DETAILED ACTION
Objections and rejections stated in prior Office Actions are withdrawn unless restated below.
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 .
Specification
The disclosure is objected to because it contains an embedded hyperlink and/or other form of browser-executable code. Applicant is required to delete the embedded hyperlink and/or other form of browser-executable code; references to websites should be limited to the top-level domain name without any prefix such as http:// or other browser-executable code. See MPEP § 608.01. At least para. [0048] has an embedded hyperlink; the specification should be reviewed to remove any embedded hyperlinks that may be present.
Claim Interpretation
A special definition for “droplet” is provided in para. [0019] of the specification. The definition for a droplet liquid-liquid separated phase is consistent with the use of droplet in the art, for example as discussed in Shiraki et al. (Effect of additives on liquid droplets and aggregates of proteins, Biophysical Rev. 12, 2020, 587-92).
In claim 6, the active step of “producing a droplet comprising a step of assembling a protein” is interpreted as requiring bringing a protein that is not in phase-separated form into a droplet phase-separated form (i.e. assembling).
Regarding recitation of “thioredoxin-like domain,” the is a well-known term in the art and is not considered to be indefinite. See Galligan et al. (The human protein disulfide isomerase gene family, Human Genomics 6, 2012, 6). Amendment to “thioredoxin” would not be correct since such domains are not thioredoxin.
Claim Rejections - 35 USC § 112
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 and 3-9 (all pending claims) are 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 applications subject to pre-AIA 35 U.S.C. 112, the inventor(s), at the time the application was filed, had possession of the claimed invention.
The purpose of the written description requirement is to ensure that the inventor had possession, at the time the invention was made, of the specific subject matter claimed. For a broad generic claim, the specification must provide adequate written description to identify the genus of the claim.
“A written description of an invention involving a chemical genus, like a description of a chemical species, 'requires a precise definition, such as by structure, formula, [or] chemical name,' of the claimed subject matter sufficient to distinguish it from other materials." Fiers, 984 F.2d at 1171, 25 USPQ2d 1601; In re Smythe, 480 F.2d 1376, 1383, 178 USPQ 279, 284985 (CCPA 1973) (“In other cases, particularly but not necessarily, chemical cases, where there is unpredictability in performance of certain species or subcombinations other than those specifically enumerated, one skilled in the art may be found not to have been placed in possession of a genus.”). Regents of the University of California v. Eli Lilly & Co., 119, F.3d 1559, 1568, 43 USPQ2d 1398, 1405 (Fed. Cir. 1997).
MPEP § 2163 further states that if a biomolecule is described only by a functional characteristic, without any disclosed correlation between function and structure of the biomolecule, it is "not sufficient characteristic for written description purposes, even when accompanied by a method of obtaining the claimed biomolecule.”
“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 . . ., reduction to drawings . . ., 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.” MPEP 2163(II)(3)(a).
Furthermore, 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. The disclosure of only one species encompassed within a genus adequately describes a claim directed to that genus only if the disclosure ‘indicates that the patentee has invented species sufficient to constitute the gen[us].’ See Enzo Biochem, 323 F.3d at 966, 63 USPQ2d at 1615; Noelle v. Lederman, 355 F.3d 1343, 1350, 69 USPQ2d 1508, 1514 (Fed. Cir. 2004) (Fed. Cir. 2004) (‘[A] patentee of a biotechnological invention cannot necessarily claim a genus after only describing a limited number of species because there may be unpredictability in the results obtained from species other than those specifically enumerated.’). ‘A patentee will not be deemed to have invented species sufficient to constitute the genus by virtue of having disclosed a single species when … the evidence indicates ordinary artisans could not predict the operability in the invention of any species other than the one disclosed.’ In re Curtis, 354 F.3d 1347, 1358, 69 USPQ2d 1274, 1282 (Fed. Cir. 2004).” MPEP 2163(II)(3)(a).
