in bone biology may be able to evaluate polypeptides in various models, the art is not routine or predictive without guidance. Testing each cause of bone loss would be required and constructing/validating would take substantial testing
It is not the skill of those in the art to treat bone defects/bone loss across any population (independent of cause) with a TMD peptide. Bone remodeling is regulated by complex, multi-organ signaling and polypeptide success depends on many different factors. One cannot assume the peptide will have the same efficacy across different conditions causing bone loss/defects.
Amount of Guidance/ The Presence or Absence of Working Examples
Applicant’s reduce to practice the following: Applicants utilize rTMD23 (domains 2-3 of TM) and rTMD123 (domains 1-3 of TM) for treating bone defects in a diabetic model (see paragraph 0087). Applicant’s conclude “In conclusion, thrombomodulin domain 23-containing proteins, including TMD23, TMD123, and bioactive variants thereof, can inhibit osteoclastogenesis and promote osteoblastogenesis” (see paragraph 0092). One a single animal modes is disclosed: STZ diabetic mouse calvarial defect, representing impaired local healing in severe hyperglycemic conditions. There are no examples for systemic bone preservation, hormonal or age related bone loss, bone augmentation procedures or bone regeneration in other models.
One of ordinary skill in the art would not consider the examples provided in the instant specification to be representative of the full scope of the claimed genus.
The Quantity of Experimentation Necessary
To practice the claimed method for all causes of bone loss or healing defects, a skilled artisan would need to identify effective doses, delivery routes, and treatment durations for each disease model and evaluate function under different inflammatory, hormonal and mechanical microenvironments. Considering the factors above, the skilled artisan would be burdened with undue experimentation in determining if one of the claimed peptides would be effective at treating or preventing bone or bone related disorders. The experimentation required represents years of inventive effort. When the above factors are weighed, it is the examiner's position that one skilled in the art could not practice the invention without undue experimentation.
Therefore, in view of the Wands factors, the claims appear to require undue experimentation to use the full scope of the claimed invention.
Response to Applicant’s Arguments
Applicants argue As amended, claims 1-9, 16, 20-21 recite “a method for stimulating bone regeneration, bone augmentation, enhancing bone defect healing, and alleviating a bone loss”.
Therefore, the scope of the claimed invention does not encompass “treating and/or preventing any bone defect or bone related disorder”, nor encompass “a polypeptide comprising an amino acid sequence that that is at least 80% identical to TMD23”, as the Examiner has alleged.
(ii) The specification disclosure enables making and using recombinant polypeptides rTMD23, rTMD123, and variants thereof, rTMD23NA and rTMD123NA. The variant was reduced to practice.
The experiments on osteoblast cells, osteoclast cells, and on bone defect healing/bone regeneration were fully disclosed. The data on osteoblast show that rTMD23, rTMD123, and variant rTMD23NA has biological activity of promoting osteoblast proliferation and migration, enhancing osteoblast mineralization, bone regeneration and osteoblast function. The data on osteoclast show rTMD23, rTMD123 and the variant rTMD23NA inhibit osteoclast, and rTMD123 inhibits bone resorption activity of osteoclasts.
The data on bone defect healing/bone regeneration show that rTMD23 but not rTMD1 has the capacity to promote osteoblastic functions and bone healing. Accordingly, as amended, claims 1-9, 16, 20-21 satisfies the enabling requirements of 35 U.S.C. 112(a), first paragraph.
Applicant’s arguments have been fully considered but not found persuasive. The Examiner acknowledges that “treating a disorder” and “80 % identity” have been removed from the claims. However, the question is whether the specification enables the claimed method for the full scope of stimulating bone regeneration, bone augmentation, enhancing bone defect healing and alleviating bone loos in any subject in need thereof regardless of etiology. Applicants disclose a single in vivo model (STZ diabetic calvarial defect) and an in vitro osteoblast/osteoclast assays. However, the claims cover treating bone loss and bone healing from any cause, in any patient population and across multiple distinct outcomes (regeneration, augmentation etc…). There is no data to support activity in postmenopausal osteoporosis, inflammatory erosion/resorption or glucocorticoid induced loss. There are no examples of scaffolds, implants or procedures for bone augmentation. There is no indication of systemic effects or preservation of bone in metabolically neutral models (non pathogenic), Applicants argue that the polypeptides are generally osteogenic and anti-resorptive but provide no mechanism of action, targeting or signaling and do not explain how efficacy in a diabetic model predicts broader utility, especially in different pathological settings/conditions.
Taken together, the cited data do not support the breadth of the claim and no nexus or mechanistic rationale is provided that would allow a skilled artisan to apply the method across all embodiments without undue experimentation. Accordingly, the rejection is maintained.
New Objections
Claim 1 is objected to for the following informality: the limitation of “wherein the recombinant polypeptide” should be replaced with -wherein the biologically active recombinant polypeptide- to be consistent throughout the claim.
Claim 3 is objected to for the following informality: the limitation “domains 2 comprises an amino acid sequence from …” in line 1 should be -domain[[s]] 2 comprises the amino acid sequence-.
Furthermore, the “an” in line 2 following “the domain 3 comprises” should be replace with -the-.
Claim 4 is objected to for the following informality: the limitation of “wherein the recombinant polypeptide” should be replaced with -wherein the biologically active recombinant polypeptide-. Furthermore, the limitation of “an amino acid” should be replaced with -the amino acid sequence-.
Claims 5-6 and 8 are objected to for the following informality: the limitation of “the recombinant variant” should be replaced with - the biologically active recombinant variant-.
Claim 7 is objected to for the following informality: the limitation of “wherein the recombinant polypeptide” should be replaced with -wherein the biologically active recombinant polypeptide-.
Claim 9 is objected to for the following informality: the limitation of “and the recombinant variant” should be replaced with -and the biologically active recombinant variant-.
Claim 16 is objected to for the following informality: the limitation of “wherein the recombinant polypeptide” should be replaced with -wherein the biologically active recombinant polypeptide-.
Claim 21 is objected to for the following informality: the limitation of “wherein the recombinant variant” should be replaced with -wherein the biologically active recombinant variant-.
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.
Any inquiry concerning this communication or earlier communications from the examiner should be directed to ERINNE R DABKOWSKI whose telephone number is (571)272-1829. The examiner can normally be reached Monday-Friday 7:30-5:30 Est.
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If attempts to reach the examiner by telephone are unsuccessful, the examiner’s supervisor, Lianko Garyu can be reached at 571-270-7367. The fax phone number for the organization where this application or proceeding is assigned is 571-273-8300.
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/ERINNE R DABKOWSKI/Examiner, Art Unit 1654
/JULIE HA/Primary Examiner, Art Unit 1654
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