The claims recite a genus of any “artificial protein” containing at least one thioredoxin-like domain and calcium-binding region or a PDI family protein (artificial or not) containing a PDI formed into a droplet as defined in para. [0019] of the specification. Such droplet formation is a physical phase separation property of the protein and not a function of innate enzymatic ability. While claim 1 and claim 6 allow for the presence of other proteins and/or substances within the droplet, the claims are understood to be specifically addressed to a genus of proteins containing a thioredoxin-like domain and calcium-binding region with no other required proteins present.
“As it has not been known heretofore that a protein having chaperone and enzyme functions forms a droplet by itself, an object of the present invention is to develop a technology for preparing such droplet .” Specification, para. [0004]. As such, the specification is understood as describing that ability of proteins containing thioredoxin-like domains to form droplets is not known in the art generally. The specification contains one example of a protein containing a thioredoxin-like domain (and a calcium-binding region) forming a droplet being “P5 protein” that can “reversibly assemble [into droplets] in a calcium-dependent manner.” Specification, para. [0043]. As such, the specification discloses one working embodiment of a protein capable of forming a droplet with a required presence of calcium and by extension having a calcium-binding region.
PDI family proteins are structurally diverse. As reviewed by Galligan et al. (The human protein disulfide isomerase gene family, Human Genomics 6, 2012, 6): The PDI gene family currently comprises 21 genes, varying in size, expression, localization, and enzymatic function. Although it is implied that all members of the PDI family possess the ability to rearrange disulfide bonds, only a subset is considered orthologous and able to carry out these reactions, with the other members being paralogous and linked to the family through evolution, not function. While these proteins may be functionally different, the unifying feature of all PDI family members is the presence of a TRX-like domain. These may be present as either a catalytically active a or a’ domain (the presence of a CXXC motif ) or a catalytically inactive b or b’ domain.
Table 1 of Galligan indicates that protein P5 is also known in the art as PDIA6. Figure 1 of Galligan shows a cartoon representation of various PDI family proteins wherein only a few have “green represents the Asp/Glu rich Ca2+-binding domain,” wherein PDIA6 has such a Ca2+-binding domain.
“The disclosure of only one species encompassed within a genus adequately describes a claim directed to that genus only if the disclosure ‘indicates that the patentee has invented species sufficient to constitute the gen[us].” “A patentee will not be deemed to have invented species sufficient to constitute the genus by virtue of having disclosed a single species when … the evidence indicates ordinary artisans could not predict the operability in the invention of any species other than the one disclosed.”
As set forth above, the specification presents only a single example of a thioredoxin-like domain protein with ability to form a droplet being P5/PDIA6 and more specifically no examples of an artificial protein are described. The specification describes that calcium is required for droplet formation such that a calcium binding domain is required for droplet formation. Regardless, the specification provides for no discuss or description of the minimum structural elements required for a protein with a thioredoxin-like domain to form droplets, since no modifications to protein P5 or any other protein are discussed that would reveal this information.
From the disclosure of the specification, it is not possible for an ordinarily skilled artisan to predict the operability of any protein having one or two thioredoxin-like domains (joined by a linker as recited in claim 3) and with or without a calcium binding domain. That is, a description that P5 is able to form droplets in the presence of calcium ion provides for no description to allow for the prediction of other proteins that may share structural elements, but are otherwise significantly different in structure as encompassed by the claims, to form droplets (or even dimers) with or without the presence of calcium.
While not prior art, Lee et al. (Ca2+-driven PDIA6 phase separation to ensure proinsulin quality control, bioRxiv, 2024, doi.org/10.1101/2024.07.30.605722) and Okamura et al. (Structure 29, 2021, 1357) (see IDS, NPL CI) evidences that at the time of filing an ordinarily skilled artisan would not be able to predict proteins other than P5/PDIA6 (with thioredoxin-like domains) to form droplets. Lee, abstract, discusses: “Here, we show that Ca2+ triggers the phase separation of PDIA6 into liquid-like condensates. In contrast to the condensation mechanism observed for proteins containing low-complexity domains, our results indicate that transient but specific electrostatic interactions occur between the first and the third folded thioredoxin-like domains of PDIA6.” The described liquid-like condensates are understood to be droplets as recited in the claims. “To determine whether PDI family members can self-assemble in a Ca2+-driven process, we measured their diameters under increasing Ca2+ concentrations by dynamic light scattering (DLS) (Fig. 1a). Although almost no changes were detectable in the average diameter of highly purified PDIA1, PDIA3, PDIA4, PDIA10, and PDIA15, a Ca2+ concentration-dependent increase in average diameter was observed for PDIA6.” Lee, page 8. As such, while PDIA6 forms droplets, other PDI family proteins do not. For example, Galligan, Fig. 1, shows that PDIA3 and PDIA4 have at least two thioredoxin-like domains but nevertheless do not form droplets, although PDIA4 has a calcium-binding domain. Further, the presence or non-presence of a linker as recited in claims 3 and 7 would not be recognized as sufficient structure to product droplets and/or to even form dimers. Even if a protein is known to form dimers, the same is not sufficient to produce droplets since, Lee, abstract, discusses that PDIA1 can form multimers.
Further, the specification, Fig. 12 (page 6) describes “Flexibility between thioredoxin-like domains is relatively high. In addition, a dimer is formed in a solution. The upper part of Fig. 13 reveals from a crystal structure that dimer formation of P5 uses as a driving force a leucine zipper motif positioned in the 4th a-helix in an aO domain at the beginning.” Okamura, Highlights (first page), states that “P5 [PDAI6] dimerizes via a unique leucine-valine adhesive motif in the first Trx-like domain.” Dimerization is described by the specification (see para. [0054]) as the first step to forming droplets along with “flexibility was rich between thioredoxin-like domain.” Although the specification describes a dimer formed by a leucine zipper and a particular flexibility between domains are critical features for producing droplets, the claims recite a genus of protein forming droplets requiring none of these features. Further, the specification provides do description of any other PDI family protein (P5) having these features, wherein Lee indicate that at least PDIA1, PDIA3, PDIA4, PDIA10, and PDIA15 (only PDIA4 may have a calcium binding region) do not form droplets in presence of calcium ion, nor does the specification provide for any ability of how to produce any artificial protein (i.e. not having a specific identity to protein P5) that would have a leucine zipper and flexible domains that may potentially allow for droplet formation.
“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 . . ., reduction to drawings, or by disclosure of relevant, identifying characteristics.” Here, the description of single protein P5 with specific structure (with specific leucine zipper and flexible domain structure) is not representative of a much broader, structurally diverse genus of droplet-forming proteins not requiring such a specific structure but only requiring a generic thioredoxin-like domain(s) that can lack a leucine zipper nor have domain flexibility between thioredoxin-like domains (in claims 1 and 6 only one thioredoxin-like domain is required).
For these reasons, a ordinarily skilled artisan cannot could not predict the operability in the claims (i.e. form droplets) of any species other than the one disclosed (P5/PDIA6) including any other artificial or PDI family protein that may be reasonably be predicted to be functional within the claims. For these reasons, the specification does not provide an adequate written description of a genus of thioredoxin-like domain proteins capable of forming droplets as recited in the claims.
Further regarding claims 5 and 9, claims 5 and 9 recite that the PDI family protein is P5; however, claims 5 and 9 do not require embodiments of the claims to not be an artificial protein as recited. That is, claims 5 and 9 are understood as reciting “a PDI family protein that is P5 and/or an artificial protein,” since claims 5 and 9 no not state that the protein of claim 1 or 6 is P5. It is noted the rejection of claims 5 and 9 may be obviated by reciting “wherein the protein is P5.”
Claim Rejections - 35 USC § 102
In the event the determination of the status of the application as subject to AIA 35 U.S.C. 102 and 103 (or as subject to pre-AIA 35 U.S.C. 102 and 103) is incorrect, any correction of the statutory basis (i.e., changing from AIA to pre-AIA ) for the rejection will not be considered a new ground of rejection if the prior art relied upon, and the rationale supporting the rejection, would be the same under either status.
The following is a quotation of the appropriate paragraphs of 35 U.S.C. 102 that form the basis for the rejections under this section made in this Office action:
A person shall be entitled to a patent unless –
(a)(1) the claimed invention was patented, described in a printed publication, or in public use, on sale, or otherwise available to the public before the effective filing date of the claimed invention.
Claim(s) 1 and 3-5 is/are rejected under 35 U.S.C. 102(a)(1) as being anticipated by Masters (HeLa cells 50 years on, Nature Reviews 2, 2002, 315-19) as evidenced by Hiller et al. (A functional chaperone condensate in the endoplasmic reticulum, Research Square, 2024, doi.org/10.21203/rs.3.rs-4796355/v1) and Uniprot, Accession No. Q15084, 2019, www.uniprot.org.
Masters describes the existence of the well-known HeLa cell line and Hiller describes a study performed on HeLa cells including their physiology.
Hiller, abstract, disclose:
One third of eukaryotic proteins are processed within the endoplasmic reticulum (ER) to obtain their correct structure. This function is ensured by a network of molecular chaperones that recognizes client proteins and assists their folding. How the ER chaperones organize in a supramolecular manner to exert their cooperativity has, however, remained unclear. Here, we report the discovery of a multi-chaperone condensate in the ER lumen, which is formed around the chaperone PDIA6 during protein folding homeostasis. We resolve the structure of PDIA6 and the mechanism underlying its condensate formation at the atomic and cellular level. We find that the multivalency required for PDIA6 phase separation is created by two specific interfaces. One of these interfaces is regulated by a Ca2+-dependent molecular switch, allowing dynamic adaptations to ER stress. The PDIA6 condensates recruit further chaperones, in particular Hsp70 BiP, J-domain protein ERdj3, disulfide isomerase PDIA1 and Hsp90 Grp94, which are the essential components of the early folding machinery. The chaperone condensates enhance folding of client proteins, which we show exemplarily on proinsulin, and prevent protein misfolding in the ER lumen. The PDIA6-scaffolded chaperone condensates hence provide the functional basis for spatial and temporal coordination of the dynamic ER chaperone network.
“We observed that endogenous PDIA6 localized in the ER in human HeLa cells, as expected (Fig. 1a).Remarkably, however, the endogenous protein was not homogeneously dispersed, but concentrated locally in well-defined clusters. Overexpressed PDIA6 formed clusters of similar shape and localization in living cells, albeit with substantially increased size (Fig. 1a and Extended Data Fig. 1a-c). PDIA6 formed similar clusters also in HEK and U2OS cells (Extended Data Fig. 1 d,e). The PDIA6 clusters were mobile within the ER and underwent fission and fusion events (Fig. 1b and Supplementary Videos 1,2). Their fluorescence recovery after photobleaching (FRAP) occurred on the timescale of minutes, which is common for biological phase separated condensates.” Hiller, page 2.
“To test this mechanistic hypothesis, we reconstituted droplets of purified recombinant PDIA6 protein in vitro. Homeostatic ER was mimicked by high Ca2+ concentration, reducing conditions, physiological pH and a crowding agent. Under these conditions, recombinant PDIA6 reproducibly formed droplets that underwent fusion events and time-dependent growth on the timescale of seconds.” Hiller, page 3.
“HeLa cells were plated onto coverslips 24 hours prior to fixation or stress treatment. At specified timepoints, cells were fi ed in 4% paraformaldehyde, permeabilized with 0.1 % Triton X-100, blocked in PBS containing 5%FBS, and stained with anti-PDIA6.” Hiller, page 14.
The imaging shown in Fig. 1A of Hiller for “Fixed HeLa cells expressing endogenous PDIA6 (left)” is for HeLa cells that are otherwise unmodified. The ”concentrated locally in well-defined clusters” of PDIA6 stated to be a “biological phase separated condensate” is a droplet as recited in the claims. Further, Hiller describes that the ER of HeLa cells contain a significant concentration of calcium ion.
Hiller further evidences that “PDIA6 dimerizes via helix α4 in domain a0.” Hiller page 3. Fig. 2a of Hiller evidences that PDIA6 has two thioredoxin-like domains (a0 and a) connected by a linker. Uniprot Q15084 evidence the sequence for human PDIA6 wherein the linker region being amino acids 288-436 includes glutamine and aspartic acid.
As such, Hiller evidences that HeLa cells that are unmodified and otherwise the same HeLa cells as described by Masters have droplets containing PDIA6 (recited protein P5) contained in the ER thereof. The claims have no limitations regarding 1) the size of droplets, 2) the presence or absence of any additional proteins or compounds outside of the “assembly of a protein” recited, or 3) the droplet only being formed in vitro. As such, droplets containing PDIA6 as found in the ER of HeLa cells as described by Masters read on a droplet as recited in claims 1 and 3-5 including that calcium ion is present in the ER of HeLa cell wherein droplets of PDIA6 are present. “A patentee will not be deemed to have invented species sufficient to constitute the genus by virtue of having disclosed a single species when … the evidence indicates ordinary artisans could not predict the operability in the invention of any species other than the one disclosed.” Again, the specification discloses a single species (P5) and the observation that PDIA4 falls outside the claims evidences that ordinary artisans could not predict the operability in the invention of any species other than the one disclosed.
Claim Rejections - 35 USC § 101
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 and 3-5 are rejected under 35 U.S.C. 101 because the claimed invention is directed to natural phenomenon without significantly more. The claim(s) recite(s) a droplet comprising a PDI family protein that can be P5/PDIA6. This judicial exception is not integrated into a practical application because the claims do not recite any features that can be considered to be an application. The claim(s) does/do not include additional elements that are sufficient to amount to significantly more than the judicial exception because the claims do not recite any elements in addition to a judicial exception.
MPEP 2106(III) directs that claims drawn to 1) a composition of matter (step 1), 2) a law of nature or a natural phenomenon or a product of nature (step 2A) and 3) lacking recitation of additional elements that make the claims directed to significantly more than a judicial exception (step 2B) are ineligible for patenting under 35 U.S.C. 101. See MPEP 2106(III), flow chart. Step 2A into two prongs as set forth in MPEP 2106.04(II)(A).
“If the claim includes a nature-based product that does not exhibit markedly different characteristics from its naturally occurring counterpart in its natural state, then the claim recites a "product of nature" exception, and requires further analysis in Step 2A Prong Two to determine whether the claim as a whole integrates the exception into a practical application.” MPEP 2106.04(c). “It is important to keep in mind that product of nature exceptions include both naturally occurring products and non-naturally occurring products that lack markedly different characteristics from any naturally occurring counterpart.” MPEP 2106.04(b)(II).
“The markedly different characteristics analysis is part of Step 2A Prong One, because the courts use this analysis to identify product of nature exceptions.” MPEP 2106.04(c). “The markedly different characteristics analysis compares the nature-based product limitation to its naturally occurring counterpart in its natural state. Markedly different characteristics can be expressed as the product’s structure, function, and/or other properties, and are evaluated based on what is recited in the claim on a case-by-case basis. If the analysis indicates that a nature-based product limitation does not exhibit markedly different characteristics, then that limitation is a product of nature exception. If the analysis indicates that a nature-based product limitation does have markedly different characteristics, then that limitation is not a product of nature exception.” MPEP 2106.04(c)(II).
Examiners should keep in mind 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.” MPEP 2106.04(c)(I).
Regarding step 1, the rejected claims recite a composition of matter. Regarding Step 2A, prong one, the rejections above are incorporated herein by reference including rejection of claims 1 and 3-5 under 35 U.S.C. 102(a)(1) as being anticipated by Masters (HeLa cells 50 years on, Nature Reviews 2, 2002, 315-19) as evidenced by Hiller et al. (A functional chaperone condensate in the endoplasmic reticulum, Research Square, 2024, doi.org/10.21203/rs.3.rs-4796355/v1). HeLa cells are a naturally-occurring product of nature. As discussed above, such natural-product HeLa cell contain a droplet containing protein P5/PDIA6 having all of the features of claims 1 and 3-5. Since the nature based product limitation of a droplet is naturally occurring, there is no need to perform the markedly different characteristic analysis.
Regarding Step 2A, prong two, there are no limitations in the claims other than the recited natural-product droplet that can be considered to integrate the product of nature into a practical application. Similarly regarding Step 2B, the rejected claims lack recitation of additional elements that make the claims directed to significantly more than a judicial exception since the rejected claims do not recite any additional elements.
The rejected claims are directed towards a judicial exception for these reasons.
Comments regarding prior art
Okumura et al. (Nature Chem. Biol. 15, 2019, 499-509) (see IDS, 12/20/23) with reference to Fig. 1b appears to be discussing PDIA1, which the record does not support undergoes droplet formation.
Okumura et al. (IDS NPL ref. CI) describes isothermal titration calorimetry (ITC) of protein P5 with CaCl2. However, there is no clear evidence from Okumura that any solution with a calcium ion concentration greater than 1 mM was formed or that any phased separated droplet is necessarily formed. Specification describes 3 mM calcium ion for droplet formation of pure P5 protein.
Response to arguments
Applicant argues:
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The claims are not limited to a PDI family protein having a thioredoxin-like domain and a calcium-binding region. The claims recite a genus of any artificial protein not required to be a PDI family protein having a thioredoxin-like domain and a calcium-binding region.
The declaration under 37 CFR 1.132 filed 09/08/2025 is insufficient to overcome the rejection of claims 1 and 3-5 based upon 35 U.S.C. 112(a) as set forth in the last Office action because:
35 U.S.C. 112(a) states “The specification shall contain a written description of the invention.” The Declaration filed 09/08/2025 is not the specification; as such, the specification cannot itself provide a written description of the invention/claims.” While a declaration can provide further information supporting how the disclosure of the specification is sufficient, the present declaration discusses a protein Erp57 that is not discussed in the specification and otherwise the declaration has no discussion of how the disclosure of the as-filed specification provides a sufficient disclosure to satisfy the written description requirement for the genus of proteins recited. The evidence of record shows that:
Some PDI family proteins with a thioredoxin-like domain and a calcium-binding region, such as PDAI6/P5, have ability to form a droplets a recited;
Some PDI family proteins with a thioredoxin-like domain and a calcium-binding region, such as PDIA4 as discussed in the rejection, do not have ability to form a droplet as recited; and
No artificial protein with a thioredoxin-like domain and a calcium-binding region has been described to form a droplet as recited.
The specification taken together with the specification provides for no discussion of how to differentiate between PDI family and artificial proteins with a thioredoxin-like domain and a calcium-binding region that function within the claims and those that do not to recognize possession of the genus recited.
Applicant argues:
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The reasons why a HeLa cell inherently satisfies all the features of claims 1 and 3-5 is set forth above.
The evidence of Hiller discussed above evidences that the lumen of ER in HeLa cells wherein droplets of P5/PDIA6 are found have high Ca2+ concentration. The present claims read on a PDIA6/P5 droplet as found in the ER lumen of naturally-occurring HeLa cells wherein such ER lumen has “high Ca2+ concentration.” The claims do not require a droplet to be in vitro nor to have any structural requirements different from a droplet as found in vivo.
Conclusion
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.
Any inquiry concerning this communication or earlier communications from the examiner should be directed to TODD M EPSTEIN whose telephone number is (571)272-5141. The examiner can normally be reached Mon-Fri 9:00a-5:30p.
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/TODD M EPSTEIN/Primary Examiner, Art Unit 1652